ExplorEnz: EC 6.3.1.13

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6.3.1.13

Accepted name:

L-cysteine:1D-myo-inositol 2-amino-2-deoxy-α-D-glucopyranoside ligase

Reaction:

1-O-(2-amino-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol + L-cysteine + ATP = 1-O-[2-(L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol + AMP + diphosphate

For diagram of mycothiol biosynthesis, click here

Glossary:

mycothiol = 1-O-[2-(N²-acetyl-L-cysteinamido)-2-deoxy^--D-glucopyranosyl]-1D-myo-inositol

Other name(s):

MshC; MshC ligase; Cys:GlcN-Ins ligase; mycothiol ligase

Systematic name:

L-cysteine:1-O-(2-amino-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol ligase (AMP-forming)

Comments:

This enzyme is a key enzyme in the biosynthesis of mycothiol, a small molecular weight thiol found in Mycobacteria spp. and other actinomycetes. Mycothiol plays a fundamental role in these organisms by helping to provide protection from the effects of reactive oxygen species and electrophiles, including many antibiotics. The enzyme may represent a novel target for new classes of antituberculars [2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Fan, F., Luxenburger, A., Painter, G.F. and Blanchard, J.S. Steady-state and pre-steady-state kinetic analysis of Mycobacterium smegmatis cysteine ligase (MshC). Biochemistry 46 (2007) 11421–11429. [DOI] [PMID: 17848100]
2.	Gutierrez-Lugo, M.T., Newton, G.L., Fahey, R.C. and Bewley, C.A. Cloning, expression and rapid purification of active recombinant mycothiol ligase as B1 immunoglobulin binding domain of streptococcal protein G, glutathione-S-transferase and maltose binding protein fusion proteins in Mycobacterium smegmatis. Protein Expr. Purif. 50 (2006) 128–136. [DOI] [PMID: 16908186]
3.	Tremblay, L.W., Fan, F., Vetting, M.W. and Blanchard, J.S. The 1.6 Å crystal structure of Mycobacterium smegmatis MshC: the penultimate enzyme in the mycothiol biosynthetic pathway. Biochemistry 47 (2008) 13326–13335. [DOI] [PMID: 19053270]

[EC 6.3.1.13 created 2009]