KEGG ENZYME: 2.3.1.284

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

MTU:

Rv3822

MTV:

RVBD_3822

MTC:

MT3930

MRA:

MRA_3862

MTF:	TBFG_13856

MTB:	TBMG_03869

MTK:	TBSG_03892

MTZ:	TBXG_003839

MTG:	MRGA327_23530

MTI:	MRGA423_24115

MTE:	CCDC5079_3552

MTUR:

CFBS_4052

MTL:	CCDC5180_3501

MTO:	MTCTRI2_3901

MTD:

UDA_3822

MTN:	ERDMAN_4189

MTJ:	J112_20550

MTUB:

MT7199_3891

MTUC:

J113_26750

MTUE:

J114_20425

MTX:	M943_19625

MTUH:

I917_26880

MTUL:

TBHG_03760

MTUT:

HKBT1_4035

MTUU:

HKBT2_4045

MTQ:	HKBS1_4048

MBO:	BQ2027_MB3852(chp1)

MBB:	BCG_3884 BCG_3885

MBT:	JTY_3886 JTY_3887

MBM:	BCGMEX_3885 BCGMEX_3886

MBK:	K60_039650 K60_039660

MBX:

BCGT_3687

MAF:

MAF_38370

MMIC:

RN08_4219

MCE:	MCAN_38411

MCQ:	BN44_120232

MCV:	BN43_90339

MCX:	BN42_90347

MCZ:	BN45_110184

MORY:

MO_003974(chp1)

MMC:

Mmcs_0415

MKM:

Mkms_0424

MJL:

Mjls_0403

MSEO:

MSEO_38230(chp1)

MADI:

A7U43_19235

MVA:

Mvan_1838

MGI:	Mflv_3864 Mflv_4518

MSP:	Mspyr1_32070 Mspyr1_39180

MCB:	Mycch_1461 Mycch_2781

MNE:	D174_00260

MYN:	MyAD_00245

MVQ:	MYVA_1677 MYVA_1678

MLL:	B1R94_05730 B1R94_06160

MDU:	MDUV_14710 MDUV_35890

MAUU:

NCTC10437_00019 NCTC10437_01658

MAIC:

MAIC_50680

MPSC:

MPSYJ_00230 MPSYJ_38500

MANY:

MANY_43990

MAUB:

MAUB_00590

MPOF:

MPOR_05890 MPOR_48250

MPAE:

K0O64_02655 K0O64_05740 K0O64_15800

MRF:	MJO55_22005

MCRO:

MI149_03305 MI149_06440 MI149_16755

MFRE:

EXE63_14520

MBUG:

MU0053_002672

GOR:

KTR9_2569

GTA:	BCM27_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

LinkDB

DBGET integrated database retrieval system