L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase (EC 6.3.1.13, MshC, MshC ligase, Cys:GlcN-Ins ligase, mycothiol ligase) is an enzyme with systematic name L-cysteine:1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol ligase (AMP-forming).[1][2][3] This enzyme catalyses the following chemical reaction
- 1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + L-cysteine + ATP 1-O-[2-(L-cysteinamido)-2-deoxy-alpha-D-glucopyranosyl]-1D-myo-inositol + AMP + diphosphate
This enzyme is a key enzyme in the biosynthesis of mycothiol.
References
- ↑ Fan, F., Luxenburger, A., Painter, G.F. and Blanchard, J.S. (2007). "Steady-state and pre-steady-state kinetic analysis of Mycobacterium smegmatis cysteine ligase (MshC)". Biochemistry 46: 11421–11429. doi:10.1021/bi7011492. PMID 17848100.
- ↑ Gutierrez-Lugo, M.T., Newton, G.L., Fahey, R.C. and Bewley, C.A. (2006). "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: 128–136. doi:10.1016/j.pep.2006.07.005. PMID 16908186.
- ↑ Tremblay, L.W., Fan, F., Vetting, M.W. and Blanchard, J.S. (2008). "The 1.6 Å crystal structure of Mycobacterium smegmatis MshC: the penultimate enzyme in the mycothiol biosynthetic pathway". Biochemistry 47: 13326–13335. doi:10.1021/bi801708f. PMID 19053270.
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