A catalytic mechanism for the enzyme benzylamine oxidase from pig plasma
نویسندگان
چکیده
منابع مشابه
Active-sitve titration of pig plasma benzylamine oxidase with phenylhydrazine.
Pig plasma benzylamine oxidase is a protein containing cupric copper and pyridoxal phosphate. The pyridoxal phosphate is stably linked to the enzyme. Discrepancies in the numbers of active sites per molecule of enzyme are reported in the literature. This paper shows that the fully active pure enzyme contains 3 mol of pyridoxal phosphate per mol, whereas enzymes with a lower specific activity ar...
متن کاملProperties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods.
Benzylamine oxidase from pig plasma has been studied by a variety of chemical and physical techniques. 1. Analytical ultracentrifugation, gel electrophoresis and isoelectric-focusing studies suggest that the enzyme is composed of two subunits with closely similar primary structures. 2. E.s.r. and n.m.r. measurements show that the enzyme contains two well-separated (greater than 0.6 nm) Cu2+ ion...
متن کاملEzCatDB: the Enzyme Catalytic-mechanism Database
The EzCatDB (Enzyme Catalytic-mechanism Database) specifically includes catalytic mechanisms of enzymes in terms of sequences and tertiary structures of enzymes, and proposed catalytic mechanisms, along with ligand structures. The EzCatDB groups enzyme data in the Protein Data Bank (PDB) and the SWISS-PROT database with identical domain compositions, Enzyme Commission (EC) numbers and catalytic...
متن کاملStudies on the active site of pig plasma amine oxidase.
Amine oxidase from pig plasma (PPAO) has two bound Cu2+ ions and at least one pyrroloquinoline quinone (PQQ) moiety as cofactors. It is shown that recovery of activity by copper-depleted PPAO is linear with respect to added Cu2+ ions. Recovery of e.s.r. and optical spectral characteristics of active-site copper parallel the recovery of catalytic activity. These results are consistent with both ...
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Attempts to obtain experimental values for the kinetic parameters of phenanthridine oxidation by guinea pig or rabbit liver aldehyde oxidase using common spectrophotometric methods have not been successful due to a lower limit of detection. In the present study, a new spectrofluorimetric assay in combination with a multivariate calibration method for enzymatic kinetic study of aldehyde oxidase ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1972
ISSN: 0306-3283
DOI: 10.1042/bj1300713