The Enzyme Database

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EC 2.3.1.283     
Accepted name: 2′-acyl-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase
Reaction: a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 2′-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose = a 3′-(hydroxy)phthioceranyl-2′-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose + holo-[(hydroxy)phthioceranic acid synthase]
Other name(s): papA1 (gene name)
Systematic name: (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase]:2′-acyl-2-O-sulfo-α,α-trehalose 3′-(hydroxy)phthioceranyltransferase
Comments: This mycobacterial enzyme catalyses the acylation of 2′-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose at the 3′ position by a (hydroxy)phthioceranoyl group during the biosynthesis of mycobacterial sulfolipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bhatt, K., Gurcha, S.S., Bhatt, A., Besra, G.S. and Jacobs, W.R., Jr. Two polyketide-synthase-associated acyltransferases are required for sulfolipid biosynthesis in Mycobacterium tuberculosis. Microbiology 153 (2007) 513–520. [PMID: 17259623]
2.  Kumar, P., Schelle, M.W., Jain, M., Lin, F.L., Petzold, C.J., Leavell, M.D., Leary, J.A., Cox, J.S. and Bertozzi, C.R. PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Proc. Natl. Acad. Sci. USA 104 (2007) 11221–11226. [PMID: 17592143]
[EC 2.3.1.283 created 2019]
 
 
EC 2.3.1.284     
Accepted name: 3′-(hydroxy)phthioceranyl-2′-palmitoyl(stearoyl)-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase
Reaction: 3 3′-(hydroxy)phthioceranyl-2′-palmitoyl(stearoyl)-2-O-sulfo-α,α-trehalose = 3,6,6′-tris-(hydroxy)phthioceranyl-2-palmitoyl(stearoyl)-2′-sulfo-α-alpha-trehalose + 2 2′-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose
Glossary: 3,6,6′-tris-(hydroxy)phthioceranyl-2-palmitoyl(stearoyl)-2′-sulfo-α-alpha-trehalose = a mycobacterial sulfolipid
Other name(s): chp1 (gene name)
Systematic name: 3′-(hydroxy)phthioceranyl-2′-palmitoyl(stearoyl)-2-O-sulfo-α,α-trehalose:3′-(hydroxy)phthioceranyl-2′-palmitoyl(stearoyl)-2-O-sulfo-α,α-trehalose 6,6′-di(hydroxy)phthioceranyltransferase
Comments: 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Seeliger, J.C., Holsclaw, C.M., Schelle, M.W., Botyanszki, Z., Gilmore, S.A., Tully, S.E., Niederweis, M., Cravatt, B.F., Leary, J.A. and Bertozzi, C.R. Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 287 (2012) 7990–8000. [PMID: 22194604]
[EC 2.3.1.284 created 2019]
 
 
EC 2.3.1.288     
Accepted name: 2-O-sulfo trehalose long-chain-acyltransferase
Reaction: (1) stearoyl-CoA + 2-O-sulfo-α,α-trehalose = 2-O-sulfo-2′-stearoyl-α,α-trehalose + CoA
(2) palmitoyl-CoA + 2-O-sulfo-α,α-trehalose = 2-O-sulfo-2′-palmitoyl-α,α-trehalose + CoA
Other name(s): papA2 (gene name)
Systematic name: acyl-CoA:2-O-sulfo-α,α-trehalose 2′-long-chain-acyltransferase
Comments: This mycobacterial enzyme catalyses the acylation of 2-O-sulfo-α,α-trehalose at the 2′ position by a C16 or C18 fatty acyl group during the biosynthesis of mycobacterial sulfolipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kumar, P., Schelle, M.W., Jain, M., Lin, F.L., Petzold, C.J., Leavell, M.D., Leary, J.A., Cox, J.S. and Bertozzi, C.R. PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Proc. Natl. Acad. Sci. USA 104 (2007) 11221–11226. [PMID: 17592143]
2.  Seeliger, J.C., Holsclaw, C.M., Schelle, M.W., Botyanszki, Z., Gilmore, S.A., Tully, S.E., Niederweis, M., Cravatt, B.F., Leary, J.A. and Bertozzi, C.R. Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 287 (2012) 7990–8000. [PMID: 22194604]
[EC 2.3.1.288 created 2019]
 
 
EC 2.8.2.37     
Accepted name: trehalose 2-sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + α,α-trehalose = adenosine 3′,5′-bisphosphate + 2-O-sulfo-α,α-trehalose
Glossary: 2-O-sulfo-α,α-trehalose = trehalose 2-sulfate = α-D-glucopyranosyl 2-O-sulfo-α-D-glucopyranoside
Other name(s): Stf0 sulfotransferase; 3′-phosphoadenylyl-sulfate:α,α-trehalose 2-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:α,α-trehalose 2-sulfonotransferase
Comments: The sulfation of trehalose in the bacterium Mycobacterium tuberculosis is required for the biosynthesis of sulfolipid-1.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mougous, J.D., Petzold, C.J., Senaratne, R.H., Lee, D.H., Akey, D.L., Lin, F.L., Munchel, S.E., Pratt, M.R., Riley, L.W., Leary, J.A., Berger, J.M. and Bertozzi, C.R. Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 11 (2004) 721–729. [DOI] [PMID: 15258569]
2.  Pi, N., Hoang, M.B., Gao, H., Mougous, J.D., Bertozzi, C.R. and Leary, J.A. Kinetic measurements and mechanism determination of Stf0 sulfotransferase using mass spectrometry. Anal. Biochem. 341 (2005) 94–104. [DOI] [PMID: 15866533]
[EC 2.8.2.37 created 2014]
 
 


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