Source:http://linkedlifedata.com/resource/pubmed/id/12686122
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2003-4-10
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pubmed:abstractText |
The mature copper amine oxidases (CAOs) contain a tyrosine-derived 2,4,5-trihydroxyphenylalanyl quinone (topa quinone or TPQ) and a cupric ion in close proximity. Through a combination of structural, spectroscopic and kinetic analyses, a chemical mechanism for the self-processing of an active site tyrosine to TPQ has been proposed. Once formed, TPQ acts as a switch between the heterolytic transformation of amine substrates to aldehydes, via a pyridoxal phosphate-like Schiff base complex, and one electron chemistry involving reduction of molecular oxygen. The relationship between the biogenetic and catalytic processes is discussed.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
1647
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
131-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading | |
pubmed:year |
2003
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pubmed:articleTitle |
The multi-functional topa-quinone copper amine oxidases.
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pubmed:affiliation |
Department of Chemistry, University of California, Berkeley, CA 94720, USA. klinman@socrates.berkeley.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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