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Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases.
Zgiby SM, Thomson GJ, Qamar S, Berry A. Zgiby SM, et al. Among authors: berry a. Eur J Biochem. 2000 Mar;267(6):1858-68. doi: 10.1046/j.1432-1327.2000.01191.x. Eur J Biochem. 2000. PMID: 10712619 Free article.
Fructose 1,6-bisphosphate aldolase catalyses the reversible condensation of glycerone-P and glyceraldehyde 3-phosphate into fructose 1,6-bisphosphate. A recent structure of the Escherichia coli Class II fructose 1,6-bisphosphate aldolase [Hall, D.R., Leonard, G.A., …
Fructose 1,6-bisphosphate aldolase catalyses the reversible condensation of glycerone-P and glyceraldehyde 3-phosphate into fructose 1,6-bis …
Alternative proton donors/acceptors in the catalytic mechanism of the glutathione reductase of Escherichia coli: the role of histidine-439 and tyrosine-99.
Deonarain MP, Berry A, Scrutton NS, Perham RN. Deonarain MP, et al. Among authors: berry a. Biochemistry. 1989 Dec 12;28(25):9602-7. doi: 10.1021/bi00451a008. Biochemistry. 1989. PMID: 2558727
This reinforces our previous finding [Berry et al. (1989) Biochemistry 28, 1264-1269] that direct protonation and deprotonation of the histidine residue are not essential for the reaction to occur. The retention of catalytic activity by the H439A mutant demonstrates furthe …
This reinforces our previous finding [Berry et al. (1989) Biochemistry 28, 1264-1269] that direct protonation and deprotonation of th …
1,621 results