Comparison of the Small Molecule Metabolic Enzymes of Escherichia coli and Saccharomyces cerevisiae

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Figure 4.
Figure 4.

Examples of internal duplication and domain shuffling. (a) The yeast lactoylglutathione lyase (glyoxalase I) consists of two domains of the Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase family, whereas the Escherichia coli enzyme consists of one domain and is active as a homodimer. (b) The yeast glutathione synthetase contains an additional N-terminal copy of the Glutathione ATP-binding domain-like family. It is known that theE. coli enzyme is a homotetramer.

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  1. Genome Res. 12: 916-929

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