KEGG   ENZYME: 2.3.1.288
Entry
EC 2.3.1.288                Enzyme                                 

Name
2-O-sulfo trehalose long-chain-acyltransferase;
papA2 (gene name)
Class
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
Sysname
acyl-CoA:2-O-sulfo-alpha,alpha-trehalose 2'-long-chain-acyltransferase
Reaction(IUBMB)
(1) stearoyl-CoA + 2-O-sulfo-alpha,alpha-trehalose = 2-O-sulfo-2'-stearoyl-alpha,alpha-trehalose + CoA [RN:R12465];
(2) palmitoyl-CoA + 2-O-sulfo-alpha,alpha-trehalose = 2-O-sulfo-2'-palmitoyl-alpha,alpha-trehalose + CoA [RN:R12466]
Reaction(KEGG)
R12465 R12466
Substrate
stearoyl-CoA [CPD:C00412];
2-O-sulfo-alpha,alpha-trehalose [CPD:C20985];
palmitoyl-CoA [CPD:C00154]
Product
2-O-sulfo-2'-stearoyl-alpha,alpha-trehalose [CPD:C22177];
CoA [CPD:C00010];
2-O-sulfo-2'-palmitoyl-alpha,alpha-trehalose [CPD:C22176]
Comment
This mycobacterial enzyme catalyses the acylation of 2-O-sulfo-alpha,alpha-trehalose at the 2' position by a C16 or C18 fatty acyl group during the biosynthesis of mycobacterial sulfolipids.
History
EC 2.3.1.288 created 2019
Orthology
K22795  2-O-sulfo trehalose long-chain-acyltransferase
Genes
MTU: Rv3820c(papA2)
MTV: RVBD_3820c
MTC: MT3928
MRA: MRA_3860(papA2)
MTF: TBFG_13854
MTB: TBMG_03867
MTK: TBSG_03890
MTZ: TBXG_003837
MTG: MRGA327_23520
MTI: MRGA423_24105
MTUR: CFBS_4050(papA2)
MTO: MTCTRI2_3899(papA2)
MTD: UDA_3820c(papA2)
MTN: ERDMAN_4187(papA2)
MTUC: J113_26740
MTUE: J114_20415
MTUL: TBHG_03758
MTUT: HKBT1_4033(papA2)
MTUU: HKBT2_4043(papA2)
MTQ: HKBS1_4046(papA2)
MBO: BQ2027_MB3850C(papA2)
MBB: BCG_3882c(papA2)
MBT: JTY_3884(papA2)
MBM: BCGMEX_3883c(papA2)
MBX: BCGT_3684
MAF: MAF_38350(papA2)
MMIC: RN08_4217
MCE: MCAN_15491 MCAN_38391(papA2)
MCQ: BN44_120230(papA)
MCV: BN43_30650(papA) BN43_90337(papA)
MCX: BN42_90345(papA)
MCZ: BN45_110182(papA) BN45_30635(papA)
 » show all
Reference
1  [PMID:17592143]
  Authors
Kumar P, Schelle MW, Jain M, Lin FL, Petzold CJ, Leavell MD, Leary JA, Cox JS, Bertozzi CR
  Title
PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1.
  Journal
Proc Natl Acad Sci U S A 104:11221-6 (2007)
DOI:10.1073/pnas.0611649104
  Sequence
[mtu:Rv3820c]
Reference
2  [PMID:22194604]
  Authors
Seeliger JC, Holsclaw CM, Schelle MW, Botyanszki Z, Gilmore SA, Tully SE, Niederweis M, Cravatt BF, Leary JA, Bertozzi CR
  Title
Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis.
  Journal
J Biol Chem 287:7990-8000 (2012)
DOI:10.1074/jbc.M111.315473
  Sequence
[mtu:Rv3820c]
Other DBs
ExplorEnz - The Enzyme Database: 2.3.1.288
IUBMB Enzyme Nomenclature: 2.3.1.288
ExPASy - ENZYME nomenclature database: 2.3.1.288
BRENDA, the Enzyme Database: 2.3.1.288

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