PMID:10368300
| Citation |
Saadat, D and Harrison, DH (1999) The crystal structure of methylglyoxal synthase from Escherichia coli. Structure 7:309-17 |
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| Abstract |
The reaction mechanism of methylglyoxal synthase (MGS) is believed to be similar to that of triosephosphate isomerase (TIM). Both enzymes utilise dihydroxyacetone phosphate (DHAP) to form an enediol(ate) phosphate intermediate as the first step of their reaction pathways. However, the second catalytic step in the MGS reaction pathway is characterized by the elimination of phosphate and collapse of the enediol(ate) to form methylglyoxal instead of reprotonation to form the isomer glyceraldehyde 3-phosphate. |
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| Keywords |
Allosteric Regulation; Allosteric Site; Amino Acid Substitution; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Binding Sites; Carbon-Oxygen Lyases/chemistry; Carbon-Oxygen Lyases/genetics; Catalytic Domain; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/genetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphates/metabolism; Protein Conformation; Recombinant Fusion Proteins/chemistry |
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