RGD Reference Report - Identification of an amino acid residue involved in the substrate-binding site of rat liver uricase by site-directed mutagenesis. - Rat Genome Database

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Identification of an amino acid residue involved in the substrate-binding site of rat liver uricase by site-directed mutagenesis.

Authors: Ito, M  Kato, S  Nakamura, M  Go, M  Takagi, Y 
Citation: Ito M, etal., Biochem Biophys Res Commun. 1992 Aug 31;187(1):101-7.
RGD ID: 12859077
Pubmed: PMID:1520291   (View Abstract at PubMed)

Computer analysis has shown that a conserved amino acid sequence (Leu 160 to Lys 164) of rat liver uricase is also present in other enzymes with purine substrates. The significances of the amino acids in this sequence were studied by site-directed mutagenesis. Replacement of Lys 164 by Glu or Ile resulted in loss of uricase activity and decrease in binding of the competitive inhibitor xanthine. The far ultraviolet circular dichroic spectra of the mutant uricases were identical to that of the wild type protein, indicating that the replacement of Lys 164 by other amino acids did not result in serious modification of the conformation of uricase. These findings suggest that this amino acid is involved in the substrate-binding site of the enzyme.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
UoxRaturate catabolic process involved_inIDA PMID:1520291UniProt 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
UoxRaturate oxidase activity enablesIDA PMID:1520291UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Uox  (urate oxidase)


Additional Information