ExplorEnz: EC 2.5.1.145

Your query returned 1 entry. Printable version

2.5.1.145

Accepted name:

phosphatidylglycerol—prolipoprotein diacylglyceryl transferase

Reaction:

L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine = sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine

Other name(s):

lgt (gene name)

Systematic name:

L-1-phosphatidyl-sn-glycerol:[prolipoprotein]-L-cysteine diacyl-sn-glyceryltransferase

Comments:

This bacterial enzyme, which is associated with the membrane, catalyses the transfer of an sn-1,2-diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the prospective N-terminal cysteine of a prolipoprotein, the first step in the formation of mature triacylated lipoproteins.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Sankaran, K. and Wu, H.C. Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J. Biol. Chem. 269 (1994) 19701–19706. [PMID: 8051048]
2.	Qi, H.Y., Sankaran, K., Gan, K. and Wu, H.C. Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase: functionally significant conserved regions. J. Bacteriol. 177 (1995) 6820–6824. [PMID: 7592473]
3.	Gan, K., Sankaran, K., Williams, M.G., Aldea, M., Rudd, K.E., Kushner, S.R. and Wu, H.C. The umpA gene of Escherichia coli encodes phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling. J. Bacteriol. 177 (1995) 1879–1882. [PMID: 7896715]
4.	Sankaran, K., Gan, K., Rash, B., Qi, H.Y., Wu, H.C. and Rick, P.D. Roles of histidine-103 and tyrosine-235 in the function of the prolipoprotein diacylglyceryl transferase of Escherichia coli. J. Bacteriol. 179 (1997) 2944–2948. [PMID: 9139912]
5.	Pailler, J., Aucher, W., Pires, M. and Buddelmeijer, N. Phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments, and its essential residues are embedded in the membrane. J. Bacteriol. 194 (2012) 2142–2151. [DOI] [PMID: 22287519]

[EC 2.5.1.145 created 2018]