| EC |
2.4.1.250 |
| Accepted name: |
D-inositol-3-phosphate glycosyltransferase |
| Reaction: |
UDP-N-acetyl-α-D-glucosamine + 1D-myo-inositol 3-phosphate = 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP |
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For diagram of mycothiol biosynthesis, click here |
| Glossary: |
mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol |
| Other name(s): |
mycothiol glycosyltransferases; 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 (configuration-retaining) |
| 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: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Newton, G.L., Koledin, T., Gorovitz, B., Rawat, M., Fahey, R.C. and Av-Gay, Y. The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA). J. Bacteriol. 185 (2003) 3476–3479. [DOI] [PMID: 12754249] |
| 2. |
Newton, G.L., Ta, P., Bzymek, K.P. and Fahey, R.C. Biochemistry of the initial steps of mycothiol biosynthesis. J. Biol. Chem. 281 (2006) 33910–33920. [DOI] [PMID: 16940050] |
| 3. |
Vetting, M.W., Frantom, P.A. and Blanchard, J.S. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis. J. Biol. Chem. 283 (2008) 15834–15844. [DOI] [PMID: 18390549] |
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| [EC 2.4.1.250 created 2010] |
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