Substrate specificity, substrate channeling, and allostery in BphJ: an acylating aldehyde dehydrogenase associated with the pyruvate aldolase BphI
P Baker, J Carere, SYK Seah
Index: Baker, Perrin; Carere, Jason; Seah, Stephen Y. K. Biochemistry, 2012 , vol. 51, # 22 p. 4558 - 4567
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Citation Number: 9
Abstract
BphJ, a nonphosphorylating acylating aldehyde dehydrogenase, catalyzes the conversion of aldehydes to form acyl-coenzyme A in the presence of NAD+ and coenzyme A (CoA). The enzyme is structurally related to the nonacylating aldehyde dehydrogenases, aspartate-β- semialdehyde dehydrogenase and phosphorylating glyceraldehyde-3-phosphate dehydrogenase. Cys-131 was identified as the catalytic thiol in BphJ, and pH profiles ...
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