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phosphopyruvate hydratase
phosphopyruvate hydratase (enolase) catalyzes the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways
Enolase (phosphopyruvate hydratase, EC 4.2.1.11) is a widely distributed cytosolic enzyme with a critical role in glycolysis. In bacteria, it occurs in nearly every species. Enolases from multiple lineages have been reported to exhibit surface expression and to have virulence-related moonlighting functions, such as binding to fibrinogen or other host proteins.
Methylaspartate ammonia-lyase C-terminus
Methylaspartate ammonia-lyase EC:4.3.1.2 catalyses the second step of fermentation of glutamate. It is a homodimer. This family represents the C-terminal region of Methylaspartate ammonia-lyase and contains a TIM barrel fold similar to the Pfam:PF01188. This family represents the catalytic domain and contains a metal binding site [2]. [1]. 1420191. Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein. Goda SK, Minton NP, Botting NP, Gani D;. Biochemistry 1992;31:10747-10756. [2]. 11748244. The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step. Asuncion M, Blankenfeldt W, Barlow JN, Gani D, Naismith JH;. J Biol Chem 2002;277:8306-8311. (from Pfam)
Enolase, N-terminal domain
Enolase, C-terminal TIM barrel domain
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