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The enzyme from Escherichia coli consists of two alpha8-beta8 (TIM) barrels positioned face to face and thought to have evolved by gene duplication. [1] The active site lies between the tops of the two barrels, the N-terminal barrel binds 5-methyltetrahydropteroyltri-L-glutamic acid and the C-terminal barrel binds homocysteine. Homocysteine is ...
The 3 substrates of this enzyme are D-glycerate, NAD +, and NADP +, whereas its 4 products are hydroxypyruvate, NADH, NADPH, and H +. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD + or NADP + as acceptor. The systematic name of this enzyme class is D-glycerate:NADP + 2 ...
In enzymology, a glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) is an enzyme that catalyzes the chemical reaction. ATP + alpha-D-glucose 1-phosphate diphosphate + ADP-glucose. Thus, the two substrates of this enzyme are ATP and alpha-D-glucose 1-phosphate, whereas its two products are diphosphate and ADP-glucose.
In enzymology, a nucleoside deoxyribosyltransferase (EC 2.4.2.6) is an enzyme that catalyzes the chemical reaction. 2-deoxy-D-ribosyl-base 1 + base 2 2-deoxy-D-ribosyl-base 2 + base 1. Thus, the two substrates of this enzyme are 2-deoxy-D-ribosyl-base 1 and base 2, whereas its two products are 2-deoxy-D-ribosyl-base 2 and base 1.
In enzymology, a glutamate synthase (NADPH) (EC 1.4.1.13) is an enzyme that catalyzes the chemical reaction. L-glutamine + 2-oxoglutarate + NADPH + H + 2 L-glutamate + NADP + Thus, the four substrates of this enzyme are L-glutamine, 2-oxoglutarate (α-ketoglutarate), NADPH, and H +, whereas the two products are L-glutamate and NADP +.
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The systematic name of this enzyme class is acylphosphate phosphohydrolase. Other names in common use include acetylphosphatase, 1,3-diphosphoglycerate phosphatase, acetic phosphatase, Ho 1-3, and GP 1-3. This enzyme participates in 3 metabolic pathways: glycolysis / gluconeogenesis; pyruvate metabolism, and; benzoate degradation via coa ligation.
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