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Literature DB >> 629766

The pyridoxal-binding site in pyridoxamine-pyruvate transaminase.

Abstract

The enzyme-substrate complex formed between pyridoxamine-pyruvate transaminase (EC 2.6.1.30) and pyridoxal was reduced with NaBH4. After carboxymethylation and tryptic digestion, pyridoxyl-lysine-containing peptides were isolated by a combination of Sephadex and Dowex 50 chromatography. Analysis of these peptides shows the structure around the pyridoxal-binding lysine residues to be Ala-Asp-Ile-Tyr-Val-Thr-Gly-Pro-Asx-Lys(Pxy)-Cys-Leu(Pro2, Gly2, Ala2, Met)(Thr, Leu2)Gly-Val-Ser-Glu-Arg. This structure differs from those found for the corresponding peptides from pyridoxal phosphate-dependent enzymes.

Entities: Chemical Mutation

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Year: 1978 PMID： 629766 PMCID： PMC1184184 DOI： 10.1042/bj1690429

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

17 in total

1. The complete amino acid sequence of cytoplasmic aspartate aminotransferase from pig heart.

Authors: Y A. Ovchinnikov; C A. Egorov; N A. Aldanova; M Y. Feigina; V M. Lipkin; N G. Abdulaev; E V. Grishin; A P. Kiselev; N N. Modyanov; A E. Braunstein; O L. Polyanovsky; V V. Nosikov
Journal: FEBS Lett Date: 1973-01-01 Impact factor: 4.124

2. PYRIDOXAMINE-PYRUVATE TRANSAMINASE. II. CHARACTERISTICS OF THE ENZYME.

Authors: W B DEMPSEY; E E SNELL
Journal: Biochemistry Date: 1963 Nov-Dec Impact factor: 3.162

3. REACTION OF PYRIDOXAMINE-PYRUVATE TRANSAMINASE WITH SULFHYDRYL REAGENTS.

Authors: M FUJIOKA; E E SNELL
Journal: J Biol Chem Date: 1965-07 Impact factor: 5.157

4. Enzymatic transamination of pyridoxamine. II. Crystalline pyridoxamine-pyruvate transaminase.

Authors: H WADA; E E SNELL
Journal: J Biol Chem Date: 1962-01 Impact factor: 5.157

5. [Amino acid determination on paper chromatograms].

Authors: J HEILMANN; J BARROLLIER; E WATZKE
Journal: Hoppe Seylers Z Physiol Chem Date: 1957

6. D-Serine dehydratase from Escherichia coli. IV. Comparative sequences of pyridoxylpeptides derived from the active site and from an inhibitory site of the enzyme.

Authors: Y Z Huang; E E Snell
Journal: J Biol Chem Date: 1972-11-25 Impact factor: 5.157

7. The chemical structure of tryptophanase from Escherichia coli. 3. Isolation and amino acid sequence of the tryptic peptides.

Authors: H Kagamiyama; H Matsubara; E E Snell
Journal: J Biol Chem Date: 1972-03-10 Impact factor: 5.157

The pyridoxal-binding site in pyridoxamine-pyruvate transaminase.

1. The complete amino acid sequence of cytoplasmic aspartate aminotransferase from pig heart.

2. PYRIDOXAMINE-PYRUVATE TRANSAMINASE. II. CHARACTERISTICS OF THE ENZYME.

3. REACTION OF PYRIDOXAMINE-PYRUVATE TRANSAMINASE WITH SULFHYDRYL REAGENTS.

4. Enzymatic transamination of pyridoxamine. II. Crystalline pyridoxamine-pyruvate transaminase.

5. [Amino acid determination on paper chromatograms].

6. D-Serine dehydratase from Escherichia coli. IV. Comparative sequences of pyridoxylpeptides derived from the active site and from an inhibitory site of the enzyme.

7. The chemical structure of tryptophanase from Escherichia coli. 3. Isolation and amino acid sequence of the tryptic peptides.

8. Hydrolysis of phenylthiohydantoins of amino acids.

9. Separation of dansyl-amino acids by polyamide layer chromatography.

10. Phenanthrenequinone as an analytical reagent for arginine and other monosubstituted guanidines.

1. Molecular cloning, expression and characterization of pyridoxamine-pyruvate aminotransferase.