Post-translational phosphorylation of serine 74 of human deoxycytidine kinase favors the enzyme adopting the open conformation making it competent for nucleoside binding and release

Biochemistry

Volumn 50, Issue 14, 2011, Pages 2870-2880

  Hazra, Saugata ^a   Szewczak, Andrzej ^b   Ort, Stephan ^b   Konrad, Manfred ^b   Lavie, Arnon ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^b MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING AND RELEASE; CATALYTIC CYCLES; CATALYTIC PROPERTIES; GLUTAMIC ACID; IN-VIVO; KINETIC PROPERTIES; OPEN CONFORMATION; PHOSPHORYL TRANSFER; PRODUCT RELEASE; REACTION SCHEMES; SIDE CHAINS; WILD TYPES;

BIOMOLECULES; ENZYMES; PHOSPHORYLATION;

AMINO ACIDS;

DEOXYCYTIDINE KINASE; ENZYME VARIANT; GLUTAMIC ACID; INDOLE; NUCLEOSIDE; SERINE; TRYPTOPHAN;

ARTICLE; CATALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME PHOSPHORYLATION; ENZYME RELEASE; ENZYME STRUCTURE; ENZYME SUBSTRATE; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; STEADY STATE; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; BIOCATALYSIS; DEOXYCYTIDINE KINASE; GLUTAMIC ACID; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEOSIDES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SERINE;

EID: 79953673896     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2001032     Document Type: Article

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