Title : Site-directed mutagenesis of human myeloperoxidase: further identification of residues involved in catalytic activity and heme interaction.

Pub. Date : 1994 Jul 15

PMID : 8037771






2 Functional Relationships(s)
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1 Evidence for the involvement of four spatially clustered residues, Asp260(94), His261(95), Glu408(242) and Met409(243), in catalytic and spectral properties of human myeloperoxidase was provided by the analysis of site-directed mutants wherein these amino acids have been substituted by asparagine, alanine, glutamine and glutamine respectively. Glutamine myeloperoxidase Homo sapiens
2 Evidence for the involvement of four spatially clustered residues, Asp260(94), His261(95), Glu408(242) and Met409(243), in catalytic and spectral properties of human myeloperoxidase was provided by the analysis of site-directed mutants wherein these amino acids have been substituted by asparagine, alanine, glutamine and glutamine respectively. Glutamine myeloperoxidase Homo sapiens