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1tay

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[[Image:1tay.gif|left|200px]]
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{{STRUCTURE_1tay| PDB=1tay | SCENE= }}
{{STRUCTURE_1tay| PDB=1tay | SCENE= }}
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'''DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME'''
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===DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME===
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==Overview==
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The functional role of tyrosine-63 in the catalytic action of human lysozyme (EC 3.2.1.17) has been probed by site-directed mutagenesis. In order to identify the role of Tyr63 in the interaction with substrate, both the three-dimensional structures and the enzymatic functions of the mutants, in which Tyr63 was converted to phenylalanine, tryptophan, leucine, or alanine, have been characterized in comparison with those of the wild-type enzyme. X-ray crystallographical analysis of the mutant enzyme at not less than 1.77-A resolution indicated no remarkable change in tertiary structure except the side chain of 63rd residue. The conversion of Tyr63 to Phe or Trp did not change the enzymatic properties against the noncharged substrate (or substrate analogs) largely, while the conversion to Leu or Ala markedly reduced the catalytic activity to a few percent of wild-type enzyme. Kinetic analysis using p-nitrophenyl penta-N-acetyl-beta-(1----4)-chitopentaoside (PNP-(GlcNAc)5) as a substrate revealed that the reduction of activity should mainly be attributed to the reduction of affinity between enzyme and substrate. The apparent contribution of the phenolic hydroxyl group and the phenol group in the side chain of Tyr63 was estimated to 0.4 +/- 0.4 and 2.5 +/- 0.8 kcal mol-1, respectively. The result suggested that the direct contact between the planar side-chain group of Tyr63 and the sugar residue at subsite B is a major determinant of binding specificity toward a electrostatically neutral substrate in the catalytic action of human lysozyme.
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(as it appears on PubMed at http://www.pubmed.gov), where 1390708 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1390708}}
==About this Structure==
==About this Structure==
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[[Category: Jigami, Y.]]
[[Category: Jigami, Y.]]
[[Category: Muraki, M.]]
[[Category: Muraki, M.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:45:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:43:29 2008''

Revision as of 17:43, 27 July 2008

Image:1tay.png

Template:STRUCTURE 1tay

DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME

Template:ABSTRACT PUBMED 1390708

About this Structure

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

Reference

Dissection of the functional role of structural elements of tyrosine-63 in the catalytic action of human lysozyme., Muraki M, Harata K, Jigami Y, Biochemistry. 1992 Sep 29;31(38):9212-9. PMID:1390708

Page seeded by OCA on Sun Jul 27 20:43:29 2008

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