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| pyridoxal |
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| CHEBI:17310 |
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| A pyridinecarbaldehyde that is pyridine-4-carbaldehyde bearing methyl, hydroxy and hydroxymethyl substituents at positions 2, 3 and 5 respectively. The 4-carboxyaldehyde form of vitamin B6, it is converted into pyridoxal phosphate, a coenzyme for the synthesis of amino acids, neurotransmitters, sphingolipids and aminolevulinic acid. |
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This entity has been manually annotated by the ChEBI Team.
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CHEBI:14976, CHEBI:45112, CHEBI:8667, CHEBI:26423
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| eMolecules:1012333, ZINC000000120249 |
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Molfile
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SDF
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more structures >>
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call loadScript javascripts\jsmol\core\package.js call loadScript javascripts\jsmol\core\core.z.js -- required by ClazzNode call loadScript javascripts\jsmol\J\awtjs2d\WebOutputChannel.js Jmol JavaScript applet jmolApplet0_object__191484343612263__ initializing getValue debug = null getValue logLevel = null getValue allowjavascript = null AppletRegistry.checkIn(jmolApplet0_object__191484343612263__) call loadScript javascripts\jsmol\core\corestate.z.js viewerOptions: { "name":"jmolApplet0_object","applet":true,"documentBase":"https://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17310","platform":"J.awtjs2d.Platform","fullName":"jmolApplet0_object__191484343612263__","display":"jmolApplet0_canvas2d","signedApplet":"true","appletReadyCallback":"Jmol._readyCallback","statusListener":"[J.appletjs.Jmol.MyStatusListener object]","codeBase":"https://www.ebi.ac.uk/chebi/javascripts/jsmol/","syncId":"191484343612263","bgcolor":"#000" } (C) 2012 Jmol Development Jmol Version: 13.2.7 $Date: 2013-10-01 11:35:15 -0500 (Tue, 01 Oct 2013) $ java.vendor: j2s java.version: 0.0 os.name: j2s Access: ALL memory: 0.0/0.0 processors available: 1 useCommandThread: false appletId:jmolApplet0_object (signed) starting HoverWatcher_1 getValue emulate = null defaults = "Jmol" getValue boxbgcolor = null getValue bgcolor = #000 backgroundColor = "#000" getValue ANIMFRAMECallback = null getValue APPLETREADYCallback = Jmol._readyCallback APPLETREADYCallback = "Jmol._readyCallback" getValue ATOMMOVEDCallback = null getValue CLICKCallback = null getValue ECHOCallback = null getValue ERRORCallback = null getValue EVALCallback = null getValue HOVERCallback = null getValue LOADSTRUCTCallback = null getValue MEASURECallback = null getValue MESSAGECallback = null getValue MINIMIZATIONCallback = null getValue PICKCallback = null getValue RESIZECallback = null getValue SCRIPTCallback = null getValue SYNCCallback = null getValue STRUCTUREMODIFIEDCallback = null getValue doTranslate = null language=en_US getValue popupMenu = null getValue script = null Jmol applet jmolApplet0_object__191484343612263__ ready call loadScript javascripts\jsmol\core\corescript.z.js call loadScript javascripts\jsmol\J\script\FileLoadThread.js starting QueueThread0_2 script 1 started starting HoverWatcher_3 starting HoverWatcher_4 The Resolver thinks Mol Marvin 03220818273D starting HoverWatcher_5 Time for openFile( Marvin 03220818273D 21 21 0 0 0 0 999 V2000 1.1763 -0.0018 -0.2963 C 0 0 0 0 0 0 0 0 0 5 0 0 -0.3617 -1.8330 -0.5502 N 0 0 0 0 0 0 0 0 0 1 0 0 0.8762 -1.3168 -0.7225 C 0 0 0 0 0 0 0 0 0 6 0 0 0.1386 0.7506 0.3389 C 0 0 0 0 0 0 0 0 0 4 0 0 -1.1496 0.1581 0.4851 C 0 0 0 0 0 0 0 0 0 3 0 0 -1.3862 -1.1598 0.0260 C 0 0 0 0 0 0 0 0 0 2 0 0 2.5585 0.5076 -0.5209 C 0 0 0 0 0 0 0 0 0 0 0 0 2.5381 1.6050 -1.4279 O 0 0 0 0 0 0 0 0 0 0 0 0 -2.6963 -1.8374 0.1386 C 0 0 0 0 0 0 0 0 0 0 0 0 -2.1085 0.7932 1.0073 O 0 0 0 0 0 0 0 0 0 0 0 0 0.3735 2.0433 0.8119 C 0 0 0 0 0 0 0 0 0 0 0 0 -0.2378 2.5658 1.7333 O 0 0 0 0 0 0 0 0 0 0 0 0 1.5728 -1.9160 -1.1700 H 0 0 0 0 0 0 0 0 0 0 0 0 2.9901 0.8308 0.4284 H 0 0 0 0 0 0 0 0 0 0 0 0 3.2476 -0.2308 -0.9395 H 0 0 0 0 0 0 0 0 0 0 0 0 3.4309 2.0036 -1.3728 H 0 0 0 0 0 0 0 0 0 0 0 0 -2.9910 -1.9010 1.1875 H 0 0 0 0 0 0 0 0 0 0 0 0 -2.6878 -2.8511 -0.2674 H 0 0 0 0 0 0 0 0 0 0 0 0 -3.4532 -1.2686 -0.4045 H 0 0 0 0 0 0 0 0 0 0 0 0 -2.9103 0.4413 1.0924 H 0 0 0 0 0 0 0 0 0 0 0 0 1.0799 2.6169 0.4225 H 0 0 0 0 0 0 0 0 0 0 0 0 3 2 4 0 0 0 0 1 3 4 0 0 0 0 4 1 4 0 0 0 0 5 4 4 0 0 0 0 6 5 4 0 0 0 0 6 2 4 0 0 0 0 7 1 1 0 0 0 0 8 7 1 0 0 0 0 9 6 1 0 0 0 0 10 5 1 0 0 0 0 11 4 1 0 0 0 0 12 11 2 0 0 0 0 3 13 1 0 0 0 0 7 14 1 0 0 0 0 7 15 1 0 0 0 0 8 16 1 0 0 0 0 9 17 1 0 0 0 0 9 18 1 0 0 0 0 9 19 1 0 0 0 0 10 20 1 0 0 0 0 11 21 1 0 0 0 0 M END): 17 ms reading 21 atoms ModelSet: haveSymmetry:false haveUnitcells:false haveFractionalCoord:false 1 model in this collection. Use getProperty "modelInfo" or getProperty "auxiliaryInfo" to inspect them. Default Van der Waals type for model set to Babel 21 atoms created ModelSet: not autobonding; use forceAutobond=true to force automatic bond creation Script completed Jmol script terminated
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| Pyridoxal (PL) is one form of vitamin B6.
Some medically relevant bacteria, such as those in the genera Granulicatella and Abiotrophia, require pyridoxal for growth. This nutritional requirement can lead to the culture phenomenon of satellite growth. In in vitro culture, these pyridoxal-dependent bacteria may only grow in areas surrounding colonies of bacteria from other genera ("satellitism") that are capable of producing pyridoxal.
Pyridoxal is involved in what is believed to be the most ancient reaction of aerobic metabolism on Earth, about 2.9 billion years ago, a forerunner of the Great Oxidation Event.
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Read full article at Wikipedia
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| InChI=1S/C8H9NO3/c1-5-8(12)7(4-11)6(3-10)2-9-5/h2,4,10,12H,3H2,1H3 |
| RADKZDMFGJYCBB-UHFFFAOYSA-N |
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Mus musculus
(NCBI:txid10090)
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Source: BioModels - MODEL1507180067
See:
PubMed
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Mus musculus
(NCBI:txid10090)
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From MetaboLights
of strain
C57bl/6 mouse (NCIT:C14424)
See:
MetaboLights Study
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Saccharomyces cerevisiae
(NCBI:txid4932)
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Source: yeast.sf.net
See:
PubMed
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Escherichia coli
(NCBI:txid562)
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See:
PubMed
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Trypanosoma brucei
(NCBI:txid5691)
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From MetaboLights
See:
MetaboLights Study
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Daphnia pulex
(NCBI:txid6669)
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From MetaboLights
See:
MetaboLights Study
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Homo sapiens
(NCBI:txid9606)
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See:
DOI
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Homo sapiens
(NCBI:txid9606)
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Found in
blood
(UBERON:0000178).
See:
Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
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Homo sapiens
(NCBI:txid9606)
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From MetaboLights
See:
MetaboLights Study
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mouse metabolite
Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus).
human metabolite
Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens).
Saccharomyces cerevisiae metabolite
Any fungal metabolite produced during a metabolic reaction in Baker's yeast (Saccharomyces cerevisiae ).
Escherichia coli metabolite
Any bacterial metabolite produced during a metabolic reaction in Escherichia coli.
cofactor
An organic molecule or ion (usually a metal ion) that is required by an enzyme for its activity. It may be attached either loosely (coenzyme) or tightly (prosthetic group).
water-soluble vitamin (role)
Any vitamin that dissolves in water and readily absorbed into tissues for immediate use. Unlike the fat-soluble vitamins, they are not stored in the body and need to be replenished regularly in the diet and will rarely accumulate to toxic levels since they are quickly excreted from the body via urine.
(via B vitamin )
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nutraceutical
A product in capsule, tablet or liquid form that provide essential nutrients, such as a vitamin, an essential mineral, a protein, an herb, or similar nutritional substance.
(via B vitamin )
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View more via ChEBI Ontology
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3-hydroxy-5-(hydroxymethyl)-2-methylpyridine-4-carbaldehyde
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3-HYDROXY-5-(HYDROXYMETHYL)-2-METHYLISONICOTINALDEHYDE
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PDBeChem
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Pyridoxal
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KEGG COMPOUND
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pyridoxal
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UniProt
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pyridoxaldehyde
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ChemIDplus
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1021
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ChemSpider
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4134
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DrugCentral
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C00007509
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KNApSAcK
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C00250
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KEGG COMPOUND
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DB00147
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DrugBank
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HMDB0001545
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HMDB
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PXL
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PDBeChem
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Pyridoxal
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Wikipedia
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PYRIDOXAL
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MetaCyc
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| View more database links |
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218674
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Gmelin Registry Number
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Gmelin
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383768
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Reaxys Registry Number
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Reaxys
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66-72-8
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CAS Registry Number
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ChemIDplus
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Johnston EA, Lloyd SB, Granger DL (2020)
Properties of a fungicidal product formed from a reaction between L-cystine and pyridoxal.
Medical mycology 58, 919-927 [PubMed:31915818]
[show Abstract]
Previously we found that three components of a commonly used mammalian cell culture medium incorporated into agar killed cryptococci (Granger and Call 2019). The components were L-cystine, iron [Fe(III)], and pyridoxal (CIP). We now report on a buffered solution at neutral pH of the three components, which was highly fungicidal without agar. We showed that CIP fungicidal activity, identical to the findings with cell culture medium, was inactivated by visible light and was unstable with storage in the dark. Congeners replacing either pyridoxal or L-cystine in CIP revealed structural requirements for fungicidal activity. Replacing pyridoxal in CIP with 2-hydroxy-5-nitrobenzaldehyde produced a solution that was equally fungicidal and maintained fungicidal activity upon storage in the dark for up to 50 days. We employed methods for excluding iron from CIP and found that fungicidal activity was not affected. Upon mixing L-cystine and pyridoxal in buffer at pH 7.0, diode array spectroscopy revealed a red-shift of absorbance maximum from 391 nm to 398 nm. Our findings point to Schiff base reaction between the pyridoxal aldehyde group of C1 with the alpha amino group(s) of cystine to yield a fungicidal compound. Light at wave length approximately 400 nm inactivates this complex accompanied by bleaching of the pyridine ring of pyridoxal. Our findings may be useful for design of a class of fungicidal compounds formed through Schiff base reaction of disulfide compounds with aromatic ring-bearing aldehydes. | Chawla J, Kvarnberg D (2014)
Hydrosoluble vitamins.
Handbook of clinical neurology 120, 891-914 [PubMed:24365359]
[show Abstract]
The hydrosoluble vitamins are a group of organic substances that are required by humans in small amounts to prevent disorders of metabolism. Significant progress has been made in our understanding of the biochemical, physiologic and nutritional aspects of the water-soluble vitamins. Deficiency of these particular vitamins, most commonly due to inadequate nutrition, can result in disorders of the nervous system. Many of these disorders have been successfully prevented in developed countries; however, they are still common in developing countries. Of the hydrosoluble vitamins, the nervous system depends the most on vitamins B and C (ascorbic acid) for proper functioning. The B group vitamins include thiamin (vitamin B1), riboflavin (vitamin B2), niacin or niacinamide (vitamin B3), pantothenic acid (vitamin B5), pyridoxine or pyridoxal (vitamin B6) and cobalamin (vitamin B12). Clinical findings depend upon the deficiency of the underlying vitamin; generally, deficiency symptoms are seen from a combination rather than an isolated vitamin deficiency. True hereditary metabolic disorders and serious deficiency-associated diseases are rare and in general limited to particular geographic regions and high-risk groups. Their recognition is truly important as that determines the appropriate therapeutic management. The general availability of vitamins to practically everyone and several national health programs have saved many lives and prevented complications. However, there has been some apprehension for several decades about how harmless generous dosages of these vitamins are. Overt overdosages can cause vitamin toxicity affecting various body systems including the nervous system. Systemically, vitamin toxicity is associated with nonspecific symptoms, such as nausea, vomiting, diarrhea, and skin rash which are common with any acute or chronic vitamin overdose. At a national level, recommended daily allowances for vitamins become policy statements. Nutrition policy has far reaching implications in the food industry, in agriculture, and in food provision programs. Overall, water-soluble vitamins are complex molecular structures and even today, many areas of vitamin biochemistry still need to be explored. Many readers might be of the opinion that the classic forms of nutritional deficiency diseases have faded into the background of interesting history. This has caused their diverse symptoms to be neglected by most modern physicians since vitamin enrichment of many foods automatically erases them from their consideration in differential diagnosis. Vitamin B12 and folic acid deficiencies are discussed in other chapters. | Nanri A, Pham NM, Kurotani K, Kume A, Kuwahara K, Sato M, Hayabuchi H, Mizoue T (2013)
Serum pyridoxal concentrations and depressive symptoms among Japanese adults: results from a prospective study.
European journal of clinical nutrition 67, 1060-1065 [PubMed:23801094]
[show Abstract]
Background/objectivesVitamin B6 is suggested to have a protective role against depression. However, the association between vitamin B6 intake and depression remains inconclusive, and few studies have examined the relationship between circulating vitamin B6 concentrations and depressive symptoms. Here, we investigated the cross-sectional and prospective associations between serum pyridoxal concentrations and depressive symptoms among Japanese workers.Subjects/methodsParticipants were 422 municipal employees (aged 21-67 years) who participated in a baseline survey in 2006 for cross-sectional analysis, and 210 subjects without depressive symptoms at baseline (2006) who completed both baseline and follow-up (2009) surveys for prospective analysis. Depressive symptoms were assessed using the Center for Epidemiologic Studies Depression (CES-D) scale. Logistic regression analysis was used to estimate the odds ratio of depressive symptoms (CES-D scale of ≥ 19) according to tertile of serum pyridoxal with adjustment for potential confounding variables.ResultsIn the cross-sectional analysis, serum pyridoxal concentrations were significantly associated with a decreased prevalence of depressive symptoms (P for trend=0.03); the multivariable-adjusted odds ratio of depressive symptoms for the highest tertile of pyridoxal was 0.54 (95% confidence interval 0.30-0.96) compared with the lowest tertile. In longitudinal analyses, higher serum pyridoxal concentrations at baseline were associated with a trend toward reduced depressive symptoms after 3 years; the multivariable-adjusted odds ratio of depressive symptoms for the highest versus the lowest tertile of pyridoxal concentration was 0.55 (95% confidence interval 0.13-2.32).ConclusionsA higher vitamin B6 status may be associated with a decreased risk of depressive symptoms in Japanese. | Roux A, Xu Y, Heilier JF, Olivier MF, Ezan E, Tabet JC, Junot C (2012)
Annotation of the human adult urinary metabolome and metabolite identification using ultra high performance liquid chromatography coupled to a linear quadrupole ion trap-Orbitrap mass spectrometer.
Analytical chemistry 84, 6429-6437 [PubMed:22770225]
[show Abstract]
Metabolic profiles of biofluids obtained by atmospheric pressure ionization mass spectrometry-based technologies contain hundreds to thousands of features, most of them remaining unknown or at least not characterized in analytical systems. We report here on the annotation of the human adult urinary metabolome and metabolite identification from electrospray ionization mass spectrometry (ESI-MS)-based metabolomics data sets. Features of biological interest were first of all annotated using the ESI-MS database of the laboratory. They were also grouped, thanks to software tools, and annotated using public databases. Metabolite identification was achieved using two complementary approaches: (i) formal identification by matching chromatographic retention times, mass spectra, and also product ion spectra (if required) of metabolites to be characterized in biological data sets to those of reference compounds and (ii) putative identification from biological data thanks to MS/MS experiments for metabolites not available in our chemical library. By these means, 384 metabolites corresponding to 1484 annotated features (659 in negative ion mode and 825 in positive ion mode) were characterized in human urine samples. Of these metabolites, 192 and 66 were formally and putatively identified, respectively, and 54 are reported in human urine for the first time. These lists of features could be used by other laboratories to annotate their ESI-MS metabolomics data sets. | Kind S, Jeong WK, Schröder H, Wittmann C (2010)
Systems-wide metabolic pathway engineering in Corynebacterium glutamicum for bio-based production of diaminopentane.
Metabolic engineering 12, 341-351 [PubMed:20381632]
[show Abstract]
In the present work the Gram-positive bacterium Corynebacterium glutamicum was engineered into an efficient, tailor-made production strain for diaminopentane (cadaverine), a highly attractive building block for bio-based polyamides. The engineering comprised expression of lysine decarboxylase (ldcC) from Escherichia coli, catalyzing the conversion of lysine into diaminopentane, and systems-wide metabolic engineering of central supporting pathways. Substantially re-designing the metabolism yielded superior strains with desirable properties such as (i) the release from unwanted feedback regulation at the level of aspartokinase and pyruvate carboxylase by introducing the point mutations lysC311 and pycA458, (ii) an optimized supply of the key precursor oxaloacetate by amplifying the anaplerotic enzyme, pyruvate carboxylase, and deleting phosphoenolpyruvate carboxykinase which otherwise removes oxaloacetate, (iii) enhanced biosynthetic flux via combined amplification of aspartokinase, dihydrodipicolinate reductase, diaminopimelate dehydrogenase and diaminopimelate decarboxylase, and (iv) attenuated flux into the threonine pathway competing with production by the leaky mutation hom59 in the homoserine dehydrogenase gene. Lysine decarboxylase proved to be a bottleneck for efficient production, since its in vitro activity and in vivo flux were closely correlated. To achieve an optimal strain having only stable genomic modifications, the combination of the strong constitutive C. glutamicum tuf promoter and optimized codon usage allowed efficient genome-based ldcC expression and resulted in a high diaminopentane yield of 200 mmol mol(-1). By supplementing the medium with 1 mgL(-1) pyridoxal, the cofactor of lysine decarboxylase, the yield was increased to 300 mmol mol(-1). In the production strain obtained, lysine secretion was almost completely abolished. Metabolic analysis, however, revealed substantial formation of an as yet unknown by-product. It was identified as an acetylated variant, N-acetyl-diaminopentane, which reached levels of more than 25% of that of the desired product. | van der Werf MJ, Overkamp KM, Muilwijk B, Coulier L, Hankemeier T (2007)
Microbial metabolomics: toward a platform with full metabolome coverage.
Analytical biochemistry 370, 17-25 [PubMed:17765195]
[show Abstract]
Achieving metabolome data with satisfactory coverage is a formidable challenge in metabolomics because metabolites are a chemically highly diverse group of compounds. Here we present a strategy for the development of an advanced analytical platform that allows the comprehensive analysis of microbial metabolomes. Our approach started with in silico metabolome information from three microorganisms-Escherichia coli, Bacillus subtilis, and Saccharomyces cerevisiae-and resulted in a list of 905 different metabolites. Subsequently, these metabolites were classified based on their physicochemical properties, followed by the development of complementary gas chromatography-mass spectrometry and liquid chromatography-mass spectrometry methods, each of which analyzes different metabolite classes. This metabolomics platform, consisting of six different analytical methods, was applied for the analysis of the metabolites for which commercial standards could be purchased (399 compounds). Of these 399 metabolites, 380 could be analyzed with the platform. To demonstrate the potential of this metabolomics platform, we report on its application to the analysis of the metabolome composition of mid-logarithmic E. coli cells grown on a mineral salts medium using glucose as the carbon source. Of the 431 peaks detected, 235 (=176 unique metabolites) could be identified. These include 61 metabolites that were not previously identified or annotated in existing E. coli databases. | Rajamohan F, Nelms L, Joslin DL, Lu B, Reagan WJ, Lawton M (2006)
cDNA cloning, expression, purification, distribution, and characterization of biologically active canine alanine aminotransferase-1.
Protein expression and purification 48, 81-89 [PubMed:16495081]
[show Abstract]
Alanine aminotransferase (ALT) is a pyridoxal enzyme found mainly in the liver and kidney, but also in small amounts in the heart, muscle, fat, and brain. Serum aminotransferase activities have been used broadly as surrogate markers for tissue injury and disease in human and veterinary clinical settings and in safety assessment of chemicals and pharmaceuticals. Because of its relative abundance in liver, increased serum ALT activity is generally considered indicative of liver damage. Two ALT isoenzymes, ALT1 and ALT2, are known and have been cloned and sequenced from human, rat, and mouse. In this study, we have cloned the complementary DNA encoding the canine orthologue of ALT1 (cALT1). The complete cDNA sequence comprised 1852 bases and contained a 1485-base open reading frame, which encodes a polypeptide of 494 amino acid residues. Canine ALT1 shares 87.7, 87.2, and 87.0% amino acid identity to its human, mouse, and rat orthologues, respectively. The cDNA was expressed in Escherichia coli, with a N-terminal His (6x) tag, and the recombinant enzyme was purified using immobilized metal-affinity chromatography. The final yield of the purified recombinant cALT1 was greater than 5mg/L culture. The alanine transaminase activity of purified cALT1 was 229.81U/mg protein, which is approximately 38-fold higher than that of total soluble recombinant E. coli cell lysate, confirming that the enzyme is a functional ALT. Evaluation of various canine tissues by RT-PCR revealed that the level of ALT1 expression is in the order of: heart>liver>fat approximately brain approximately gastrocnemius>kidney. The purified cALT1 will be helpful to develop isoenzyme-specific anti-bodies, which could further improve the diagnostic resolution of current ALT assays in drug safety studies. | Yiakouvaki A, Savović J, Al-Qenaei A, Dowden J, Pourzand C (2006)
Caged-iron chelators a novel approach towards protecting skin cells against UVA-induced necrotic cell death.
The Journal of investigative dermatology 126, 2287-2295 [PubMed:16710308]
[show Abstract]
Exposure of human skin cells to solar UVA radiation leads to an immediate dose-dependent increase of labile iron that subsequently promotes oxidative damage and necrotic cell death. Strong iron chelators have been shown to suppress cell damage and necrotic cell death by moderating the amount of labile iron pool (LIP), but chronic use would cause severe side effects owing to systemic iron depletion. Prodrugs that become activated in skin cells at physiologically relevant doses of UVA, such as "caged-iron chelators", may provide dose- and context-dependent release. Herein, we describe prototypical iron chelator compounds derived from salicylaldehyde isonicotinoyl hydrazone and pyridoxal isonicotinoyl hydrazone and demonstrate that the intracellular LIP and subsequent necrotic cell death of human skin fibroblasts is significantly decreased upon exposure to a combination of the prototypical compounds and physiologically relevant UVA doses. Iron regulatory protein bandshift and calcein fluorescence assays reveal decreased intracellular LIP following irradiation of caged-chelator-treated cells, but not in control samples where either UVA light, or caged-chelator is absent. Furthermore, flow cytometry shows that these compounds have no significant toxicity in the skin fibroblasts. This novel light-activated prodrug strategy may therefore be used to protect skin cells against the deleterious effects of sunlight. | Huang YC, Lan PH, Cheng CH, Lee BJ, Kan MN (2002)
Vitamin B6 intakes and status of mechanically ventilated critically ill patients in Taiwan.
European journal of clinical nutrition 56, 387-392 [PubMed:12001008]
[show Abstract]
ObjectiveTo assess vitamin B6 intake and status of critically ill patients. The relationship between vitamin B6 status indicators and the severity of illness and outcome in these patients was also examined.DesignProspective clinical study.SettingThe study was performed at the Taichung Veteran General Hospital, in the central part of Taiwan.SubjectsNinety-four patients in the intensive care unit (ICU) entered the study and 46 patients successfully completed this study.InterventionsNo intervention.Main outcome measuresVitamin B6 intake was recorded for 14 days. Vitamin B6 status was assessed by direct measures (plasma pyridoxal 5'-phosphate (PLP), pyridoxal (PL), and urinary 4-pyridoxic acid (4-PA)) and indirect measures (erythrocyte alanine (EALT-AC) and aspartate (EAST-AC) aminotransaminase activity coefficient). The severity of illness (APACHE II score), the length of ventilation dependency, and the length of ICU and hospital stay were recorded.ResultsPatients had an adequate mean vitamin B6 intake (16.26+/-19.39 mg) during the 14 day study. Mean vitamin B6 intake was significantly higher on day 14 than on day 1 (P<0.001). However, plasma PLP and PL concentrations significantly decreased at the 14th day after admission (P<0.05). Erythrocyte alanine aminotransaminase activity coefficient and EAST-AC did not change significantly. Urinary 4-PA significantly increased at the 14th day (P<0.001). No significant relationships were found between APACHE II scores and clinical outcomes (the length of ICU and hospital stay, the length of ventilation dependency) of patients, vitamin B6 intake or status indicators.ConclusionsCritically ill patients received nutritional support in the ICU, and had sufficient mean vitamin B6 intake and adequate vitamin B6 status. Therefore, the severity of illness and the results should not be affected by vitamin B6 status. However, we have noted that plasma PLP and PL concentrations significantly decreased while vitamin B6 intake significantly increased on day 14. Critical clinical conditions and complex metabolism in the critically ill may account for the reduction of plasma PLP and PL. Since vitamin B6 deficiency causes profound effects on immune system function, dietary or supplemented vitamin B6 intake is suggested for hospitalized patients. | Fonda ML (1993)
Vitamin B6 metabolism and binding to proteins in the blood of alcoholic and nonalcoholic men.
Alcoholism, clinical and experimental research 17, 1171-1178 [PubMed:8116826]
[show Abstract]
Blood obtained from nonalcoholic and alcoholic subjects was incubated with 100 nM [3H]pyridoxine to study its uptake and metabolism by erythrocytes and the binding of vitamin B6 metabolites to proteins in plasma and erythrocytes. Erythrocytes of the alcoholics accumulated tritium faster than those of the controls; however, they contained the same total amount of tritiated compounds by 15 min. After incubation for 30 min, the erythrocytes had converted most of the pyridoxine to pyridoxal phosphate and pyridoxal. Pyridoxal-P remained in the erythrocytes, and approximately 40% of the pyridoxal diffused into the plasma. [3H]Pyridoxal and [3H]pyridoxal-P levels in the erythrocytes and plasma of the alcoholics were similar to those in the controls. However, dialyzed hemolysates of the alcoholics had more [3H]pyridoxal and a lower percentage of [3H]pyridoxal-P than those of the controls. The total concentration of plasma pyridoxal-P was lower in the alcoholics than in the controls and did not change upon incubation of whole blood with pyridoxine or upon dialysis. The erythrocytes of the alcoholics and controls had similar concentrations of pyridoxal-P that increased 2.5-fold upon incubation of whole blood with pyridoxine for 30 min and returned to the initial concentrations upon dialysis. The amount of [3H]pyridoxal and [3H]pyridoxal-P bound to protein was assessed by treating hemolysate and plasma samples with borohydride before dialysis. More 3H was bound to protein in the erythrocytes than in the plasma. The amount of protein-bound 3H in the erythrocytes of the alcoholics was lower than that of the controls, whereas the amount of protein-bound 3H in plasma was similar in both groups.(ABSTRACT TRUNCATED AT 250 WORDS) | Schenker S, Johnson RF, Mahuren JD, Henderson GI, Coburn SP (1992)
Human placental vitamin B6 (pyridoxal) transport: normal characteristics and effects of ethanol.
The American journal of physiology 262, R966-74 [PubMed:1621875]
[show Abstract]
The aims of this study were to define normal human placental transport of pyridoxal, an important form of vitamin B6 in pregnancy, and to determine the effect of short-term alcohol on this process. Our studies used the isolated single cotyledon from the term placenta. Pyridoxal crossed the human placenta readily in both directions, but the transfer was a little less than half that of antipyrine and was significantly greater in the direction of the fetus. Pyridoxine appeared to have a similar clearance from the maternal compartment as pyridoxal, but transport of intact pyridoxal 5'-phosphate was much smaller. There was no saturable transfer of pyridoxal, and it was not transferred from the maternal to fetal compartments against a concentration gradient. Placental concentration of pyridoxal exceeded both maternal and fetal perfusate pyridoxal concentrations, but this concentration was equal for both perfusion directions. These composite data are most suggestive of passive transport of pyridoxal across the placenta, binding of the vitamin in the placenta as an explanation for its concentration there, and greater phosphorylation of pyridoxal in the placenta when the compound is transferred in the fetal direction, possibly displacing pyridoxal from its binding sites and permitting its greater release into the fetal compartment. Alcohol, 400-250 mg/dl over 2.5 h, inhibited the transport of pyridoxal from the maternal to fetal compartments by approximately 42% (P = 0.03) and resulted in a lower transfer of pyridoxal 5'-phosphate into the fetal perfusate (P = 0.02). | el-Habet AE, el-Sewedy SM, el-Sharaky A, Gaafar NK, Abdel-Rafee A, Hamoud F (1987)
Biochemical studies on bilharzial and nonbilharzial hyperoxaluria: effect of pyridoxine and allopurinol treatment.
Biochemical medicine and metabolic biology 38, 1-8 [PubMed:3663392]
[show Abstract]
The urinary excretion levels of oxalic acid, calcium, kynurenic, and xanthurenic acids and serum pyridoxal and pyridoxal phosphate concentrations were determined for nonbilharzial and bilharzial hyperoxaluric patients with or without urinary stones. The effects of pyridoxine and allopurinol treatment were also studied. The different groups studied showed elevated levels of urinary oxalic acid, calcium, kynurenic, and xanthurenic acids as well as decreases in serum pyridoxal and pyridoxal phosphate concentrations. These data indicate that nonbilharzial hyperoxaluric patients suffer from dietary B6 deficiency, whereas bilharzial hyperoxaluric patients may suffer from impaired pyridoxine phosphokinase activity. Pyridoxine supplementation is recommended for the treatment of nonbilharzial hyperoxaluric patients. Allopurinol may be the proper drug in the treatment of oxaluria and stone formation or of bilharzial patients. | Linares P, Luque de Castro MD, Valcarcel M (1985)
Simultaneous determination of pyridoxal and pyridoxal 5-phosphate in human serum by flow injection analysis.
Analytical chemistry 57, 2101-2106 [PubMed:4051187] | Kark JA, Tarassoff PG, Bongiovanni R (1983)
Pyridoxal phosphate as an antisickling agent in vitro.
The Journal of clinical investigation 71, 1224-1229 [PubMed:6853710]
[show Abstract]
Although pyridoxal phosphate is known to inhibit gelation of purified hemoglobin S, antisickling activity has never been demonstrated for intact erythrocytes. We incubated washed erythrocytes at 37 degrees C either in buffer alone, or with added pyridoxal phosphate or pyridoxal, washed these cells, suspended them in untreated buffer, and compared the percent modified hemoglobin, the oxygen affinity, and the extent of sickling under hypoxia. Pyridoxal phosphate modified intracellular hemoglobin more slowly than pyridoxal. Pyridoxal phosphate lowered the oxygen affinity of normal cells, but had no effect on oxygen binding by sickle cells. Pyridoxal increased the oxygen affinity of normal and sickle erythrocytes equally. Pyridoxal phosphate significantly inhibited sickling of sickle or sickle trait erythrocytes (P less than 0.001). Inhibition of sickling by pyridoxal phosphate was largely independent of oxygen binding; whereas inhibition of sickling by pyridoxal was almost entirely dependent on increased oxygen binding. Although pyridoxal phosphate and pyridoxal both inhibit sickling by modification of hemoglobin S, they differ in the kinetics of whole cell modification, the effect on oxygen affinity of intact cells, and the mechanism of action of the antisickling activity. | Kark JA, Bongiovanni R, Hicks CU, Tarassoff PG, Hannah JS, Yoshida GY (1982)
Modification of intracellular hemoglobin with pyridoxal and pyridoxal 5'-phosphate.
Blood cells 8, 299-314 [PubMed:7159754]
[show Abstract]
The aldehyde forms of vitamin B6, pyridoxal and pyridoxal 5'-phosphate (PLP) have aroused interest as antisickling agents because of their ability to modify hemoglobin (Hb) and their low toxicity. To study their rate of formation and stability inside red cells, pyridoxal-Hb and PLP-Hb were measured in lysates from treated normal and sickle erythrocytes using isocratic high pressure liquid chromatography on Bio-Rex 70. The validity of this assay was confirmed by isoelectric focussing, fluorescence scans of reduced globin, and treatment of cells with pyridoxal 14C. Optimal conditions were described for treatment of whole blood with pyridoxal and washed erythrocytes with PLP. Although there was competition between 2,3-DPG and PLP, but not pyridoxal, for binding to Hb, depletion of 2,3-DPG prior to treatment was unnecessary. No special requirements were noted for the anticoagulants or buffers used. Sickle erythrocytes formed PLP-Hb more rapidly than normal erythrocytes, but pyridoxal-Hb appeared at the same rate in both types of erythrocytes. During incubation of treated erythrocytes in untreated plasma, the stability of pyridoxal-Hb varied inversely with the hematocrit, but PLP-Hb was stable at all hematocrits tested. The absence of hemolysis during a 4 day incubation of treated normal red cells implies that treatment with pyridoxal or PLP did not severely impair red cell metabolism. | Mehansho H, Henderson LM (1980)
Transport and accumulation of pyridoxine and pyridoxal by erythrocytes.
The Journal of biological chemistry 255, 11901-11907 [PubMed:7440576]
[show Abstract]
The mechanisms of transport of pyridoxine (PN) and pyridoxal (PL) into erythrocytes have been investigated using the rapid-mixing technique with 3H-labeled substrates. Erythrocytes take up PN by passive diffusion as indicated by the fact that the initial influx process is nonsaturable and is not affected by pyridoxamine (PM), PL, or 4'-deoxypyridoxine. Transport of PL has the same characteristics. The transport of both PN and PL is temperature-dependent with a sharp increase in rate of uptake between 15 and 20 degrees C. The accumulation of 3H from [3H]PN against a concentration gradient was the result of phosphorylation. When the phosphorylation of [3H]PN was reduced by adding 160 microM unlabeled PN, PL, PM, or 4'-deoxypyridoxine, the cell:medium concentration ratio for 3H did not exceed unity. In contrast, with [3H]PL, 1.6 mM concentrations of these unlabeled substrates did not reduce the cell:medium concentration ratio of 3H. This kinase-in-dependent accumulation of PL against a concentration gradient, in the absence of evidence for mediated transport, suggested that binding by an intracellular protein was responsible. Evidence for such binding was obtained from Sephadex G-75 gel filtration, ultrafiltration, and equilibrium dialysis studies with [3H]PL. Reduction of the PL x protein complex with NaBH4 resulted in a stable pyridoxyl protein. The high binding capacity and the molecular weight by gel filtration suggest that hemoglobin is the binding protein. | Bossé TR, Donald EA (1979)
The vitamin B6 requirement in oral contraceptive users. I. Assessment by pyridoxal level and transferase activity in erythrocytes.
The American journal of clinical nutrition 32, 1015-1023 [PubMed:433818]
[show Abstract]
Eight college-age women using estrogen-containing oral contraceptives (OC) were fed a low vitamin B6 diet (0.36 mg/day) for 42 days. During the first 10 days (adjustment period) the diet was supplemented with 1.7 mg pyridoxine hydrochloride bringing the total intake to 2.06 mg/day. Following depletion, repletion was done in three consecutive steps: intakes of 0.96, 1.56, and 5.06 mg were consumed for 8, 9, and 7 days, respectively. Continuous 24-hr urine collections were made throughout the study and fasting blood samples were drawn periodically. Vitamin B6 nutriture was assessed by erythrocyte pyridoxal level, erythrocyte alanine aminotransferase and erythrocyte aspartic aminotransferase activity; and stimulation of these enzyme systems with pyridoxal phosphate. Results were compared with data obtained from non-OC users who consumed a similar diet. The data obtained suggest that 0.96 mg vitamin B6 was not adequate to meet the needs of OC users. Predepletion levels had been reached in almost all subjects at an intake of 1.5 mg/day. Assessed by the parameters studied, an intake between 1.5 and 5.0 mg/day of vitamin B6 was adequate to meet the needs of OC users; this compares with 1.5 mg/day previously suggested for the nonuser. | Brenner A, Wapnir RA (1978)
A pyridoxine-dependent behavioral disorder unmasked by isoniazid.
American journal of diseases of children (1960) 132, 773-776 [PubMed:150790]
[show Abstract]
A 3-year-old girl had behavioral deterioration, with hyperkinesis, irritability, and sleeping difficulties after the therapeutic administration of isoniazid. The administration of pharmacologic doses of pyridoxine hydrochloride led to a disappearance of symptoms. After discontinuing isoniazid therapy a similar pattern of behavior was noted that was controlled by pyridoxine. A placebo had no effect, but niacinamide was as effective as pyridoxine. Periodic withdrawal of pyridoxine was associated with return of the hyperkinesis. The level of pyridoxal in the blood was normal during the periods of relapse. Metabolic studies suggested a block in the kynurenine pathway of tryptophan metabolism. The patient has been followed for six years and has required pharmacologic doses of pyridoxine to control her behavior. |
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