Kinetic characterization of tyramine oxidase of Arthrobacter species

J. Wouters, P. Perpete, P. Hayen, N. Anceau, F. Durant

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)737-743
Number of pages7
JournalBiochemistry and molecular biology international
Volume32
Issue number4
Publication statusPublished - 1 Jan 1994

Fingerprint

Arthrobacter
Monoamine Oxidase
Amines
Kinetics
Oxidoreductases
Enzymes
Amine Oxidase (Copper-Containing)
Substrate Specificity
Chemical properties
Molecular Weight
Molecular weight
Substrates
Proteins

Cite this

@article{9b4e074302b54d3ea1678e53846964ff,
title = "Kinetic characterization of tyramine oxidase of Arthrobacter species",
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.",
author = "J. Wouters and P. Perpete and P. Hayen and N. Anceau and F. Durant",
year = "1994",
month = "1",
day = "1",
language = "English",
volume = "32",
pages = "737--743",
journal = "Biochemistry and molecular biology international",
issn = "1039-9712",
publisher = "Academic Press Inc.",
number = "4",

}

Kinetic characterization of tyramine oxidase of Arthrobacter species. / Wouters, J.; Perpete, P.; Hayen, P.; Anceau, N.; Durant, F.

In: Biochemistry and molecular biology international, Vol. 32, No. 4, 01.01.1994, p. 737-743.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Kinetic characterization of tyramine oxidase of Arthrobacter species

AU - Wouters, J.

AU - Perpete, P.

AU - Hayen, P.

AU - Anceau, N.

AU - Durant, F.

PY - 1994/1/1

Y1 - 1994/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0028274906&partnerID=8YFLogxK

M3 - Article

C2 - 8038724

AN - SCOPUS:0028274906

VL - 32

SP - 737

EP - 743

JO - Biochemistry and molecular biology international

JF - Biochemistry and molecular biology international

SN - 1039-9712

IS - 4

ER -