EC 2.4.1.250 - D-inositol-3-phosphate glycosyltransferase

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IntEnz Enzyme Nomenclature
EC 2.4.1.250

Names

Accepted name:
D-inositol-3-phosphate glycosyltransferase
Other names:
N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase
mycothiol glycosyltransferase
MshA
UDP-N-acetyl-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase
Systematic name:
UDP-N-acetyl-α-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase (conformation-retaining)

Reaction

Comments:

The enzyme, which belongs to the GT-B fold superfamily, catalyses the first dedicated reaction in the biosynthesis of mycothiol [1]. The substrate was initially believed to be inositol, but eventually shown to be D-myo-inositol 3-phosphate [2]. A substantial conformational change occurs upon UDP binding, which generates the binding site for D-myo-inositol 3-phosphate [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102710
UniProtKB/Swiss-Prot: (70) [show] [UniProt]

References

  1. Newton, G. L., Koledin, T., Gorovitz, B., Rawat, M., Fahey, R. C., Av-Gay, Y.
    The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA).
    J. Bacteriol. 185: 3476-3479 (2003). [PMID: 12754249]
  2. Newton, G. L., Ta, P., Bzymek, K. P., Fahey, R. C.
    Biochemistry of the initial steps of mycothiol biosynthesis.
    J. Biol. Chem. 281: 33910-33920 (2006). [PMID: 16940050]
  3. Vetting, M. W., Frantom, P. A., Blanchard, J. S.
    Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis.
    J. Biol. Chem. 283: 15834-15844 (2008). [PMID: 18390549]

[EC 2.4.1.250 created 2010]