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| 4-Aminobenzoic acid (also known as para-aminobenzoic acid or PABA because the two functional groups are attached to the benzene ring across from one another in the para position) is an organic compound with the formula H2NC6H4CO2H. PABA is a white crystalline solid, although commercial samples can appear gray. It is slightly soluble in water. It consists of a benzene ring substituted with amino and carboxyl groups. The compound occurs extensively in the natural world.
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Read full article at Wikipedia
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| InChI=1S/C7H7NO2/c8-6-3-1-5(2-4-6)7(9)10/h1-4H,8H2,(H,9,10) |
| ALYNCZNDIQEVRV-UHFFFAOYSA-N |
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Arabidopsis thaliana
(NCBI:txid3702)
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See:
PubMed
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Escherichia coli
(NCBI:txid562)
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See:
PubMed
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Bronsted acid
A molecular entity capable of donating a hydron to an acceptor (Bronsted base).
(via oxoacid )
Bronsted base
A molecular entity capable of accepting a hydron from a donor (Bronsted acid).
(via organic amino compound )
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Escherichia coli metabolite
Any bacterial metabolite produced during a metabolic reaction in Escherichia coli.
plant metabolite
Any eukaryotic metabolite produced during a metabolic reaction in plants, the kingdom that include flowering plants, conifers and other gymnosperms.
allergen
A chemical compound, or part thereof, which causes the onset of an allergic reaction by interacting with any of the molecular pathways involved in an allergy.
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View more via ChEBI Ontology
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1-Amino-4-carboxybenzene
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HMDB
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4-Amino-benzoic acid
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ChEMBL
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4-Aminobenzoesäure
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ChEBI
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4-Aminobenzoic acid
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KEGG COMPOUND
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4-AMINOBENZOIC ACID
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PDBeChem
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4-Carboxyaniline
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HMDB
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4-Carboxyphenylamine
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HMDB
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ABEE
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KEGG COMPOUND
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γ-aminobenzoic acid
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HMDB
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gamma-Aminobenzoic acid
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HMDB
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p-Aminobenzoesäure
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ChEBI
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p-aminobenzoic acid
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NIST Chemistry WebBook
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p-carboxyaniline
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HMDB
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p-carboxyphenylamine
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HMDB
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PABA
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NIST Chemistry WebBook
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para-aminobenzoic acid
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NIST Chemistry WebBook
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150-13-0
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CAS Registry Number
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KEGG COMPOUND
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150-13-0
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CAS Registry Number
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NIST Chemistry WebBook
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150-13-0
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CAS Registry Number
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ChemIDplus
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471605
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Reaxys Registry Number
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Reaxys
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50150
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Gmelin Registry Number
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Gmelin
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Song GC, Choi HK, Ryu CM (2013)
The folate precursor para-aminobenzoic acid elicits induced resistance against Cucumber mosaic virus and Xanthomonas axonopodis.
Annals of botany 111, 925-934 [PubMed:23471007]
[show Abstract]
Background and aimsThe use of vitamins including vitamin B1, B2 and K3 for the induction of systemic acquired resistance (SAR) to protect crops against plant pathogens has been evaluated previously. The use of vitamins is beneficial because it is cost effective and safe for the environment. The use of folate precursors, including ortho-aminobenzoic acid, to induce SAR against a soft-rot pathogen in tobacco has been reported previously.MethodsIn the present study, para-aminobenzoic acid (PABA, also referred to as vitamin Bx) was selected owing to its effect on the induction of SAR against Xanthomonas axonopodis pv. vesicatoria in pepper plants through greenhouse screening.Key resultsDipping of pepper seedlings in a 1 mm PABA solution in field trials induced SAR against artificially infiltrated X. axonopodis pv. vesicatoria and naturally occurring cucumber mosaic virus. Expression of the Capsicum annuum pathogenesis-related 4 gene was primed in response to pathogen infection as assessed by quantitative real-time PCR. The accumulation of cucumber mosaic virus RNA was reduced in PABA-treated pepper plants at 40 and 105 d post-treatment. Unexpectedly, fruit yield was increased in PABA-treated plants, indicating that PABA-mediated SAR successfully protected pepper plants from infection by bacterial and viral pathogens without significant fitness allocation costs.ConclusionsThe present study is the first to demonstrate the effective elicitation of SAR by a folate precursor under field conditions. | Richter MK, Focks A, Siegfried B, Rentsch D, Krauss M, Schwarzenbach RP, Hollender J (2013)
Identification and dynamic modeling of biomarkers for bacterial uptake and effect of sulfonamide antimicrobials.
Environmental pollution (Barking, Essex : 1987) 172, 208-215 [PubMed:23063996]
[show Abstract]
The effects of sulfathiazole (STA) on Escherichia coli with glucose as a growth substrate was investigated to elucidate the effect-based reaction of sulfonamides in bacteria and to identify biomarkers for bacterial uptake and effect. The predominant metabolite was identified as pterine-sulfathiazole by LC-high resolution mass spectrometry. The formation of pterine-sulfathiazole per cell was constant and independent of the extracellular STA concentrations, as they exceeded the modeled half-saturation concentration K(M)(S) of 0.011 μmol L(-1). The concentration of the dihydrofolic acid precursor para-aminobenzoic acid (pABA) increased with growth and with concentrations of the competitor STA. This increase was counteracted for higher STA concentrations by growth inhibition as verified by model simulation of pABA dynamics. The EC value for the inhibition of pABA increase was 6.9 ± 0.7 μmol L(-1) STA, which is similar to that calculated from optical density dynamics indicating that pABA is a direct biomarker for the SA effect. | Duberley KE, Abramov AY, Chalasani A, Heales SJ, Rahman S, Hargreaves IP (2013)
Human neuronal coenzyme Q10 deficiency results in global loss of mitochondrial respiratory chain activity, increased mitochondrial oxidative stress and reversal of ATP synthase activity: implications for pathogenesis and treatment.
Journal of inherited metabolic disease 36, 63-73 [PubMed:22767283]
[show Abstract]
Disorders of coenzyme Q(10) (CoQ(10)) biosynthesis represent the most treatable subgroup of mitochondrial diseases. Neurological involvement is frequently observed in CoQ(10) deficiency, typically presenting as cerebellar ataxia and/or seizures. The aetiology of the neurological presentation of CoQ(10) deficiency has yet to be fully elucidated and therefore in order to investigate these phenomena we have established a neuronal cell model of CoQ(10) deficiency by treatment of neuronal SH-SY5Y cell line with para-aminobenzoic acid (PABA). PABA is a competitive inhibitor of the CoQ(10) biosynthetic pathway enzyme, COQ2. PABA treatment (1 mM) resulted in a 54 % decrease (46 % residual CoQ(10)) decrease in neuronal CoQ(10) status (p < 0.01). Reduction of neuronal CoQ(10) status was accompanied by a progressive decrease in mitochondrial respiratory chain enzyme activities, with a 67.5 % decrease in cellular ATP production at 46 % residual CoQ(10). Mitochondrial oxidative stress increased four-fold at 77 % and 46 % residual CoQ(10). A 40 % increase in mitochondrial membrane potential was detected at 46 % residual CoQ(10) with depolarisation following oligomycin treatment suggesting a reversal of complex V activity. This neuronal cell model provides insights into the effects of CoQ(10) deficiency on neuronal mitochondrial function and oxidative stress, and will be an important tool to evaluate candidate therapies for neurological conditions associated with CoQ(10) deficiency. | Zhou L, Ji Y, Zeng C, Zhang Y, Wang Z, Yang X (2013)
Aquatic photodegradation of sunscreen agent p-aminobenzoic acid in the presence of dissolved organic matter.
Water research 47, 153-162 [PubMed:23084339]
[show Abstract]
Dissolved organic matter (DOM) is an important photosensitizer for the phototransformation of organic contaminants in sunlit natural waters. This article focuses on the photolysis kinetics and mechanism of sunscreen agent p-aminobenzoic acid (PABA) in the presence of four kinds of DOM; Suwannee River fulvic acid (SRFA), Suwannee River humic acid (SRHA), Nordic Lake fulvic acid (NOFA) and Nordic Lake humic acid (NOHA). It is evident that direct photolysis of PABA is highly pH-dependent because different species of PABA have different electrical densities on the ring system. The presence of four kinds of DOM inhibits the photolysis of PABA primarily due to their light screening effect. Meanwhile, a complex interaction involving energy transfer, triplet carbonyl group induced electron transfer, and amino acid induced proton abstraction between PABA and DOM is verified by competition kinetics experiments and density functional theory (DFT) computation. In addition, DOM-induced singlet oxygen ((1)O(2)) and hydroxyl radical (OH) are determined to play an insignificant role in PABA photolysis by competition dynamics method. Photoproducts identification using solid phase extraction-liquid chromatography-mass spectrometry (SPE-LC-MS) techniques reveals that the distribution of the photoproducts could not be affected by the addition of DOM. Two photodegradation pathways of PABA are temporarily proposed, in which the di(tri)-polymerization of intermediates are the dominant pathway whereas the oxidation of amino group to nitryl followed by hydroxylation is a minor process. Our findings reveal that direct photolysis is the dominant transformation pathway of PABA in natural sunlit waters, while the presence of DOM could evidently influence such process by light screening effect, energy transfer, electron transfer and proton abstraction mechanism. The findings in this study provide useful information for understanding of interaction between DOM and organic contaminants. | Ko YG, Ma PX (2012)
Growth of oriented p-aminobenzoic acid crystals by directional freezing.
CrystEngComm 14, 7891-7894 [PubMed:23144588]
[show Abstract]
Oriented long needle-like p-aminobenzoic acid (PABA) crystals are successfully prepared by directional freezing of PABA solution in this work. The width of the oriented crystals is controlled by changing the directional cooling rate, resulting in varying crystal morphologies and thermodynamic properties while maintaining the same chemical structure. | Föllmann W, Blaszkewicz M, Behm C, Degen GH, Golka K (2012)
N-Acetylation of p-aminobenzoic acid and p-phenylenediamine in primary porcine urinary bladder epithelial cells and in the human urothelial cell line 5637.
Journal of toxicology and environmental health. Part A 75, 1206-1215 [PubMed:22994574]
[show Abstract]
N-Acetyltransferases (NAT) are important enzymes in the metabolism of certain carcinogenic arylamines, as N-acetylation decreases or prevents their bioactivation via N-hydroxylation. To study such processes in the bladder, cell culture models may be used, but metabolic competence needs to be characterized. This study focused on the N-acetylation capacity of two urothelial cell systems, using p-aminobenzoic acid (PABA) and the hair dye precursor p-phenylenediamine (PPD), two well-known substrates of the enzyme NAT1. The constitutive NAT1 activity was investigated using primary cultures of porcine urinary bladder epithelial cells (PUBEC) and in the human urothelial cell line 5637 to assess their suitability for further in vitro studies on PABA and PPD-induced toxicity. N-Acetylation of PABA and PPD was determined by high-performance liquid chromatography (HPLC) analysis in cytosols of the two cell systems upon incubation with various substrate levels for up to 60 min. The primary PUBEC revealed higher N-acetylation rates (2.5-fold for PABA, 5-fold for PPD) compared to the 5637 cell line, based on both PABA conversion to its acetylated metabolite and formation of mono- and diacetylated PPD. The urothelial cell systems may thus be useful as a tool for further studies on the N-acetylation of aromatic amines via NAT1. | Jenkinson C, Jenkins RE, Maggs JL, Kitteringham NR, Aleksic M, Park BK, Naisbitt DJ (2009)
A mechanistic investigation into the irreversible protein binding and antigenicity of p-phenylenediamine.
Chemical research in toxicology 22, 1172-1180 [PubMed:19469519]
[show Abstract]
Exposure to the skin sensitizer p-phenylenediamine (PPD) is associated with allergic contact dermatitis; however, the ability of PPD to modify protein has not been fully investigated. The aims of this study were to characterize the reactions of PPD and the structurally related chemical 2,5-dimethyl-1,4-benzoquinonediamine with model nucleophiles, a synthetic peptide (DS3) containing each of the naturally occurring amino acids and His-tagged glutathione-S-transferase pi (GSTP), and to explore the effect of dimethyl substitution on PPD-specific T-cell responses using lymphocytes from allergic patients. The reductive soft nucleophiles N-acetyl cysteine and glutathione prevented PPD self-conjugation reactions and Bandrowski's base formation, but no adducts were detected. N-Acetyl lysine, a hard nucleophile, did not alter the rate of PPD degradation or form PPD adducts. With PPD and 2,5-dimethyl-1,4-benzoquinonediamine, only cysteine was targeted in the DS3 peptide. PPD and 2,5-dimethyl-1,4-benzoquinonediamine were also found to selectively modify the reactive Cys 47 residue of GSTP, which has a pK(a) of 3.5-4.2 and therefore exists in a largely protonated form. Glutathione formed mixed disulfides with the DS3 peptide, reducing levels of PPD binding. Lymphocytes from PPD allergic patients proliferated in the presence of PPD but not with 2,5-dimethyl-1,4-benzoquinonediamine. These results reveal that PPD and 2,5-dimethyl-1,4-benzoquinonediamine bind selectively to specific cysteine residues in peptides and proteins. Lymphocytes from PPD allergic patients were capable of discriminating between the different haptenic structures, suggesting that the hapten, but not the peptide moiety associated with MHC, is an important determinant for T-cell recognition. | Tao YH, Yuan Z, Tang XQ, Xu HB, Yang XL (2006)
Inhibition of GABA shunt enzymes' activity by 4-hydroxybenzaldehyde derivatives.
Bioorganic & medicinal chemistry letters 16, 592-595 (Source: ChEMBL) [PubMed:16290145]
[show Abstract]
4-Hydroxybenzaldehyde (HBA) derivatives were examined as inhibitors for GABA transaminase (GABA-T) and succinic semialdehyde dehydrogenase (SSADH). Investigation of structure-activity relation revealed that a carbonyl group or an amino group as well as a hydroxy group at the para position of the benzene ring are important for both enzymes' inhibition. HBA was shown to give competitive inhibition of GABA-T with respect to alpha-ketoglutarate and competitive inhibition of SSADH. 4-Hydroxybenzylamine (HBM) also showed the competitive inhibition on GABA-T with respect to GABA. In conclusion, the inhibitory effects of HBA and HBM on both enzymes could result from the similarity between both molecules and the two enzymes' substrates in structure, as well as the conjugative effect of the benzene ring. This suggested that the presence of the benzene ring may be accepted by the active site of both enzymes, HBA and HBM may be considered as lead compounds to design novel GABA-T inhibitors. | Dixon S, Ziebart KT, He Z, Jeddeloh M, Yoo CL, Wang X, Lehman A, Lam KS, Toney MD, Kurth MJ (2006)
Aminodeoxychorismate synthase inhibitors from one-bead one-compound combinatorial libraries: "staged" inhibitor design.
Journal of medicinal chemistry 49, 7413-7426 (Source: ChEMBL) [PubMed:17149871]
[show Abstract]
4-Amino-4-deoxychorismate synthase (ADCS) catalyzes the first step in the conversion of chorismate into p-aminobenzoate, which is incorporated into folic acid. We aim to discover compounds that inhibit ADCS and serve as leads for a new class of antimicrobial compounds. This report presents (1) synthesis of a mass-tag encoded library based on a "staged" design, (2) massively parallel fluorescence-based on-bead screening, (3) rapid structural identification of hits, and (4) full kinetic analysis of ADCS. All inhibitors are competitive against chorismate and Mg(2+). The most potent ADCS inhibitor identified has a K(i) of 360 microM. We show that the combinatorial diversity elements add substantial binding affinity by interacting with residues outside of but proximal to the active site. The methods presented here constitute a paradigm for inhibitor discovery through active site targeting, enabled by rapid library synthesis, facile massively parallel screening, and straightforward hit identification. | Wyss DF, Arasappan A, Senior MM, Wang YS, Beyer BM, Njoroge FG, McCoy MA (2004)
Non-peptidic small-molecule inhibitors of the single-chain hepatitis C virus NS3 protease/NS4A cofactor complex discovered by structure-based NMR screening.
Journal of medicinal chemistry 47, 2486-2498 (Source: ChEMBL) [PubMed:15115392]
[show Abstract]
NMR-based screening of a customized fragment library identified 16 small-molecule hits that bind weakly (K(D) approximately 100 microM to 10 mM) to substrate binding sites of the NS4A-bound NS3 protease of the hepatitis C virus (HCV). Analogues for five classes of NMR hits were evaluated by a combination of NMR and biochemical data yielding SAR and, in most cases, optimized hits with improved potencies (K(D) approximately K(I) approximately 40 microM to 1 mM). NMR chemical shift perturbation data were used to establish the binding location and orientation of the active site directed scaffolds in these five analogue series. Two of these scaffolds, which bind the enzyme at the proximal S1-S3 and S2' substrate binding sites, were linked together producing competitive inhibitors of the HCV NS3 protease with potencies in the micromolar range. This example illustrates that the low molecular weight scaffolds discovered from structure-based NMR screening can be optimized with focused structure-guided chemistry to produce potent nonpeptidic small-molecule inhibitors of the HCV NS3 protease. | Basset GJ, Quinlivan EP, Ravanel S, Rébeillé F, Nichols BP, Shinozaki K, Seki M, Adams-Phillips LC, Giovannoni JJ, Gregory JF, Hanson AD (2004)
Folate synthesis in plants: the p-aminobenzoate branch is initiated by a bifunctional PabA-PabB protein that is targeted to plastids.
Proceedings of the National Academy of Sciences of the United States of America 101, 1496-1501 [PubMed:14745019]
[show Abstract]
It is not known how plants synthesize the p-aminobenzoate (PABA) moiety of folates. In Escherichia coli, PABA is made from chorismate in two steps. First, the PabA and PabB proteins interact to catalyze transfer of the amide nitrogen of glutamine to chorismate, forming 4-amino-4-deoxychorismate (ADC). The PabC protein then mediates elimination of pyruvate and aromatization to give PABA. Fungi, actinomycetes, and Plasmodium spp. also synthesize PABA but have proteins comprising fused domains homologous to PabA and PabB. These bipartite proteins are commonly called "PABA synthases," although it is unclear whether they produce PABA or ADC. Genomic approaches identified Arabidopsis and tomato cDNAs encoding bipartite proteins containing fused PabA and PabB domains, plus a putative chloroplast targeting peptide. These cDNAs encode functional enzymes, as demonstrated by complementation of an E. coli pabA pabB double mutant and a yeast PABA-synthase deletant. The partially purified recombinant Arabidopsis protein did not produce PABA unless the E. coli PabC enzyme was added, indicating that it forms ADC, not PABA. The enzyme behaved as a monomer in size-exclusion chromatography and was not inhibited by physiological concentrations of PABA, its glucose ester, or folates. When the putative targeting peptide was fused to GFP and expressed in protoplasts, the fusion protein appeared only in chloroplasts, indicating that PABA synthesis is plastidial. In the pericarp of tomato fruit, the PabA-PabB mRNA level fell drastically as ripening advanced, but there was no fall in total PABA content, which stayed between 0.7 and 2.3 nmol.g(-1) fresh weight. | Gildersleeve J, Janes J, Ulrich H, Yang P, Barbas C, Schultz PG (2002)
Development of a genetic selection for catalytic antibodies.
Bioorganic & medicinal chemistry letters 12, 1691-1694 (Source: ChEMBL) [PubMed:12039592]
[show Abstract]
The design and evaluation of a new genetic selection system for evolving catalytic antibodies with aldolase activity are described. Through a series of model selections, we have identified selection conditions where expression of a catalytically active antibody confers a growth advantage to Escherichia coli. In addition, we provide evidence that the growth advantage is a direct result of catalytic activity. | Chand P, Babu YS, Bantia S, Chu N, Cole LB, Kotian PL, Laver WG, Montgomery JA, Pathak VP, Petty SL, Shrout DP, Walsh DA, Walsh GM (1997)
Design and synthesis of benzoic acid derivatives as influenza neuraminidase inhibitors using structure-based drug design.
Journal of medicinal chemistry 40, 4030-4052 (Source: ChEMBL) [PubMed:9406595]
[show Abstract]
A series of 94 benzoic acid derivatives was synthesized and tested for its ability to inhibit influenza neuraminidase. The enzyme-inhibitor complex structure was determined by X-ray crystallographic analysis for compounds which inhibited the enzyme. The most potent compound tested in vitro, 5 (4-acetylamino)-3-guanidinobenzoic acid), had an IC50 = 2.5 x 10(-6) M against N9 neuraminidase. Compound 5 was oriented in the active site of the neuraminidase in a manner that was not predicted from the reported active site binding of GANA (4) with neuraminidase. In a mouse model of influenza, 5 did not protect the mice from weight loss due to the influenza virus when dosed intranasally. | Good AC, Peterson SJ, Richards WG (1993)
QSAR's from similarity matrices. Technique validation and application in the comparison of different similarity evaluation methods.
Journal of medicinal chemistry 36, 2929-2937 (Source: ChEMBL) [PubMed:8411009]
[show Abstract]
It has recently been shown that good quantitative structure-activity relationships can be obtained through statistical analysis of molecular similarity matrices. Here we extend the technique to seven additional molecular series, previously studied using Comparative Molecular Field Analysis (CoMFA) methodology. The results are used to confirm technique applicability across a wider range of QSAR problems and to compare quantitatively the ability of various similarity indices to describe biological systems. The relative merits of this technique in comparison to CoMFA are discussed. | Da YZ, Ito K, Fujiwara H (1992)
Energy aspects of oil/water partition leading to the novel hydrophobic parameters for the analysis of quantitative structure-activity relationships.
Journal of medicinal chemistry 35, 3382-3387 (Source: ChEMBL) [PubMed:1527790]
[show Abstract]
Partition properties, that is partition coefficients and enthalpies (delta Hp degree) and entropies (delta Sp degree) of partition, have been measured for 50 benzoic acids in the 1-octanol/water system, and their role in QSAR (quantitative structure-activity relationship) analysis examined. The novel hydrophobic parameters have been introduced as a result of the separation of the Gibbs free energy term into the corresponding enthalpy and entropy terms. Application of these novel parameters to some available biological activity data supported the usefulness of these parameters in QSAR analysis. Relative contributions of the enthalpy and entropy terms are also discussed. | Dunn WJ, Koehler MG, Grigoras S (1987)
The role of solvent-accessible surface area in determining partition coefficients.
Journal of medicinal chemistry 30, 1121-1126 (Source: ChEMBL) [PubMed:3599019]
[show Abstract]
The logarithm of the partition coefficient (log P) of low-molecular-weight organic compounds is a physicochemical parameter used extensively in structure-biological activity studies to model interactions of the compounds with nonpolar phases in vitro and in vivo. The partition coefficient can be determined between water and a number of nonpolar solvents. The most common nonpolar solvent is 1-octanol, but solvents such as benzene, carbon tetrachloride, and chloroform are frequently used as models for the nonpolar phases. The functional relationship between chemical structure and partitioning is not well-understood. In this paper, partition coefficient data for 50 solutes in six nonpolar solvent systems are analyzed by using principal components analysis. The objective of the work is to explore the relationship between solute structure and partitioning behavior for simple organic compounds. Two structural factors are found to be important, with the isotropic surface area being the most important. The isotropic surface area can be used to estimate log P in some solvents and as an independent variable in quantitative structure-activity relationships (QSAR). This is illustrated by estimating the rate of epidermal diffusion of steroids. | Bundgaard H, Nielsen NM (1987)
Esters of N,N-disubstituted 2-hydroxyacetamides as a novel highly biolabile prodrug type for carboxylic acid agents.
Journal of medicinal chemistry 30, 451-454 (Source: ChEMBL) [PubMed:3820215] | Ames MM, Selassie CD, Woodson LC, Van Loon JA, Hansch C, Weinshilboum RM (1986)
Thiopurine methyltransferase: structure-activity relationships for benzoic acid inhibitors and thiophenol substrates.
Journal of medicinal chemistry 29, 354-358 (Source: ChEMBL) [PubMed:3950915]
[show Abstract]
Twenty-seven substituted benzoic acids have been studied as inhibitors of partially purified human renal thiopurine methyltransferase (TPMT). Quantitative structure-activity relationship (QSAR) analysis resulted in the following equation: pI50 = 1.25( +/- 0.53)pi'3 + 0.73( +/- 0.38)MR3,4 + 2.92( +/- 0.39). In this equation pI50 is the -log of the concentration of compound that inhibits the enzyme activity by 50% (IC50);pi'3 is the relative hydrophobicity of the more hydrophobic of the two meta substituents; and MR3,4 is the molar refractivity of the more hydrophobic of the two meta substituents and of the para substituent on the phenyl ring. In addition, 14 substituted thiophenols were tested as substrates for the enzyme. All 14 thiophenols tested were excellent substrates with Km constants (0.8-7.8 microM) that were at least 2 orders of magnitude lower than those of any known thiopurine substrate for TPMT. However, there was no discernible relationship between the activities of thiophenol substrates and their physicochemical parameters. These results suggest that benzoic acid inhibitors of and thiophenol substrates for TPMT may interact with different sites on the enzyme. | Ansbacher S (1941)
p-AMINOBENZOIC ACID, A VITAMIN.
Science (New York, N.Y.) 93, 164-165 [PubMed:17743450] | Wiedling S (1941)
P-AMINOBENZOIC ACID, AN ESSENTIAL METABOLITE FOR AUTOTROPHIC ORGANISMS.
Science (New York, N.Y.) 94, 389 [PubMed:17800214] |
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