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rdf:type |
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lifeskim:mentions |
umls-concept:C0001473,
umls-concept:C0020291,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0026882,
umls-concept:C0031603,
umls-concept:C0036226,
umls-concept:C0205103,
umls-concept:C0205431,
umls-concept:C0596235,
umls-concept:C1524003
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pubmed:issue |
1
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pubmed:dateCreated |
1999-3-11
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pubmed:abstractText |
Arg198 of sarcoplasmic reticulum Ca2+-ATPase was substituted with lysine, glutamine, glutamic acid, alanine, and isoleucine by site-directed mutagenesis. Kinetic analysis was performed with microsomal membranes isolated from COS-1 cells which were transfected with the mutated cDNAs. The rate of dephosphorylation of the ADP-insensitive phosphoenzyme was determined by first phosphorylating the Ca2+-ATPase with 32Pi and then diluting the sample with non-radioactive Pi. This rate was reduced substantially in the mutant R198Q, more strongly in the mutants R198A and R1981, and most strongly in the mutant R198E, but to a much lesser extent in R198K. The reduction in the rate of dephosphorylation was consistent with the observed decrease in the turnover rate of the Ca2+-ATPase accompanied by the steady-state accumulation of the ADP-insensitive phosphoenzyme formed from ATP. These results indicate that the positive charge and high hydrophilicity of Arg198 are critical for rapid hydrolysis of the ADP-insensitive phosphoenzyme.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
444
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
54-8
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:10037147-Adenosine Diphosphate,
pubmed-meshheading:10037147-Adenosine Triphosphate,
pubmed-meshheading:10037147-Amino Acid Substitution,
pubmed-meshheading:10037147-Animals,
pubmed-meshheading:10037147-Arginine,
pubmed-meshheading:10037147-Blotting, Western,
pubmed-meshheading:10037147-COS Cells,
pubmed-meshheading:10037147-Calcium-Transporting ATPases,
pubmed-meshheading:10037147-Hydrolysis,
pubmed-meshheading:10037147-Kinetics,
pubmed-meshheading:10037147-Microsomes,
pubmed-meshheading:10037147-Mutagenesis, Site-Directed,
pubmed-meshheading:10037147-Phosphates,
pubmed-meshheading:10037147-Phosphorylation,
pubmed-meshheading:10037147-Potassium,
pubmed-meshheading:10037147-Rabbits,
pubmed-meshheading:10037147-Sarcoplasmic Reticulum,
pubmed-meshheading:10037147-Transfection
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pubmed:year |
1999
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pubmed:articleTitle |
Mutations of Arg198 in sarcoplasmic reticulum Ca2+-ATPase cause inhibition of hydrolysis of the phosphoenzyme intermediate formed from inorganic phosphate.
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pubmed:affiliation |
Department of Biochemistry, Asahikawa Medical College, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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