Kinetic mechanistic studies of wild-type leucine-rich repeat kinase2: Characterization of the kinase and GTPase activities

Biochemistry

Volumn 49, Issue 9, 2010, Pages 2008-2017

  Liu, Min ^a   Dobson, Brittany ^a   Glicksman, Marcie A ^a   Yue, Zhenyu ^b   Stein, Ross L ^c  

^a The Harvard Center for Neurodegeneration & Repair   (United States)

^b MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^c GLAXOSMITHKLINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; ENZYMATIC PROPERTIES; GTP HYDROLYSIS; GTPASE ACTIVITY; INHIBITION MECHANISMS; INITIAL VELOCITIES; KINASE ACTIVITY; KINASE INHIBITORS; KINETIC MECHANISM; LEUCINE-RICH REPEATS; MECHANISTIC STUDIES; MOLAR FRACTIONS; NUCLEOTIDE ANALOGUES; PARKINSON'S DISEASE; PEPTIDE SUBSTRATES; RANDOM MECHANISMS; RAPID EQUILIBRIUM; RATE LIMITING; SUBSTRATE BINDING; WILD-TYPE LEUCINE;

AMINO ACIDS; BINDING ENERGY; ENZYME INHIBITION; HYDROLYSIS; PEPTIDES; PHOSPHORYLATION;

SUBSTRATES;

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; GUANOSINE DIPHOSPHATE; GUANOSINE PHOSPHATE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; LDN 73794; LEUCINE RICH REPEAT KINASE 2; PHOSPHOTRANSFERASE INHIBITOR; POLO LIKE KINASE; PURINE NUCLEOSIDE PHOSPHORYLASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CATALYSIS; DRUG IDENTIFICATION; DRUG SCREENING; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME INHIBITION; ENZYME KINETICS; ENZYME SUBSTRATE; FLUORESCENCE RESONANCE ENERGY TRANSFER; HYDROLYSIS; IC 50; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; STEADY STATE; WILD TYPE;

AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; FLUORESCENCE RESONANCE ENERGY TRANSFER; GTP PHOSPHOHYDROLASES; HUMANS; MICE; MICE, TRANSGENIC; MOLECULAR SEQUENCE DATA; PARKINSON DISEASE; PHOSPHORYLATION; PROTEIN KINASE INHIBITORS; PROTEIN-SERINE-THREONINE KINASES; SUBSTRATE SPECIFICITY;

MURINAE;

EID: 77749255337     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi901851y     Document Type: Article

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