MetaCyc Reaction:

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:

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 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Together with EC, long-chain-fatty-acyl-CoA reductase, forms a fatty acid reductase system which produces the substrate of EC, alkanal monooxygenase (FMN), thus being a component of the bacterial luciferase system.

Citations: [Riendeau82, Wall86]

Relationship Links: BRENDA:EC: , ENZYME:EC: , IUBMB-ExplorEnz:EC: , UniProt:RELATED-TO:P14286 , UniProt:RELATED-TO:P29334 , UniProt:RELATED-TO:Q51885 , UniProt:RELATED-TO:Q52100 , UniProt:RELATED-TO:Q56823

Revised 10-Nov-2011 by Caspi R , SRI International


Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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

Wall86: Wall, L., Meighen, E.A. (1986). "Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum." Biochemistry 25: 4315-4321.

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Sat Oct 10, 2015, BIOCYC14A.