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Novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus sp. strain OxB-1: purification, characterization, and molecular cloning of the gene.
Genetic evidence for a novel gene cluster that is responsible for aldoxime metabolism in this microorganism is provided, and the enzyme has been tentatively named phenylacetaldoxime dehydratase.
Distribution of Aldoxime Dehydratase in Microorganisms
It is shown that aldoxime dehydratase and nitrile-hydrolyzing activities are widely distributed among 188 ald oxime and 19 nitRIle degraders and that the enzymes were induced by a Aldoximes or nitriles.
A gene cluster responsible for alkylaldoxime metabolism coexisting with nitrile hydratase and amidase in Rhodococcus globerulus A-4.
The existence of an aldoxime dehydratase genetically linked with NHase and amidase, and responsible for the metabolism of alkylaldoxime in R. globerulus is reported here.
Properties of a novel D-stereospecific aminopeptidase from Ochrobactrum anthropi.
Comparing the Km and Vmax values for the major substrates, it is clear that the enzyme prefers peptides to amino acid arylamides or amino acid amides.
Identification of a set of genes involved in the formation of the substrate for the incorporation of the unusual "glycolate" chain extension unit in ansamitocin biosynthesis.
The unusual "glycolate" extender unit at C-9/C-10 of ansamitocin is not derived from 2-hydroxymalonyl-CoA or 2-methoxymaloneyl- CoA, but is formed from an acyl carrier protein (ACP)-bound substrate, possibly 2-Methoxylcysteamine-ACP.
Functional expression of genes involved in the biosynthesis of the novel polyketide chain extension unit, methoxymalonyl-acyl carrier protein, and engineered biosynthesis of
A subcluster of five genes from the ansamitocin biosynthetic gene cluster of Actinosynnema pretiosum was coexpressed in Streptomyces lividans with the genes encoding the 6-deoxyerythronolide B (6-DEB) synthase from Saccharopolyspora erythraea, indicating that asm13-17 are sufficient for synthesis of this unusual chain extension unit.
Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase.
This analysis resolves the conflict that had linked MAL to the histidine and phenylalanine ammonia lyase family of enzymes.
Purification and Characterization of Aldoxime Dehydratase of the Head Blight Fungus, Fusarium graminearum
  • Y. Kato, Y. Asano
  • Chemistry, Medicine
    Bioscience, biotechnology, and biochemistry
  • 1 January 2005
Fungal aldoxime dehydratase (Oxd) of Fusarium graminearum was purified and characterized for the first time from its overexpressing Escherichia coli transformant and belongs to a group of phenylacetaldoxime dehydrationases (EC, based on its substrate specificity and kinetic analysis.
Nitrile hydratase involved in aldoxime metabolism from Rhodococcus sp. strain YH3-3 purification and characterization.
Nitrile hydratase responsible for aldoxime metabolism from the E-pyridine-3-aldoxime degrading bacterium, Rhodococcus sp. strain YH3-3 was purified and characterized. Addition of cobalt ion was