Literature DB >> 8053675

Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases.

P A Tipton1, B S Beecher.   

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 M(r) 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. beta-Isopropylmalate is a substrate for tartrate dehydrogenase with a Km of 14 +/- 2 microM; 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.

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Year:  1994        PMID: 8053675     DOI: 10.1006/abbi.1994.1352

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  12 in total

1.  Functional prediction: identification of protein orthologs and paralogs.

Authors:  R Chen; S S Jeong
Journal:  Protein Sci       Date:  2000-12       Impact factor: 6.725

2.  Redesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase.

Authors:  R Chen; A Greer; A M Dean
Journal:  Proc Natl Acad Sci U S A       Date:  1996-10-29       Impact factor: 11.205

Review 3.  Microbial genome analysis: the COG approach.

Authors:  Michael Y Galperin; David M Kristensen; Kira S Makarova; Yuri I Wolf; Eugene V Koonin
Journal:  Brief Bioinform       Date:  2019-07-19       Impact factor: 11.622

4.  A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity.

Authors:  R Chen; A Greer; A M Dean
Journal:  Proc Natl Acad Sci U S A       Date:  1995-12-05       Impact factor: 11.205

5.  Induced fit and the catalytic mechanism of isocitrate dehydrogenase.

Authors:  Susana Gonçalves; Stephen P Miller; Maria A Carrondo; Anthony M Dean; Pedro M Matias
Journal:  Biochemistry       Date:  2012-08-27       Impact factor: 3.162

Review 6.  Combining solvent isotope effects with substrate isotope effects in mechanistic studies of alcohol and amine oxidation by enzymes.

Authors:  Paul F Fitzpatrick
Journal:  Biochim Biophys Acta       Date:  2014-10-30

7.  Sequence and mutational analysis of a tartrate utilization operon from Agrobacterium vitis.

Authors:  P Crouzet; L Otten
Journal:  J Bacteriol       Date:  1995-11       Impact factor: 3.490

8.  Escherichia coli D-malate dehydrogenase, a generalist enzyme active in the leucine biosynthesis pathway.

Authors:  Anastassia A Vorobieva; Mohammad Shahneawz Khan; Patrice Soumillion
Journal:  J Biol Chem       Date:  2014-08-26       Impact factor: 5.157

9.  The role of glutamate 87 in the kinetic mechanism of Thermus thermophilus isopropylmalate dehydrogenase.

Authors:  A M Dean; L Dvorak
Journal:  Protein Sci       Date:  1995-10       Impact factor: 6.725

10.  Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in Methanocaldococcus jannaschii.

Authors:  Randy M Drevland; Abdul Waheed; David E Graham
Journal:  J Bacteriol       Date:  2007-04-20       Impact factor: 3.490

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