L-cysteine:1D-myo-inositol 2-amino-2-deoxy-α-D-glucopyranoside ligase
Identifiers
EC no.6.3.1.13
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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

  1. ^ Fan F, Luxenburger A, Painter GF, Blanchard JS (October 2007). "Steady-state and pre-steady-state kinetic analysis of Mycobacterium smegmatis cysteine ligase (MshC)". Biochemistry. 46 (40): 11421–9. doi:10.1021/bi7011492. PMC 2526253. PMID 17848100.
  2. ^ Gutierrez-Lugo MT, Newton GL, Fahey RC, Bewley CA (November 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" (PDF). Protein Expression and Purification. 50 (1): 128–36. doi:10.1016/j.pep.2006.07.005. PMID 16908186.
  3. ^ Tremblay LW, Fan F, Vetting MW, Blanchard JS (December 2008). "The 1.6 A crystal structure of Mycobacterium smegmatis MshC: the penultimate enzyme in the mycothiol biosynthetic pathway". Biochemistry. 47 (50): 13326–35. doi:10.1021/bi801708f. PMC 2628295. PMID 19053270.

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Enzymes: CO CS and CN ligases (EC 6.1-6.3)
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