|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 22.214.171.124
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
Mass balance status: Balanced.
Enzyme Commission Primary Name: long-chain-fatty-acid—luciferin-component ligase
Enzyme Commission Synonyms: acyl-protein synθse
Taxonomic Range: Bacteria
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -2.4406128 [Latendresse13]
Enzyme Commission Summary:
Together with EC 126.96.36.199, long-chain-fatty-acyl-CoA reductase, forms a fatty acid reductase system which produces the substrate of EC 188.8.131.52, alkanal monooxygenase (FMN), thus being a component of the bacterial luciferase system.
Relationship Links: BRENDA:EC:184.108.40.206 , ENZYME:EC:220.127.116.11 , IUBMB-ExplorEnz:EC:18.104.22.168 , UniProt:RELATED-TO:P14286 , UniProt:RELATED-TO:P29334 , UniProt:RELATED-TO:Q51885 , UniProt:RELATED-TO:Q52100 , UniProt:RELATED-TO:Q56823
Riendeau82: Riendeau D, Rodriguez A, Meighen E (1982). "Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex." J Biol Chem 257(12);6908-15. PMID: 7085612
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493