KEGG   ENZYME: 2.3.1.284
Entry
EC 2.3.1.284                Enzyme                                 
Name
3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase;
chp1 (gene name)
Class
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
Sysname
3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-alpha,alpha-trehalose:3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-alpha,alpha-trehalose 6,6'-di(hydroxy)phthioceranyltransferase
Reaction(IUBMB)
3 3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-alpha,alpha-trehalose = 3,6,6'-tris-(hydroxy)phthioceranyl-2-palmitoyl(stearoyl)-2'-sulfo-alpha-alpha-trehalose + 2 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose [RN:R12348]
Reaction(KEGG)
R12348
Substrate
3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-alpha,alpha-trehalose [CPD:C22094]
Product
3,6,6'-tris-(hydroxy)phthioceranyl-2-palmitoyl(stearoyl)-2'-sulfo-alpha-alpha-trehalose;
2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose [CPD:C22096]
Comment
The enzyme, present in mycobacteria, catalyses the ultimate step in the biosynthesis of mycobacterial sulfolipids. It catalyses two successive transfers of a (hydroxy)phthioceranyl group from two diacylated intermediates to third diacylated intermediate, generating the tetraacylated sulfolipid.
History
EC 2.3.1.284 created 2019
Orthology
K23416  3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase
Genes
AEXAstex_3003
MTURv3822
MTVRVBD_3822
MTCMT3930
MRAMRA_3862
MTFTBFG_13856
MTBTBMG_03869
MTKTBSG_03892
MTZTBXG_003839
MTGMRGA327_23530
MTIMRGA423_24115
MTECCDC5079_3552
MTURCFBS_4052
MTLCCDC5180_3501
MTOMTCTRI2_3901
MTDUDA_3822
MTNERDMAN_4189
MTJJ112_20550
MTUBMT7199_3891
MTUCJ113_26750
MTUEJ114_20425
MTXM943_19625
MTUHI917_26880
MTULTBHG_03760
MTUTHKBT1_4035
MTUUHKBT2_4045
MTQHKBS1_4048
MBOBQ2027_MB3852
MBBBCG_3884 BCG_3885
MBTJTY_3886 JTY_3887
MBMBCGMEX_3885 BCGMEX_3886
MBKK60_039650 K60_039660
MBXBCGT_3687
MAFMAF_38370
MMICRN08_4219
MCEMCAN_38411
MCQBN44_120232
MCVBN43_90339
MCXBN42_90347
MCZBN45_110184
MMCMmcs_0415
MKMMkms_0424
MJLMjls_0403
MSEOMSEO_38230(chp1)
MPAEK0O64_02655 K0O64_05740 K0O64_15800
MRFMJO55_22005
MCROMI149_03305 MI149_06440 MI149_16755
MVAMvan_1838
MGIMflv_3864 Mflv_4518
MSPMspyr1_32070 Mspyr1_39180
MCBMycch_1461 Mycch_2781
MNED174_00260
MYNMyAD_00245
MVQMYVA_1677 MYVA_1678
MLLB1R94_05730 B1R94_06160
MDUMDUV_14710 MDUV_35890
MAUUNCTC10437_00019 NCTC10437_01658
MAICMAIC_50680
MPSCMPSYJ_00230 MPSYJ_38500
MANYMANY_43990
MAUBMAUB_00590
MPOFMPOR_05890 MPOR_48250
GORKTR9_2569
GTABCM27_13680
 » show all
Reference
1  [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:Rv3822]
Other DBs
ExplorEnz - The Enzyme Database: 2.3.1.284
IUBMB Enzyme Nomenclature: 2.3.1.284
ExPASy - ENZYME nomenclature database: 2.3.1.284
BRENDA, the Enzyme Database: 2.3.1.284

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