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Information on EC 2.3.1.180 - beta-ketoacyl-[acyl-carrier-protein] synthase III and Organism(s) Micrococcus luteus and UniProt Accession C5CAR9

for references in articles please use BRENDA:EC2.3.1.180
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IUBMB Comments
The enzyme is responsible for initiating straight-chain fatty acid biosynthesis by the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. In contrast to EC 2.3.1.41, beta-ketoacyl-[acyl-carrier-protein] synthase I, and EC 2.3.1.179, beta-ketoacyl-[acyl-carrier-protein] synthase II, this enzyme specifically uses short-chain acyl-CoA thioesters (preferably acetyl-CoA) rather than acyl-[acp] as its substrate . The enzyme can also catalyse the reaction of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, but to a much lesser extent . The enzymes from some organisms (e.g. the Gram-positive bacterium Streptococcus pneumoniae) can accept branched-chain acyl-CoAs in addition to acetyl-CoA (cf. EC 2.3.1.300, branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase).
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Micrococcus luteus
UNIPROT: C5CAR9
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The taxonomic range for the selected organisms is: Micrococcus luteus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
kas iii, mtfabh, kasiii, beta-ketoacyl-acyl carrier protein synthase iii, pqsbc, beta-ketoacyl-acyl carrier protein (acp) synthase iii, beta-ketoacyl-acp synthase iii, ecfabh, acetoacetyl-acp synthase, esmd1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-ketoacyl-ACP synthase III
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3-oxoacyl:ACP synthase III
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acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Claisen condensation
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:malonyl-[acyl-carrier protein] C-acyltransferase
The enzyme is responsible for initiating straight-chain fatty acid biosynthesis by the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. In contrast to EC 2.3.1.41, beta-ketoacyl-[acyl-carrier-protein] synthase I, and EC 2.3.1.179, beta-ketoacyl-[acyl-carrier-protein] synthase II, this enzyme specifically uses short-chain acyl-CoA thioesters (preferably acetyl-CoA) rather than acyl-[acp] as its substrate [1]. The enzyme can also catalyse the reaction of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, but to a much lesser extent [1]. The enzymes from some organisms (e.g. the Gram-positive bacterium Streptococcus pneumoniae) can accept branched-chain acyl-CoAs in addition to acetyl-CoA [5] (cf. EC 2.3.1.300, branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase).
CAS REGISTRY NUMBER
COMMENTARY hide
9077-10-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
malonyl-ACP + acyl-CoA
3-oxoacyl-ACP + CoA + CO2
show the reaction diagram
specificity for branched acyl-CoA substrate
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
crystal structure analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor-diffusion method, pH 9.0, 10% PEG 200, 18% PEG 8000
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged protein expressed in Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pereira, J.H.; Goh, E.B.; Keasling, J.D.; Beller, H.R.; Adams, P.D.
Structure of FabH and factors affecting the distribution of branched fatty acids in Micrococcus luteus
Acta Crystallogr. Sect. D
68
1320-1328
2012
Micrococcus luteus (C5CAR9)
Manually annotated by BRENDA team