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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2000-5-4
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pubmed:abstractText |
Many biochemical processes exploit the extraordinary versatility of flavoenzymes and their flavin cofactors. Flavoproteins are now known to have a variety of folding topologies but a careful examination of their structures suggests that there are recurrent features in their catalytic apparatus. The flavoenzymes that catalyse dehydrogenation reactions share a few invariant features in the hydrogen-bond interactions between their protein and flavin constituents. Similarly, the positioning of the reactive part of the substrate with respect to the cofactor is generally conserved. Modulation of substrate and cofactor reactivity and exact positioning of the substrate are key elements in the mode of action of these enzymes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Flavins,
http://linkedlifedata.com/resource/pubmed/chemical/Flavoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase (Cytochrome),
http://linkedlifedata.com/resource/pubmed/chemical/NADPH Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases Acting on CH-CH...,
http://linkedlifedata.com/resource/pubmed/chemical/dihydroorotate dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/glycollate oxidase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0968-0004
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
126-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10694883-Alcohol Oxidoreductases,
pubmed-meshheading:10694883-Binding Sites,
pubmed-meshheading:10694883-Catalysis,
pubmed-meshheading:10694883-Enzymes,
pubmed-meshheading:10694883-Flavins,
pubmed-meshheading:10694883-Flavoproteins,
pubmed-meshheading:10694883-Humans,
pubmed-meshheading:10694883-L-Lactate Dehydrogenase,
pubmed-meshheading:10694883-L-Lactate Dehydrogenase (Cytochrome),
pubmed-meshheading:10694883-NADPH Dehydrogenase,
pubmed-meshheading:10694883-Oxidoreductases,
pubmed-meshheading:10694883-Oxidoreductases Acting on CH-CH Group Donors,
pubmed-meshheading:10694883-Substrate Specificity
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pubmed:year |
2000
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pubmed:articleTitle |
Flavoenzymes: diverse catalysts with recurrent features.
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pubmed:affiliation |
Dept of Genetics and Microbiology, University of Pavia, via Abbiategrasso 207, 27100 Pavia, Italy.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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