Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
A Novel NADP+-dependent Serine Dehydrogenase from Agrobacterium tumefaciens
Emran Kabir ChowdhuryKazuhiko HiguchiShinji NagataHaruo Misono
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JOURNAL FREE ACCESS

1997 Volume 61 Issue 1 Pages 152-157

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Abstract

NADP-dependent serine dehydrogenase [EC 1.1.1.-], which catalyzes the oxidation of the hydroxyl group of serine to form 2-aminomalonate semialdehyde, was purified to homogeneity from a crude extract of Agrobacterium tumefaciens ICR 1600. The enzyme had a molecular mass of about 100 kDa and consisted of four identical subunits. In addition to L-serine, D-serine, L-glycerate, D-glycerate, and 2-methyl-DL-serine were substrates. However, O-methyl-DL-serine and L-threonine were inert. The enzyme showed maximal activity at about pH 9 for the oxidation of L-serine. The enzyme required NADP as a coenzyme, NAD was inert. The enzyme was not inhibited by EDTA, o-phenanthroline, or α, α'-dipyridyl, but was inhibited by HgCI2, p-chloromercuribenzoate, L-cysteine, D-cysteine, malonate, 2-methylmalonate, and tartronate. The Michaelis constants for L-serine, D-serine, and NADP were 42, 44, and 0.029 mM, respectively.

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