N114S mutation causes loss of ATP-induced aggregation of human phosphoribosylpyrophosphate synthetase 1

Biochemical and Biophysical Research Communications

Volumn 379, Issue 4, 2009, Pages 1120-1125

  Liu, Honglin ^a   Peng, Xiaohui ^b,c   Zhao, Fang ^b   Zhang, Guobin ^a   Tao, Ye ^d   Luo, Zhaofeng ^b   Li, Yang ^b,c   Teng, Maikun ^b,c   Li, Xu ^b,c   Wei, Shiqiang ^a  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^b UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^c INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

^d INSTITUTE OF HIGH ENERGY PHYSICS   (China)

Author keywords

Aggregation effect; Allosteric inhibition; ATP; Phosphoribosylpyrophosphate synthetase 1; Secondary structure; Superactivity

Indexed keywords

ADENOSINE TRIPHOSPHATE; HYDROGEN; RIBOSEPHOSPHATE PYROPHOSPHOKINASE;

ALLOSTERISM; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; GOUT; HUMAN; HYDROGEN BOND; LIGHT SCATTERING; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; SYNCHROTRON RADIATION;

ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; ASPARAGINE; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; GOUT; HUMANS; HYDROGEN BONDING; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE; SERINE;

EID: 58949095599     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.01.034     Document Type: Article

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