_EC 2.3.1.300 branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase.

5 PDB entries

EC 2.-.-.- Transferases. [47,784 PDB entries] EC 2.3.-.- Acyltransferases. [6,129 PDB entries] EC 2.3.1.- Transferring groups other than amino-acyl groups. [3,260 PDB entries] EC 2.3.1.300 branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase. [5 PDB entries]

1mzj

Reaction:		(1) 3-methylbutanoyl-CoA + malonyl-[ACP] + H(+) = 5-methyl-3-oxohexanoyl- [ACP] + CO2 + CoA. (2) 2-methylpropanoyl-CoA + malonyl-[ACP] + H(+) = 4-methyl-3- oxopentanoyl-[ACP] + CO2 + CoA. (3) (2S)-2-methylbutanoyl-CoA + malonyl-[ACP] + H(+) = (4S)-4-methyl-3- oxohexanoyl-[ACP] + CO2 + CoA.
		3-methylbutanoyl-CoA + malonyl-[ACP] + H(+) = 5-methyl-3-oxohexanoyl- [ACP] + CO2 + CoA 2-methylpropanoyl-CoA + malonyl-[ACP] + H(+) = 4-methyl-3- oxopentanoyl-[ACP] + CO2 + CoA (2S)-2-methylbutanoyl-CoA + malonyl-[ACP] + H(+) = (4S)-4-methyl-3- oxohexanoyl-[ACP] + CO2 + CoA Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments:		The enzyme is responsible for initiating branched-chain fatty acid biosynthesis by the dissociated (or type II) fatty-acid biosynthesis system (FAS-II) in some bacteria, using molecules derived from degradation of the branched-chain amino acids L-leucine, L-valine, and L-isoleucine to form the starting molecules for elongation by the FAS-II system. In some organisms the enzyme is also able to use acetyl-CoA, leading to production of a mix of branched-chain and straight-chain fatty acids (cf. Ec 2.3.1.180).
Links:		[IntEnz]   [ExPASy]   [KEGG]

There are 5 PDB entries in enzyme class E.C.2.3.1.300

PDB code		Protein
1mzj		Crystal structure of the priming beta-ketosynthase from the r1128 polyketide biosynthetic pathway Source: Streptomyces sp. R1128. Organism_taxid: 140437. Gene: zhuh. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B (334 residues) CATH domains: 3.40.47.10 3.40.47.10 Bound ligands:   Het Group ACE is 50.00% similar to enzyme product CO2   Het Group COA corresponds to enzyme product CoA   Het Group ACE is 50.00% similar to enzyme product CO2   Het Group COA corresponds to enzyme product CoA   Het Group ACE is 50.00% similar to enzyme product CO2   Het Group COA corresponds to enzyme product CoA
6a9n		Crystal structure of kas iii from propionibacterium acnes Source: Cutibacterium acnes. Propionibacterium acnes. Organism_taxid: 1747. Gene: fabh, b1b09_02220. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B (331 residues)
8vd9		Crystal structure of bacillus subtilis fabha, beta-ketoacyl carrier protein synthase iii Source: Bacillus subtilis. Organism_taxid: 1423. Gene: fabha, fabh, fabh1, yjax, bsu11330. Expressed in: escherichia coli. Expression_system_taxid: 562 Chain: A (311 residues)
8vda		Crystal structure of bacillus subtilis fabha-coenzyme a complex Source: Bacillus subtilis. Organism_taxid: 1423. Gene: fabha, fabh, fabh1, yjax, bsu11330. Expressed in: escherichia coli. Expression_system_taxid: 562 Chain: A (311 residues)
8vdb		Crystal structure of bacillus subtilis fabhb, beta-ketoacyl carrier protein synthase iii Source: Bacillus subtilis. Organism_taxid: 1423. Gene: fabhb, fabh2, yhfb, bsu10170. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B, C, D (326 residues)