CHEBI:15533 - octanoyl-CoA

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ChEBI Name octanoyl-CoA
ChEBI ID CHEBI:15533
Definition A medium-chain fatty acyl-CoA that results from the formal condensation of the thiol group of coenzyme A with the carboxy group of octanoic acid.
Stars This entity has been manually annotated by the ChEBI Team.
Secondary ChEBI IDs CHEBI:41542, CHEBI:7724, CHEBI:14681, CHEBI:25651
Supplier Information ZINC000096014975
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Octanoyl-coenzyme A is the endpoint of beta oxidation in peroxisomes. It is produced alongside acetyl-CoA and transferred to the mitochondria to be further oxidized into acetyl-CoA.
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Formula C29H50N7O17P3S
Net Charge 0
Average Mass 893.730
Monoisotopic Mass 893.21968
InChI InChI=1S/C29H50N7O17P3S/c1-4-5-6-7-8-9-20(38)57-13-12-31-19(37)10-11-32-27(41)24(40)29(2,3)15-50-56(47,48)53-55(45,46)49-14-18-23(52-54(42,43)44)22(39)28(51-18)36-17-35-21-25(30)33-16-34-26(21)36/h16-18,22-24,28,39-40H,4-15H2,1-3H3,(H,31,37)(H,32,41)(H,45,46)(H,47,48)(H2,30,33,34)(H2,42,43,44)/t18-,22-,23-,24+,28-/m1/s1
InChIKey KQMZYOXOBSXMII-CECATXLMSA-N
SMILES CCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N
Metabolite of Species Details
Mus musculus (NCBI:txid10090) Source: BioModels - MODEL1507180067 See: PubMed
Escherichia coli (NCBI:txid562) See: PubMed
Roles Classification
Chemical Role(s): acyl donor
Any donor that can transfer acyl groups between molecular entities.
(via acyl-CoA )
Biological Role(s): Escherichia coli metabolite
Any bacterial metabolite produced during a metabolic reaction in Escherichia coli.
mouse metabolite
Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus).
View more via ChEBI Ontology
ChEBI Ontology
Outgoing octanoyl-CoA (CHEBI:15533) has functional parent octanoic acid (CHEBI:28837)
octanoyl-CoA (CHEBI:15533) has role Escherichia coli metabolite (CHEBI:76971)
octanoyl-CoA (CHEBI:15533) has role mouse metabolite (CHEBI:75771)
octanoyl-CoA (CHEBI:15533) is a medium-chain fatty acyl-CoA (CHEBI:61907)
octanoyl-CoA (CHEBI:15533) is a saturated fatty acyl-CoA (CHEBI:231546)
octanoyl-CoA (CHEBI:15533) is conjugate acid of octanoyl-CoA(4−) (CHEBI:57386)
Incoming (R)-3-hydroxyoctanoyl-CoA (CHEBI:28573) has functional parent octanoyl-CoA (CHEBI:15533)
(S)-3-hydroxyoctanoyl-CoA (CHEBI:28632) has functional parent octanoyl-CoA (CHEBI:15533)
3-oxooctanoyl-CoA (CHEBI:28264) has functional parent octanoyl-CoA (CHEBI:15533)
3-thiaoctanoyl-CoA (CHEBI:41611) has functional parent octanoyl-CoA (CHEBI:15533)
7-methyl-3-oxooctanoyl-CoA (CHEBI:15506) has functional parent octanoyl-CoA (CHEBI:15533)
octanoyl-CoA(4−) (CHEBI:57386) is conjugate base of octanoyl-CoA (CHEBI:15533)
IUPAC Name
3'-phosphoadenosine 5'-(3-{(3R)-3-hydroxy-2,2-dimethyl-4-[(3-{[2-(octanoylsulfanyl)ethyl]amino}-3-oxopropyl)amino]-4-oxobutyl} dihydrogen diphosphate)
Synonyms Sources
8:0-CoA ChEBI
C8:0-CoA ChEBI
capryloyl-CoA ChEBI
capryloyl-coenzyme A ChEBI
Coenzyme A, S-octanoate ChemIDplus
n-octanoyl-CoA ChEBI
Octanoyl-CoA KEGG COMPOUND
Octanoyl-coa ChemIDplus
Octanoyl-coenzyme A ChemIDplus
octanoylcoenzyme A ChEBI
octylyl-CoA ChEBI
octylyl-coenzyme A ChEBI
Manual Xrefs Databases
393007 ChemSpider
c0048 UM-BBD
C01944 KEGG COMPOUND
CO8 PDBeChem
DB02910 DrugBank
FDB022409 FooDB
HMDB0001070 HMDB
Octanoyl-CoA Wikipedia
View more database links
Registry Numbers Types Sources
1264-52-4 CAS Registry Number ChemIDplus
6562085 Beilstein Registry Number Beilstein
8033230 Reaxys Registry Number Reaxys
Citations
Aso Y, Nomura Y, Sano M, Sato R, Tanaka T, Ohara H, Matsumoto K, Wada K (2021)
Caprylic acid enhances hydroxyhexylitaconic acid production in Aspergillus niger S17-5.
Journal of applied microbiology 130, 1972-1980 [PubMed:33064909]
[show Abstract]
Zhong L, Diao X, Zhang N, Li F, Zhou H, Chen H, Bai X, Ren X, Zhang Y, Wu D, Bian X (2021)
Engineering and elucidation of the lipoinitiation process in nonribosomal peptide biosynthesis.
Nature communications 12, 296 [PubMed:33436600]
[show Abstract]
Huang CM, Lyu SY, Lin KH, Chen CL, Chen MH, Shih HW, Hsu NS, Lo IW, Wang YL, Li YS, Wu CJ, Li TL (2019)
Teicoplanin Reprogrammed with the N-Acyl-Glucosamine Pharmacophore at the Penultimate Residue of Aglycone Acquires Broad-Spectrum Antimicrobial Activities Effectively Killing Gram-Positive and -Negative Pathogens.
ACS infectious diseases 5, 430-442 [PubMed:30599088]
[show Abstract]
Sathyanarayanan N, Cannone G, Gakhar L, Katagihallimath N, Sowdhamini R, Ramaswamy S, Vinothkumar KR (2019)
Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway.
Nature communications 10, 4127 [PubMed:31511507]
[show Abstract]
Chacón MG, Kendrick EG, Leak DJ (2019)
Engineering Escherichia coli for the production of butyl octanoate from endogenous octanoyl-CoA.
PeerJ 7, e6971 [PubMed:31304053]
[show Abstract]
Kiema TR, Thapa CJ, Laitaoja M, Schmitz W, Maksimainen MM, Fukao T, Rouvinen J, Jänis J, Wierenga RK (2019)
The peroxisomal zebrafish SCP2-thiolase (type-1) is a weak transient dimer as revealed by crystal structures and native mass spectrometry.
The Biochemical journal 476, 307-332 [PubMed:30573650]
[show Abstract]
Onwukwe GU, Koski MK, Pihko P, Schmitz W, Wierenga RK (2015)
Structures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole.
Acta crystallographica. Section D, Biological crystallography 71, 2178-2191 [PubMed:26527136]
[show Abstract]
Lyu SY, Liu YC, Chang CY, Huang CJ, Chiu YH, Huang CM, Hsu NS, Lin KH, Wu CJ, Tsai MD, Li TL (2014)
Multiple complexes of long aliphatic N-acyltransferases lead to synthesis of 2,6-diacylated/2-acyl-substituted glycopeptide antibiotics, effectively killing vancomycin-resistant enterococcus.
Journal of the American Chemical Society 136, 10989-10995 [PubMed:25095906]
[show Abstract]
Ohgusu H, Shirouzu K, Nakamura Y, Nakashima Y, Ida T, Sato T, Kojima M (2009)
Ghrelin O-acyltransferase (GOAT) has a preference for n-hexanoyl-CoA over n-octanoyl-CoA as an acyl donor.
Biochemical and biophysical research communications 386, 153-158 [PubMed:19501572]
[show Abstract]
Partanen ST, Novikov DK, Popov AN, Mursula AM, Hiltunen JK, Wierenga RK (2004)
The 1.3 A crystal structure of human mitochondrial Delta3-Delta2-enoyl-CoA isomerase shows a novel mode of binding for the fatty acyl group.
Journal of molecular biology 342, 1197-1208 [PubMed:15351645]
[show Abstract]
Hashimoto F, Furuya Y, Hayashi H (2001)
Accumulation of medium chain acyl-CoAs during beta-oxidation of long chain fatty acid by isolated peroxisomes from rat liver.
Biological & pharmaceutical bulletin 24, 600-606 [PubMed:11411544]
[show Abstract]
Engel CK, Kiema TR, Hiltunen JK, Wierenga RK (1998)
The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule.
Journal of molecular biology 275, 847-859 [PubMed:9480773]
[show Abstract]
Engel CK, Kiema TR, Hiltunen JK, Wierenga RK (1998)
The Crystal Structure of Enoyl-CoA Hydratase Complexed with Octanoyl-CoA Reveals the Structural Adaptations Required for Binding of a Long Chain Fatty Acid-CoA Molecule
Journal of molecular biology 275, 859-847 [PubMed:9514714]
[show Abstract]
Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ (1996)
Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
Biochemistry 35, 12412-12420 [PubMed:8823176]
[show Abstract]
Kumar NR, Srivastava DK (1994)
Reductive half-reaction of medium-chain fatty acyl-CoA dehydrogenase utilizing octanoyl-CoA/octenoyl-CoA as a physiological substrate/product pair: similarity in the microscopic pathways of octanoyl-CoA oxidation and octenoyl-CoA binding.
Biochemistry 33, 8833-8841 [PubMed:8038175]
[show Abstract]
Cummings JG, Thorpe C (1993)
Stereoselective interaction of 2-halo-acyl-CoA derivatives with medium chain acyl-CoA dehydrogenase from pig kidney.
Archives of biochemistry and biophysics 302, 85-91 [PubMed:8470910]
[show Abstract]
Kim JJ, Wang M, Paschke R (1993)
Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate.
Proceedings of the National Academy of Sciences of the United States of America 90, 7523-7527 [PubMed:8356049]
[show Abstract]
Moore KH, Decker BP, Schreefel FP (1988)
Hepatic hydrolysis of octanoyl-CoA and valproyl-CoA in control and valproate-fed animals.
The International journal of biochemistry 20, 175-178 [PubMed:2895026]
[show Abstract]
Saggerson ED (1982)
Carnitine acyltransferase activities in rat liver and heart measured with palmitoyl-CoA and octanoyl-CoA. Latency, effects of K+, bivalent metal ions and malonyl-CoA.
The Biochemical journal 202, 397-405 [PubMed:7092822]
[show Abstract]
Kunau WH, Dommes P (1978)
Degradation of unsaturated fatty acids. Identification of intermediates in the degradation of cis-4-decenoly-CoA by extracts of beef-liver mitochondria.
European journal of biochemistry 91, 533-544 [PubMed:729581]
[show Abstract]
Stewart HB, Tubbs PK, Stanley KK (1973)
Intermediates in fatty acid oxidation.
The Biochemical journal 132, 61-76 [PubMed:4722901]
[show Abstract]
Graham AB, Park MV (1969)
A product-inhibition study of the mechanism of mitochondrial octanoly-coenzyme A synthetase.
The Biochemical journal 111, 257-262 [PubMed:4304157]
[show Abstract]
Kusaka T, Goldman DS (1967)
Column chromatographic purification of octanoyl-CoA.
Analytical biochemistry 19, 294-299 [PubMed:6048700]
Last Modified
07 June 2024