Source:http://linkedlifedata.com/resource/pubmed/id/12069484
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2002-6-18
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| pubmed:abstractText |
A new model for catalysis of human carbonic anhydrase II is suggested. The model is based on the X-ray structure of the hydrogen bond network in the catalytic site. The outer part of the network is proposed to adjust the p K(a) of the catalytic site to the experimentally observed value of about 7. The inner part of the network is proposed to become a low-barrier hydrogen bond network in the transition state. The energy released in forming the low-barrier hydrogen bond network is used to catalyse the interconversion of CO(2) and HCO(3)(-). The suggested molecular mechanism is consistent with the generally accepted kinetic scheme for human carbonic anhydrase II.
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| 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 |
0022-5193
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2002 Elsevier Science Ltd. All rights reserved.
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| pubmed:issnType |
Print
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| pubmed:day |
21
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| pubmed:volume |
215
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
399-404
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| pubmed:dateRevised |
2004-11-17
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| pubmed:meshHeading | |
| pubmed:year |
2002
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| pubmed:articleTitle |
Hydrogen bonds and the catalytic mechanism of human carbonic anhydrase II.
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| pubmed:affiliation |
Alfred Wegener Institute for Polar and Marine Research, Bremerhaven, D-27515, Germany. sthoms@awi-bremerhaven.de
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| pubmed:publicationType |
Journal Article
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