Reaction: NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate
Other name(s): GpgS protein; GPG synthase; glucosylphosphoglycerate synthase
Systematic name: NDP-glucose:3-phospho-D-glycerate 2-α-D-glucosyltransferase
Comments: The enzyme is involved in biosynthesis of 2-O-(α-D-glucopyranosyl)-D-glycerate via the two-step pathway in which glucosyl-3-phosphoglycerate synthase catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(α-D-glucopyranosyl)-D-glycerate by EC 3.1.3.85 glucosyl-3-phosphoglycerate phosphatase. The activity is dependent on divalent cations (Mn2+, Co2+, or Mg2+). The enzyme from Persephonella marina shows moderate flexibility on the sugar donor concerning the nucleotide moiety (UDP-glucose, ADP-glucose, GDP-glucose) but is strictly specific for glucose. The enzyme is also strictly specific for 3-phospho-D-glycerate as acceptor [1]. The enzyme from Methanococcoides burtonii is strictly specific for GDP-glucose and 3-phospho-D-glycerate [2]. This enzyme catalyses the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria [4,5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Costa, J., Empadinhas, N. and da Costa, M.S. Glucosylglycerate biosynthesis in the deepest lineage of the bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina. J. Bacteriol. 189 (2007) 1648-1654. [PMID: 17189358]
2. Costa, J., Empadinhas, N., Goncalves, L., Lamosa, P., Santos, H. and da Costa, M.S. Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii. J. Bacteriol. 188 (2006) 1022-1030. [PMID: 16428406]
3. Empadinhas, N., Albuquerque, L., Mendes, V., Macedo-Ribeiro, S. and da Costa, M.S. Identification of the mycobacterial glucosyl-3-phosphoglycerate synthase. FEMS Microbiol. Lett. 280 (2008) 195-202. [PMID: 18221489]
4. Pereira, P.J., Empadinhas, N., Albuquerque, L., Sa-Moura, B., da Costa, M.S. and Macedo-Ribeiro, S. Mycobacterium tuberculosis glucosyl-3-phosphoglycerate synthase: structure of a key enzyme in methylglucose lipopolysaccharide biosynthesis. PLoS One 3 (2008) e3748. [PMID: 19015727]
5. Gest, P., Kaur, D., Pham, H.T., van der Woerd, M., Hansen, E., Brennan, P.J., Jackson, M. and Guerin, M.E. Preliminary crystallographic analysis of GpgS, a key glucosyltransferase involved in methylglucose lipopolysaccharide biosynthesis in Mycobacterium tuberculosis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 1121-1124. [PMID: 19052364]
6. Kaur, D., Pham, H., Larrouy-Maumus, G., Riviere, M., Vissa, V., Guerin, M.E., Puzo, G., Brennan, P.J. and Jackson, M. Initiation of methylglucose lipopolysaccharide biosynthesis in mycobacteria. PLoS One 4 (2009) e544. [PMID: 19421329]