Is the catalytic mechanism of bacteria, plant, and mammal copper-TPQ amine oxidases identical?

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1647, Issue 1-2, 2003, Pages 152-156

  Pietrangeli, P ^a   Nocera, S ^a   Mondovi B ^a   Morpurgo, L ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

Amine oxidase; Copper; Trihydroxyphenylalanine quinone (TPQ)

Indexed keywords

AMINE; AMINE OXIDASE (FLAVIN CONTAINING); AROMATIC COMPOUND; BENZYLHYDRAZINE; CARBONYL DERIVATIVE; COBALT; COPPER; DIETHYLDITHIOCARBAMIC ACID; HYDRAZIDE; HYDRAZINE DERIVATIVE; HYDROGEN; HYDROGEN PEROXIDE; ORGANIC COMPOUND; QUINONE DERIVATIVE; REAGENT; TRIHYDROXYPHENYLALANINEQUINONE; TYROSINE; UNCLASSIFIED DRUG; 2,4,5 TRIHYDROXYPHENYLALANINE QUINONE; 2,4,5-TRIHYDROXYPHENYLALANINE QUINONE; AMINE OXIDASE (COPPER CONTAINING); DOPA; DRUG DERIVATIVE; PROTEIN SUBUNIT;

BACTERIUM; BINDING AFFINITY; CATALYSIS; CATTLE; CHEMICAL BINDING; CONFERENCE PAPER; ENZYME ACTIVITY; ENZYME BINDING; HYDROGEN BOND; HYDROPHOBICITY; LENTIL; MAMMAL; NONHUMAN; OXIDATION; PLANT; PRIORITY JOURNAL; REACTION ANALYSIS; REDUCTION; SERUM; SPECTROSCOPY; STEADY STATE; CHEMISTRY; ENZYMOLOGY; METABOLISM; OXIDATION REDUCTION REACTION; REVIEW;

BOVINAE; LENS CULINARIS; MAMMALIA;

AMINE OXIDASE (COPPER-CONTAINING); BACTERIA; CATALYSIS; DIHYDROXYPHENYLALANINE; HYDROGEN PEROXIDE; OXIDATION-REDUCTION; PLANTS; PROTEIN SUBUNITS;

EID: 0038312048     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00083-9     Document Type: Conference Paper

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