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D-Serine dehydratase from Escherichia coli. Essential arginine residue at the pyridoxal 5'-phosphate binding site. by M N Kazarinoff; E E Snell is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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D-Serine apodehydratase from Escherichia coli is rapidly inactivated by butanedione in K+ borate buffer or by phenylglyoxal in K+ phosphate buffer at pH 8, 25 degrees. Pyridoxal-P protects against the inactivation. Modification of the apoenzyme abolishes its ability to bind the cofactor, pyridoxal-P, but the apparent Km for the substrate, D-serine, is not altered. The concentration dependence of the rate of butanedione inactivation in K+ borate buffer indicates that it is a two-step process with one butanedione bound per molecule of apoenzyme to give an inactive complex; half-maximal rate of inactivation is obtained at 37 mM butanedione. Butanedione inactivation is fully reversed following removal of excess reagent and borate. Similar studies with [14C]phenylglyoxal show that in the presence of pyridoxal-P at least 2 arginine residues may be modified without loss of activity. In the absence of pyridoxal-P modification of a single additional arginine residue results in loss of activity. Results with both inactivating reagents thus demonstrate that a critical arginine residue participates in binding of the coenzyme, pyridoxal-P. The stoichiometry of phenylglyoxal incorporation into t

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Author

M N Kazarinoff; E E Snell

Publisher

Elsevier BV

Published

1976

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)