Title of article
Tartrate Dehydrogenase, a New Member of the Family of Metal-Dependent Decarboxylating R-Hydroxyacid Dehydrogenases
Author/Authors
Tipton، نويسنده , , P.A. and Beecher، نويسنده , , B.S.، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 1994
Pages
7
From page
15
To page
21
Abstract
The gene encoding tartrate dehydrogenase has been cloned from Pseudomonas putida and sequenced. The gene is 1098 nucleotides long and encodes a protein 365 amino acids in length with a calculated Mr of 40,636. The gene and the protein encoded by it show strong homology to prokaryotic isopropylmalate dehydrogenases and, to a lesser extent, isocitrate dehydrogenase. Thus, tartrate dehydrogenase is the third member to be identified of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases which have an evolutionarily distinct NAD+-binding domain. The poor catalytic properties of tartrate dehydrogenase suggest that it has not been under strong selective pressure to maximize its ability to turn over (+)-tartrate for very long; the homology with isopropylmalate dehydrogenase makes it an attractive candidate for a recent progenitor of tartrate dehydrogenase. β-Isopropylmalate is a substrate for tartrate dehydrogenase with a Km of 14 ± 2 μM; it is turned over with a Vmax that is 35% of Vmax in the (+)-tartrate reaction. The gene encoding tartrate dehydrogenase has been expressed in Escherichia coli and large quantities of soluble enzyme can be obtained.
Journal title
Archives of Biochemistry and Biophysics
Serial Year
1994
Journal title
Archives of Biochemistry and Biophysics
Record number
1452260
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