The Enzyme Database

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EC 6.2.1.57     
Accepted name: long-chain fatty acid adenylase/transferase FadD23
Reaction: (1) ATP + stearate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + diphosphate + a stearoyl-[(hydroxy)phthioceranic acid synthase] (overall reaction)
(1a) ATP + stearate = diphosphate + (stearoyl)adenylate
(1b) (stearoyl)adenylate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + a stearoyl-[(hydroxy)phthioceranic acid synthase]
(2) ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase] (overall reaction)
(2a) ATP + palmitate = diphosphate + (palmitoyl)adenylate
(2b) (palmitoyl)adenylate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + a palmitoyl-[(hydroxy)phthioceranic acid synthase]
Other name(s): fadD23 (gene name); long-chain fatty acid adenylyltransferase FadD23
Systematic name: palmitate:holo-[(hydroxy)phthioceranic acid synthase] ligase
Comments: This mycobacterial enzyme activates palmitate and stearate by adenylation, followed by their loading onto the polyketide synthase EC 2.3.1.287, phthioceranic/hydroxyphthioceranic acid synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gokhale, R.S., Saxena, P., Chopra, T. and Mohanty, D. Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids. Nat. Prod. Rep. 24 (2007) 267–277. [PMID: 17389997]
2.  Lynett, J. and Stokes, R.W. Selection of transposon mutants of Mycobacterium tuberculosis with increased macrophage infectivity identifies fadD23 to be involved in sulfolipid production and association with macrophages. Microbiology 153 (2007) 3133–3140. [PMID: 17768256]
[EC 6.2.1.57 created 2019]
 
 


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