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6. Ligases

6.2 Forming carbon-sulfur bonds

6.2.1 Acid-thiol ligases

ID:	6.2.1.19
Description:	Long-chain-fatty-acid--protein ligase.
Alternative Name:	Acyl-protein synthetase.

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UniProtKB Enzyme Link:	UniProtKB 6.2.1.19
BRENDA Enzyme Link:	BRENDA 6.2.1.19
KEGG Enzyme Link:	KEGG6.2.1.19
BioCyc Enzyme Link:	BioCyc 6.2.1.19
ExPASy Enzyme Link:	ExPASy6.2.1.19
EC2PDB Enzyme Link:	EC2PDB 6.2.1.19
ExplorEnz Enzyme Link:	ExplorEnz 6.2.1.19
PRIAM enzyme-specific profiles Link:	PRIAM 6.2.1.19
IntEnz Enzyme Link:	IntEnz 6.2.1.19
MEDLINE Enzyme Link:	MEDLINE 6.2.1.19

RHEA:20101	a long-chain fatty acid + ATP + L-cysteinyl-[protein] = AMP + diphosphate + S-(long-chain fatty acyl)-L-cysteinyl-[protein]
RULE(radius=1)	[:1]-[C;H0;+0:2](=[:3])-[OH;+0:4].[:5]-[O;H0;+0:6]-[P;H0;+0:7](-[:8])(=[:9])-[:10].[:11]-[SH;+0:12]>>[:5]-[OH;+0:6].[:8]-[P;H0;+0:7](=[:9])(-[:10])-[OH;+0:4].[:11]-[S;H0;+0:12]-[C;H0;+0:2](-[:1])=[:3]
Reaction
Core-to-Core	No scaffolds atoms were exchanged as a result of the reaction

Title	Authors	Date	PubMed ID
Nucleotide sequence and functional analysis of the luxE gene encoding acyl-protein synthetase of the lux operon from Photobacterium leiognathi.	Lin JW, Chao YF, Weng SF	1996 Nov 21	8941351
Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex.	Riendeau D, Rodriguez A, Meighen E	1982 Jun 25	7085612
Fatty acyl-AMP as an intermediate in fatty acid reduction to aldehyde in luminescent bacteria.	Rodriguez A, Meighen E	1985 Jan 25	3968067
Identification of the acyl transfer site of fatty acyl-protein synthetase from bioluminescent bacteria.	Soly RR, Meighen EA	1991 May 5	2023262