2hkk
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(New page: 200px<br /> <applet load="2hkk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hkk, resolution 1.90Å" /> '''Carbonic anhydrase ...)
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Revision as of 20:26, 12 November 2007
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Carbonic anhydrase activators: Solution and X-ray crystallography for the interaction of andrenaline with various carbonic anhydrase isoforms
Contents |
Overview
The activation of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1), with L-adrenaline and histamine has been investigated by kinetic and X-ray, crystallographic studies. L-Adrenaline behaves as a potent activator of, isozyme CA I (activation constant of 90 nM), being a much weaker activator, of isozyme CA II (activation constant of 96 microM). Isoforms CA IV, VA, VII, and XIV were activated by L-adrenaline with K(A)s in the range of, 36-63 microM. The X-ray crystal structure of the CA II-L-adrenaline adduct, revealed that the activator plugs the entrance of the active site cavity, obstructing it almost completely.
Disease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this Structure
2HKK is a Single protein structure of sequence from Homo sapiens with ZN, HG and ALE as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
Reference
Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV., Temperini C, Innocenti A, Scozzafava A, Mastrolorenzo A, Supuran CT, Bioorg Med Chem Lett. 2007 Feb 1;17(3):628-35. Epub 2006 Nov 15. PMID:17127057
Page seeded by OCA on Mon Nov 12 22:33:25 2007
