1cj3: Difference between revisions

Revision as of 20:49, 30 June 2008

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File:1cj3.png

Template:STRUCTURE 1cj3

MUTANT TYR38GLU OF PARA-HYDROXYBENZOATE HYDROXYLASEMUTANT TYR38GLU OF PARA-HYDROXYBENZOATE HYDROXYLASE

Template:ABSTRACT PUBMED 10493859

About this StructureAbout this Structure

1CJ3 is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.

ReferenceReference

Switch of coenzyme specificity of p-hydroxybenzoate hydroxylase., Eppink MH, Overkamp KM, Schreuder HA, Van Berkel WJ, J Mol Biol. 1999 Sep 10;292(1):87-96. PMID:10493859

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 {{STRUCTURE_1cj3|  PDB=1cj3  |  SCENE=  }}
-'''MUTANT TYR38GLU OF PARA-HYDROXYBENZOATE HYDROXYLASE'''
+===MUTANT TYR38GLU OF PARA-HYDROXYBENZOATE HYDROXYLASE===
-==Overview==
+<!--
-p-Hydroxybenzoate hydroxylase (PHBH) is the archetype of the family of NAD(P)H-dependent flavoprotein aromatic hydroxylases. These enzymes share a conserved FAD-binding domain but lack a recognizable fold for binding the pyridine nucleotide. We have switched the coenzyme specificity of strictly NADPH-dependent PHBH from Pseudomonas fluorescens by site-directed mutagenesis. To that end, we altered the solvent exposed helix H2 region (residues 33-40) of the FAD-binding domain. Non-conservative selective replacements of Arg33 and Tyr38 weakened the binding of NADPH without disturbing the protein architecture. Introduction of a basic residue at position 34 increased the NADPH binding strength. Double (M2) and quadruple (M4) substitutions in the N-terminal part of helix H2 did not change the coenzyme specificity. By extending the replacements towards residues 38 and 40, M5 and M6 mutants were generated which were catalytically more efficient with NADH than with NADPH. It is concluded that specificity in P. fluorescens PHBH is conferred by interactions of Arg33, Tyr38 and Arg42 with the 2'-phosphate moiety of bound NADPH, and that introduction of an acidic group at position 38 potentially enables the recognition of the 2'-hydroxy group of NADH. This is the first report on the coenzyme reversion of a flavoprotein aromatic hydroxylase.
+The line below this paragraph, {{ABSTRACT_PUBMED_10493859}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10493859 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10493859}}
 ==About this Structure==
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 [[Category: Hydroxybenzoate]]
 [[Category: Oxidoreductase]]
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