Enzyme

Download
EC Tree
     2. Transferases
        2.4 Glycosyltransferases
            2.4.1 Hexosyltransferases
ID:2.4.1.269
Description:Mannosylglycerate synthase.
Cath: 3.90.550.10;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.1.269
BRENDA Enzyme Link: BRENDA 2.4.1.269
KEGG Enzyme Link: KEGG2.4.1.269
BioCyc Enzyme Link: BioCyc 2.4.1.269
ExPASy Enzyme Link: ExPASy2.4.1.269
EC2PDB Enzyme Link: EC2PDB 2.4.1.269
ExplorEnz Enzyme Link: ExplorEnz 2.4.1.269
PRIAM enzyme-specific profiles Link: PRIAM 2.4.1.269
IntEnz Enzyme Link: IntEnz 2.4.1.269
MEDLINE Enzyme Link: MEDLINE 2.4.1.269
MSA:

2.4.1.269;

Phylogenetic Tree:

2.4.1.269;

Uniprot:
M-CSA:
RHEA:30639 D-glycerate + GDP-alpha-D-mannose = 2-O-(alpha-D-mannosyl)-D-glycerate + GDP + H(+)
RULE(radius=1) [*:1]-[O;H0;+0:2]-[CH;+0:3](-[*:4])-[*:5].[*:6]-[OH;+0:7]>>[*:4]-[CH;+0:3](-[*:5])-[O;H0;+0:7]-[*:6].[*:1]-[OH;+0:2]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Substrate and metal ion promiscuity in mannosylglycerate synthase.Nielsen MM, Suits MD, Yang M, Barry CS, Martinez-Fleites C, Tailford LE, Flint JE, Dumon C, Davis BG, Gilbert HJ, Davies GJ2011 Apr 2921288903
Structural dissection and high-throughput screening of mannosylglycerate synthase.Flint J, Taylor E, Yang M, Bolam DN, Tailford LE, Martinez-Fleites C, Dodson EJ, Davis BG, Gilbert HJ, Davies GJ2005 Jul15951819
Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus. Biochemical and genetic characterization of a mannosylglycerate synthase.Martins LO, Empadinhas N, Marugg JD, Miguel C, Ferreira C, da Costa MS, Santos H1999 Dec 1010585410