Literature DB >> 8690703

Pyridoxal enzymes: mechanistic diversity and uniformity.

H Hayashi1.   

Abstract

Pyridoxal 5'-phosphate (PLP) acts as the coenzyme in a vast number of reactions in amino acid metabolism. The study of PLP enzymes is one of the most fascinating frontiers in enzymology, and now the mechanism s of several types of PLP enzymes are being discussed at the atomic level based on crystallographic, spectroscopic, and site-directed mutagenesis studies. In this review, I summarize the important findings, including those provided by classical studies, on the reaction mechanisms of several PLP enzymes, with the intention of discussing the chemically and thermodynamically consistent principle of the catalytic action of PLP enzymes common to all the enzymes of this group, and the uniqueness of individual enzymes that endows them substrate and reaction specificity.

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Year:  1995        PMID: 8690703     DOI: 10.1093/oxfordjournals.jbchem.a124931

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  34 in total

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3.  Strain relief at the active site of phosphoserine aminotransferase induced by radiation damage.

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5.  Crystallization and preliminary X-ray diffraction studies of the (R)-selective amine transaminase from Aspergillus fumigatus.

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6.  Cloning, expression, purification, crystallization and X-ray crystallographic analysis of Rv2606c from Mycobacterium tuberculosis H37Rv.

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8.  The C-terminus of rat L-histidine decarboxylase specifically inhibits enzymic activity and disrupts pyridoxal phosphate-dependent interactions with L-histidine substrate analogues.

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9.  Evolution of threonine aldolases, a diverse family involved in the second pathway of glycine biosynthesis.

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Journal:  J Mol Evol       Date:  2015-02-03       Impact factor: 2.395

10.  Integrating metabolomics and transcriptomics data to discover a biocatalyst that can generate the amine precursors for alkamide biosynthesis.

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