Source:http://linkedlifedata.com/resource/pubmed/id/18294854
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2008-4-14
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pubmed:abstractText |
The first activation study of the human carbonic anhydrase (hCA, EC 4.2.1.1) isoforms associated to tumors, hCA IX and XII, with a small library of natural and non-natural amino acids as well as aromatic/heterocyclic amines is reported. hCA IX was activated efficiently by dopamine, adrenaline and heterocyclic amines possessing aminoethyl-/aminomethyl-moieties (K(A)s of 9 nM-1.07 microM), whereas the best hCA XII activators were serotonin, L-adrenaline, 4-(2-aminoethyl)-morpholine and d-Phe (K(A) of 0.24-0.41 microM). Precise steric and electronic requirements are needed to be present in the molecules of effective hCA IX/hCA XII activators, in order to assure an adequate fit within the enzyme active site cavity for the formation of the enzyme-activator complex, and for an efficient proton transfer process within this complex, leading to the release of a proton and formation of the catalytically active, zinc-hydroxide species of the enzyme. Selective activation of these CA isoforms might be useful to develop pharmacologic tools or to understand whether some of these biogenic amines/amino acids may influence the progression of tumors overexpressing CA IX and/or CA XII.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amines,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/CA9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carbonic Anhydrases,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/carbonic anhydrase XII
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1464-3391
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3530-6
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pubmed:meshHeading |
pubmed-meshheading:18294854-Amines,
pubmed-meshheading:18294854-Amino Acids,
pubmed-meshheading:18294854-Antigens, Neoplasm,
pubmed-meshheading:18294854-Carbonic Anhydrases,
pubmed-meshheading:18294854-Conserved Sequence,
pubmed-meshheading:18294854-Enzyme Activation,
pubmed-meshheading:18294854-Humans,
pubmed-meshheading:18294854-Isoenzymes,
pubmed-meshheading:18294854-Kinetics,
pubmed-meshheading:18294854-Molecular Sequence Data,
pubmed-meshheading:18294854-Molecular Structure,
pubmed-meshheading:18294854-Neoplasms,
pubmed-meshheading:18294854-Sequence Alignment,
pubmed-meshheading:18294854-Structure-Activity Relationship
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pubmed:year |
2008
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pubmed:articleTitle |
Carbonic anhydrase activators: activation of the human tumor-associated isozymes IX and XII with amino acids and amines.
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pubmed:affiliation |
Centre of Molecular Medicine, Institute of Virology, Slovak Academy of Sciences, Dubravska Cesta 9, 84505 Bratislava, Slovak Republic.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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