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Open AccessJournal ArticleDOI

Properties of the bound coenzyme and subunit structure of omega-amino acid:pyruvate aminotransferase.

K Yonaha, +2 more
- 25 Feb 1983 - 
- Vol. 258, Iss: 4, pp 2260-2265
TLDR
Circular dichroic spectrum suggests that the optical properties around the active site of the enzyme are similar to those of La-amino acid transaminase.
About
This article is published in Journal of Biological Chemistry.The article was published on 1983-02-25 and is currently open access. It has received 26 citations till now. The article focuses on the topics: Pyruvate dehydrogenase complex & Dihydrolipoyl transacetylase.

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Citations
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Journal ArticleDOI

Purification, characterization, and molecular cloning of a novel amine:pyruvate transaminase from Vibrio fluvialis JS17

TL;DR: The results suggest that theTransaminase from Vibrio fluvialis JS17 is a novel amine:pyruvate transaminase that has not been reported to date.
Journal ArticleDOI

One-pot synthesis of amino-alcohols using a de-novo transketolase and beta-alanine: pyruvate transaminase pathway in Escherichia coli.

TL;DR: Production of the β‐A:P TAm alongside the native transketolase (overexpressed from plasmid pQR411), in a single E.coli host, has created a novel biocatalyst capable of the synthesis of chiral amino alcohols via a synthetic two‐step pathway.
Journal ArticleDOI

Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination.

TL;DR: D-Amino acid aminotransferase was found in several thermophilic Bacillus species and purified to homogeneity from the best producer, Bacillus sp.
Journal ArticleDOI

Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia.

TL;DR: The encoding gene (tpa) encoded a 50-kDa peptide, which revealed 33% identity to diaminopelargonate aminotransferase from Bacillus subtilis, which indicates a homotetrameric structure.
Journal ArticleDOI

Structural studies of Pseudomonas and Chromobacterium ω-aminotransferases provide insights into their differing substrate specificity

TL;DR: The X-ray structures of two ω-aminotransferases from P. aeruginosa and C. violaceum in complex with an inhibitor offer the first detailed insight into the structural basis of the substrate specificity of these industrially important enzymes.
References
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Journal ArticleDOI

Spectroscopic determination of tryptophan and tyrosine in proteins.

Harold Edelhoch
- 01 Jul 1967 - 
TL;DR: A procedure is presented which strongly reduces or elimi- nates these interactions, normalizes their absorption, and consequently permits a more precise analysis of tryptophan and tyrosine in proteins.
Journal ArticleDOI

On the determination of cystine as cysteic acid.

TL;DR: In this article, a reduction agent was used to destroy the excess performic acid before the initial reaction, and the subsequent exposure of cysteic acid residues to bromine would not be likely to be detrimental.
Journal ArticleDOI

Human fibrinopeptides. Isolation, characterization and structure.

TL;DR: The structure of human fibrinogen and the specificity of thrombin is discussed, with a focus on the A-, AP- and Y-peptides.
Journal ArticleDOI

Thin-layer chromatography of PTH amino acids

TL;DR: A simple, rapid, and reliable technique for identifying small amounts of phenylthiohydantoin (PTH) derivatives has been developed for use in the analysis by Edman degradation ofsmall amounts of peptides isolated from fingerprints.
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