Literature DB >> 8038724

Kinetic characterization of tyramine oxidase of Arthrobacter species.

J Wouters1, P Perpète, P Hayen, N Anceau, F Durant.   

Abstract

Amine oxidases (EC 1.4.3) represent a rather nebulous group of proteins with relative narrow substrate and inhibitor specificities. Several different enzymes fall into these amine oxidase classes and the classification of some of them still remains ambiguous. Kinetic and physico-chemical properties of tyramine oxidase of Arthrobacter sp. were investigated to decide if this enzyme belongs to the flavin containing tyramine oxidase class (EC 1.4.3.9) or if it is more related to another amine oxidase class. On the basis of its spectral characteristics, molecular weight and inhibition profile, the enzyme was identified as a semicarbazide sensitive copper-containing amine oxidase.

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Year:  1994        PMID: 8038724

Source DB:  PubMed          Journal:  Biochem Mol Biol Int        ISSN: 1039-9712


  3 in total

Review 1.  Evolution of catabolic pathways: Genomic insights into microbial s-triazine metabolism.

Authors:  N Shapir; E F Mongodin; M J Sadowsky; S C Daugherty; K E Nelson; L P Wackett
Journal:  J Bacteriol       Date:  2006-11-17       Impact factor: 3.490

2.  Colorimetric-enzymatic determination of tyramine by generation of gold nanoparticles.

Authors:  Jesús Navarro; Susana de Marcos; Javier Galbán
Journal:  Mikrochim Acta       Date:  2020-02-18       Impact factor: 5.833

3.  Fluorinated phenylcyclopropylamines. Part 6: Effects of electron withdrawing or donating aryl substituents on the inhibition of tyramine oxidase from Arthrobacter sp. by diastereomeric 2-aryl-2-fluoro-cyclopropylamines.

Authors:  Svenja Hruschka; Shinichi Yoshida; Kenneth L Kirk; Günter Haufe
Journal:  J Fluor Chem       Date:  2008-09       Impact factor: 2.050

  3 in total

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