1bh5
From Proteopedia
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(New page: 200px<br /> <applet load="1bh5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bh5, resolution 2.2Å" /> '''HUMAN GLYOXALASE I Q...)
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Revision as of 17:05, 29 October 2007
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HUMAN GLYOXALASE I Q33E, E172Q DOUBLE MUTANT
Overview
The Zn2+ ligands glutamate 99 and glutamate 172 in the active site of, human glyoxalase I were replaced, each in turn, by glutamines by, site-directed mutagenesis to elucidate their potential significance for, the catalytic properties of the enzyme. To compensate for the loss of the, charged amino acid residue, another of the metal ligands, glutamine 33, was simultaneously mutated into glutamate. The double mutants and the, single mutants Q33E, E99Q, and E172Q were expressed in Escherichia coli, purified on an S-hexylglutathione matrix, and characterized. Metal, analysis demonstrated that mutant Q33E/E172Q contained 1.0 mol of zinc/mol, of enzyme subunit, whereas mutant Q33E/E99Q contained only 0.3 mol of, zinc/mol of subunit. No catalytic activity could be detected with the, double ... [(full description)]
About this Structure
1BH5 is a [Single protein] structure of sequence from [Homo sapiens] with ZN and GTX as [ligands]. Active as [[1]], with EC number [4.4.1.5]. Full crystallographic information is available from [OCA].
Reference
Involvement of an active-site Zn2+ ligand in the catalytic mechanism of human glyoxalase I., Ridderstrom M, Cameron AD, Jones TA, Mannervik B, J Biol Chem. 1998 Aug 21;273(34):21623-8. PMID:9705294
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