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Human hypoxanthine-guanine phosphoribosyltransferase. Structural alteration in a dysfunctional enzyme variant (HPRTMunich) isolated from a patient with gout.
HPRTMunich is a mutant form of human hypoxanthine-guanine phosphoribosyltransferase that was isolated from a patient who presented with gout and a partial deficiency of enzyme activity. Profound abnormalities in the catalytic function of HPRTMunich are responsible for the deficiency of enzyme activity in vivo. Tryptic peptides of HPRTMunich were mapped by reverse phase high pressure liquid chromatography in an attempt to define the precise abnormality in its primary structure. Sequence analysis of aberrant peptides localized the structural alteration in HPRTMunich to residue 103. Several additional findings suggest that the mutation in this variant is most likely a serine to arginine substitution at residue 103. This amino acid substitution lies within the putative hypoxanthine-binding site of human hypoxanthine-guanine phosphoribosyltransferase possibly explaining its selective effect on intrinsic enzyme activity and binding of hypoxanthine.
PMID: 6706936 [PubMed - indexed for MEDLINE]
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Cited by 5 PubMed Central articles
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Ligation of high-melting-temperature 'clamp' sequence extends the scanning range of rare point-mutational analysis by constant denaturant capillary electrophoresis (CDCE) to most of the human genome.
Kim AS, Thilly WG.
Nucleic Acids Res. 2003 Aug 15; 31(16):e97.
[Nucleic Acids Res. 2003]
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A molecular survey of hypoxanthine-guanine phosphoribosyltransferase deficiency in man.
Wilson JM, Stout JT, Palella TD, Davidson BL, Kelley WN, Caskey CT.
J Clin Invest. 1986 Jan; 77(1):188-95.
[J Clin Invest. 1986]
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Resolution of a missense mutant in human genomic DNA by denaturing gradient gel electrophoresis and direct sequencing using in vitro DNA amplification: HPRT Munich.
Cariello NF, Scott JK, Kat AG, Thilly WG, Keohavong P.
Am J Hum Genet. 1988 May; 42(5):726-34.
[Am J Hum Genet. 1988]
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