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glutamate-cysteine ligase family protein
Most members of this family are glutamate-cysteine ligases. but the family also includes members such as YbdK from Escherichia coli K-12, a carboxylate-amine ligase whose glutamate-cysteine ligase activity is weak and may not be its physiologically relevant activity.
YbdK family carboxylate-amine ligase
This family of well-conserved proteins includes YbdK from E. coli K-12, which showed glutamate--cysteine ligase activity 500-fold slower than GshA from the same organism. Because the family is considered a putative glutamate--cysteine ligase by some, perhaps simply requiring a helper protein, it is also known as GCS2 (putative glutamate--cysteine ligase 2).
This family represents a division of a larger family, the other branch of which is predicted to act as glutamate--cysteine ligase (the first of two enzymes in glutathione biosynthesis) in the cyanobacteria. Species containing this protein, however, are generally not believe to make glutathione, and the function is unknown.
glutamate--cysteine ligase
glutamate--cysteine ligase catalyzes the first step in the biosynthesis of glutathione, forming a peptide bond between the CO group of the gamma-carboxyl of L-glutamate and an alpha-amino group of L-cysteine in an ATP- and Mg2+-dependent manner
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