Reactivity of Cdc25 phosphatase at low pH and with thiophosphorylated protein substrate

Bioorganic Chemistry

Volumn 33, Issue 4, 2005, Pages 264-273

  Rudolph, Johannes ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

Cdc25; Cdk; Cyclin; pH dependence; Phosphatase; Thiophosphate

Indexed keywords

CELL CYCLE PROTEIN; CELL CYCLE PROTEIN 25; PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SUBSTRATE; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN PHOSPHORYLATION; PROTON TRANSPORT;

CDC25 PHOSPHATASE; CYCLIN A; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR STRUCTURE; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN BINDING; SUBSTRATE SPECIFICITY; SULFHYDRYL COMPOUNDS;

EUKARYOTA;

EID: 21844441159     PISSN: 00452068     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioorg.2005.01.004     Document Type: Article

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