1heb: Difference between revisions

Revision as of 08:04, 1 July 2008

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File:1heb.png

Template:STRUCTURE 1heb

STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE IISTRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II

Template:ABSTRACT PUBMED 8485129

About this StructureAbout this Structure

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

ReferenceReference

Structural consequences of hydrophilic amino acid substitutions in the hydrophobic pocket of human carbonic anhydrase II., Nair SK, Christianson DW, Biochemistry. 1993 May 4;32(17):4506-14. PMID:8485129

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-'''STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II'''
+===STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II===
-==Overview==
+<!--
-The three-dimensional structures of Leu-198--&gt;Glu, Leu-198--&gt;His, Leu-198--&gt;Arg, and Leu-198--&gt;Ala variants of human carbonic anhydrase II (CAII) have each been determined by X-ray crystallographic methods to a resolution of 2.0 A. The side chain of Leu-198 is located at the mouth of the active site hydrophobic pocket, and this pocket is required for substrate association. Hydrophobic--&gt;hydrophilic amino acid substitutions at the mouth of the pocket decrease kcat/KM for CO2 hydration: the CO2 hydrase activities of Leu-198--&gt;Glu, Leu-198--&gt;His, and Leu-198--&gt;Arg CAIIs are diminished 19-fold, 10-fold, and 17-fold, respectively, relative to the wild-type enzyme; however, the substitution of a compact aliphatic side chain for Leu-198 has a smaller effect on catalysis, in that Leu-198--&gt;Ala CAII exhibits only a 3-fold decrease in CO2 hydrase activity [Krebs, J. F., Rana, F., Dluhy, R. A., &amp; Fierke, C. A. (1993) Biochemistry (preceding paper in this issue)]. It is intriguing that CO2 hydrase activity is not severely diminished in Leu-198--&gt;Arg CAII, even though the side chain of Arg-198 blocks the hydrophobic pocket. Therefore, the bulky side chain of Arg-198 must be reasonably mobile in order to accommodate substrate association. Significantly, a residue larger than the wild-type Leu-198 side chain does not necessarily block the substrate association pocket; e.g., the side chain of Glu-198 packs against a hydrophobic patch, the net result of which is a wider mouth for the pocket.(ABSTRACT TRUNCATED AT 250 WORDS)
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 ==About this Structure==
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 [[Category: Christianson, D W.]]
 [[Category: Nair, S K.]]
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