KEGG   ENZYME: 6.2.1.57
Entry
EC 6.2.1.57                 Enzyme                                 
Name
long-chain fatty acid adenylase/transferase FadD23;
fadD23 (gene name);
long-chain fatty acid adenylyltransferase FadD23
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
Sysname
palmitate:holo-[(hydroxy)phthioceranic acid synthase] ligase
Reaction(IUBMB)
(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 [RN:R12393];
(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 [RN:R12396];
(2b) (palmitoyl)adenylate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + a palmitoyl-[(hydroxy)phthioceranic acid synthase]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
stearate [CPD:C01530];
holo-[(hydroxy)phthioceranic acid synthase];
(stearoyl)adenylate [CPD:C22132];
palmitate [CPD:C00249];
(palmitoyl)adenylate [CPD:C22135]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
stearoyl-[(hydroxy)phthioceranic acid synthase] [CPD:C22134];
(stearoyl)adenylate [CPD:C22132];
palmitoyl-[(hydroxy)phthioceranic acid synthase] [CPD:C22124];
(palmitoyl)adenylate [CPD:C22135]
Comment
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.
History
EC 6.2.1.57 created 2019
Orthology
K12425  long-chain fatty acid adenylase/transferase FadD23
Genes
MTURv3826(fadD23)
MTVRVBD_3826
MTCMT3934
MRAMRA_3866(fadD23)
MTFTBFG_13860
MTBTBMG_03873
MTKTBSG_03896
MTZTBXG_003843
MTGMRGA327_23565
MTECCDC5079_3557
MTURCFBS_4057(fadD23)
MTLCCDC5180_3505
MTOMTCTRI2_3905(fadD23)
MTDUDA_3826(fadD23)
MTNERDMAN_4193(fadD23)
MTJJ112_20570
MTUBMT7199_3895
MTUCJ113_26780
MTUEJ114_20445
MTXM943_19645
MTULTBHG_03764
MTUTHKBT1_4039(fadD23)
MTUUHKBT2_4049(fadD23)
MTQHKBS1_4052(fadD23)
MBOBQ2027_MB3856(fadD23)
MBBBCG_3889(fadD23)
MBTJTY_3891(fadD23)
MBKK60_039700
MBXBCGT_3691
MAFMAF_38410(fadD23)
MMICRN08_4224
MCEMCAN_38451(fadD23)
MCQBN44_120236(fadD)
MCVBN43_90343(fadD)
MCXBN42_90354(fadD)
MCZBN45_110188(fadD)
MGAUMGALJ_58670(fadD23)
 » show all
Reference
1  [PMID:17389997]
  Authors
Gokhale RS, Saxena P, Chopra T, Mohanty D
  Title
Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids.
  Journal
Nat Prod Rep 24:267-77 (2007)
DOI:10.1039/b616817p
Reference
2  [PMID:17768256]
  Authors
Lynett J, Stokes RW
  Title
Selection of transposon mutants of Mycobacterium tuberculosis with increased macrophage infectivity identifies fadD23 to be involved in sulfolipid production  and association with macrophages.
  Journal
Microbiology 153:3133-40 (2007)
DOI:10.1099/mic.0.2007/007864-0
  Sequence
[mtu:Rv3826]
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.57
IUBMB Enzyme Nomenclature: 6.2.1.57
ExPASy - ENZYME nomenclature database: 6.2.1.57
BRENDA, the Enzyme Database: 6.2.1.57
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