1z93: Difference between revisions

Revision as of 02:35, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1z93.png

Template:STRUCTURE 1z93

Human Carbonic Anhydrase III:Structural and Kinetic study of Catalysis and Proton Transfer.Human Carbonic Anhydrase III:Structural and Kinetic study of Catalysis and Proton Transfer.

Template:ABSTRACT PUBMED 16042381

About this StructureAbout this Structure

1Z93 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Human carbonic anhydrase III: structural and kinetic study of catalysis and proton transfer., Duda DM, Tu C, Fisher SZ, An H, Yoshioka C, Govindasamy L, Laipis PJ, Agbandje-McKenna M, Silverman DN, McKenna R, Biochemistry. 2005 Aug 2;44(30):10046-53. PMID:16042381

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Human Carbonic Anhydrase III:Structural and Kinetic study of Catalysis and Proton Transfer.'''
+===Human Carbonic Anhydrase III:Structural and Kinetic study of Catalysis and Proton Transfer.===
-==Overview==
+<!--
-The residue phenylalanine 198 (Phe 198) is a prominent cause of the lower activity of human carbonic anhydrase III (HCA III) compared with HCA II and other isozymes which have leucine at this site. We report the crystal structures of HCA III and the site-directed mutant F198L HCA III, both at 2.1 A resolution, and the enhancement of catalytic activity by exogenous proton donors containing imidazole rings. Both enzymes had a hexahistidine extension at the carboxy-terminal end, used to aid in purification, that was ordered in the crystal structures bound in the active site cavity of an adjacent symmetry-related enzyme. This observation allowed us to comment on a number of possible binding sites for imidazole and derivatives as exogenous proton donors/acceptors in catalysis by HCA III. Kinetic and structural evidence indicates that the phenyl side chain of Phe 198 in HCA III, about 5 A from the zinc, is a steric constriction in the active site, may cause altered interactions at the zinc-bound solvent, and is a binding site for the activation of catalysis by histidylhistidine. This suggests that sites of activation of the proton-transfer pathway in carbonic anhydrase are closer to the zinc than considered in previous studies.
+The line below this paragraph, {{ABSTRACT_PUBMED_16042381}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16042381}}
 ==About this Structure==
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 [[Category: Chemical rescue]]
 [[Category: Proton wire]]
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