| pubmed-article:1898739 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1898739 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:1898739 | lifeskim:mentions | umls-concept:C0007035 | lld:lifeskim |
| pubmed-article:1898739 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:1898739 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:1898739 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:1898739 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1898739 | pubmed:dateCreated | 1991-2-12 | lld:pubmed |
| pubmed-article:1898739 | pubmed:abstractText | We have found that many dianionic species, at millimolar concentrations, significantly activate or inhibit the bovine carbonic anhydrase III-catalyzed hydration of CO2. Dianionic species such as HPO2-4 and SO2-3, with pKb values near 7, are activators, whereas weakly basis species such as SO2-4 act as inhibitors. Both activation and inhibition are partial hyperbolic in nature and do not appear to compete with monoanionic linear inhibitors like N-3. Our kinetic data are consistent with a formal mechanism of action for carbonic anhydrase III that is directly analogous to that of carbonic anhydrase II, in which Lys-64 of carbonic anhydrase III can act as an intramolecular H+ transfer group during CO2 hydration. Our data suggest that dianionic inhibitors depress the rate of H+ transfer during turnover by stabilizing the protonated form of Lys-64. We postulate that dianionic activators enhance the rate of a rate-limiting H+ transfer step in the mechanism, probably by acting directly as H+ acceptors. | lld:pubmed |
| pubmed-article:1898739 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1898739 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1898739 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1898739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1898739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1898739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1898739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1898739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1898739 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1898739 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1898739 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1898739 | pubmed:author | pubmed-author:JacksonJ MJM | lld:pubmed |
| pubmed-article:1898739 | pubmed:author | pubmed-author:CorbettA HAH | lld:pubmed |
| pubmed-article:1898739 | pubmed:author | pubmed-author:RowlettR SRS | lld:pubmed |
| pubmed-article:1898739 | pubmed:author | pubmed-author:GargiuloN... | lld:pubmed |
| pubmed-article:1898739 | pubmed:author | pubmed-author:SantoliF AFA | lld:pubmed |
| pubmed-article:1898739 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1898739 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1898739 | pubmed:volume | 266 | lld:pubmed |
| pubmed-article:1898739 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1898739 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1898739 | pubmed:pagination | 933-41 | lld:pubmed |
| pubmed-article:1898739 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1898739 | pubmed:meshHeading | pubmed-meshheading:1898739-... | lld:pubmed |
| pubmed-article:1898739 | pubmed:meshHeading | pubmed-meshheading:1898739-... | lld:pubmed |
| pubmed-article:1898739 | pubmed:meshHeading | pubmed-meshheading:1898739-... | lld:pubmed |
| pubmed-article:1898739 | pubmed:meshHeading | pubmed-meshheading:1898739-... | lld:pubmed |
| pubmed-article:1898739 | pubmed:meshHeading | pubmed-meshheading:1898739-... | lld:pubmed |
| pubmed-article:1898739 | pubmed:meshHeading | pubmed-meshheading:1898739-... | lld:pubmed |
| pubmed-article:1898739 | pubmed:meshHeading | pubmed-meshheading:1898739-... | lld:pubmed |
| pubmed-article:1898739 | pubmed:meshHeading | pubmed-meshheading:1898739-... | lld:pubmed |
| pubmed-article:1898739 | pubmed:meshHeading | pubmed-meshheading:1898739-... | lld:pubmed |
| pubmed-article:1898739 | pubmed:meshHeading | pubmed-meshheading:1898739-... | lld:pubmed |
| pubmed-article:1898739 | pubmed:meshHeading | pubmed-meshheading:1898739-... | lld:pubmed |
| pubmed-article:1898739 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1898739 | pubmed:articleTitle | Activation and inhibition of bovine carbonic anhydrase III by dianions. | lld:pubmed |
| pubmed-article:1898739 | pubmed:affiliation | Department of Chemistry, Colgate University, Hamilton, New York 13346. | lld:pubmed |
| pubmed-article:1898739 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1898739 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:1898739 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1898739 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1898739 | lld:pubmed |
