KEGG   ENZYME: 6.2.1.57Help
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
BRITE hierarchy
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) [RN:R12395];
(1a) ATP + stearate = diphosphate + (stearoyl)adenylate [RN:R12393];
(1b) (stearoyl)adenylate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + a stearoyl-[(hydroxy)phthioceranic acid synthase] [RN:R12394];
(2) ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase] (overall reaction) [RN:R12398];
(2a) ATP + palmitate = diphosphate + (palmitoyl)adenylate [RN:R12396];
(2b) (palmitoyl)adenylate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + a palmitoyl-[(hydroxy)phthioceranic acid synthase] [RN:R12397]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
stearate [CPD:C01530];
holo-[(hydroxy)phthioceranic acid synthase] [CPD:C22133];
(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
MTU: Rv3826(fadD23)
MTV: RVBD_3826
MTC: MT3934
MRA: MRA_3866(fadD23)
MTF: TBFG_13860
MTB: TBMG_03873
MTK: TBSG_03896
MTZ: TBXG_003843
MTG: MRGA327_23565
MTI: MRGA423_24155
MTUR: CFBS_4057(fadD23)
MTO: MTCTRI2_3905(fadD23)
MTD: UDA_3826(fadD23)
MTN: ERDMAN_4193(fadD23)
MTUC: J113_26780
MTUE: J114_20445
MTUL: TBHG_03764
MTUT: HKBT1_4039(fadD23)
MTUU: HKBT2_4049(fadD23)
MTQ: HKBS1_4052(fadD23)
MBO: BQ2027_MB3856(fadD23)
MBB: BCG_3889(fadD23)
MBT: JTY_3891(fadD23)
MBX: BCGT_3691
MAF: MAF_38410(fadD23)
MMIC: RN08_4224
MCE: MCAN_38451(fadD23)
MCQ: BN44_120236(fadD)
MCV: BN43_90343(fadD)
MCX: BN42_90354(fadD)
MCZ: BN45_110188(fadD)
 » show all
Taxonomy
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)
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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