Literature DB >> 1765122

A comparison of pyridoxal 5'-phosphate dependent decarboxylase and transaminase enzymes at a molecular level.

D M Smith1, N R Thomas, D Gani.   

Abstract

Pyridoxal 5'-phosphate is a coenzyme for a number of enzymes which catalyse reactions at C alpha of amino acid substrates including transaminases, decarboxylases and serine hydroxymethyltransferase. Using the X-ray coordinates for a transaminase, aspartate aminotransferase, and the results of stereochemical and mechanistic studies for decarboxylases and serine hydroxymethyltransferase, an active-site structure for the decarboxylase group is constructed. The structure of the active-site is further refined through active-site pyridoxyllysine peptide sequence comparison and a 3-D catalytic mechanism for the L-alpha-amino acid decarboxylases is proposed. The chemistry of serine hydroxymethyltransferase is re-examined in the light of the proposed decarboxylase mechanism.

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Year:  1991        PMID: 1765122     DOI: 10.1007/bf01918374

Source DB:  PubMed          Journal:  Experientia        ISSN: 0014-4754


  57 in total

1.  Pyridoxal 5'-phosphate-dependent histidine decarboxylase. Nucleotide sequence of the hdc gene and the corresponding amino acid sequence.

Authors:  G L Vaaler; M A Brasch; E E Snell
Journal:  J Biol Chem       Date:  1986-08-25       Impact factor: 5.157

2.  Stereospecific decarboxylation of specifically labeled carboxyl- 14 C aminomalonic acids by L-aspartate -decarboxylase.

Authors:  A G Palekar; S S Tate; A Meister
Journal:  Biochemistry       Date:  1971-05-25       Impact factor: 3.162

3.  Primary structure of mitochondrial aspartate aminotransferase from turkey liver. Cysteine-containing peptides.

Authors:  D Barra; F Martini; G Montarani; S Doonan; F Bossa
Journal:  FEBS Lett       Date:  1979-12-01       Impact factor: 4.124

4.  The cytosolic and mitochondrial aspartate aminotransferases from pig heart. A comparison of their primary structures, predicted secondary structures and some physical properties.

Authors:  D Barra; F Bossa; S Doonan; H M Fahmy; G J Hughes; F Martini; R Petruzzelli; B Wittmann-Liebold
Journal:  Eur J Biochem       Date:  1980-07

5.  The gene and the primary structure of ornithine decarboxylase from Saccharomyces cerevisiae.

Authors:  W A Fonzi; P S Sypherd
Journal:  J Biol Chem       Date:  1987-07-25       Impact factor: 5.157

6.  L-methionine decarboxylase from Dryopteris filix-mas: purification, characterization, substrate specificity, abortive transamination of the coenzyme, and stereochemical courses of substrate decarboxylation and coenzyme transamination.

Authors:  D E Stevenson; M Akhtar; D Gani
Journal:  Biochemistry       Date:  1990-08-21       Impact factor: 3.162

7.  Fern L-methionine decarboxylase: kinetics and mechanism of decarboxylation and abortive transamination.

Authors:  M Akhtar; D E Stevenson; D Gani
Journal:  Biochemistry       Date:  1990-08-21       Impact factor: 3.162

8.  Kinetic isotope effect studies on aspartate aminotransferase: evidence for a concerted 1,3 prototropic shift mechanism for the cytoplasmic isozyme and L-aspartate and dichotomy in mechanism.

Authors:  D A Julin; J F Kirsch
Journal:  Biochemistry       Date:  1989-05-02       Impact factor: 3.162

9.  Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis.

Authors:  C N Cronin; J F Kirsch
Journal:  Biochemistry       Date:  1988-06-14       Impact factor: 3.162

10.  Cloning and nucleotide sequence of rat ornithine decarboxylase cDNA.

Authors:  H J van Kranen; L van de Zande; C F van Kreijl; A Bisschop; B Wieringa
Journal:  Gene       Date:  1987       Impact factor: 3.688

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  1 in total

Review 1.  Controlling reaction specificity in pyridoxal phosphate enzymes.

Authors:  Michael D Toney
Journal:  Biochim Biophys Acta       Date:  2011-06-06
  1 in total

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