Vancura, A., O'Connor, A., Patterson, S. D., Mirza, U., Chait, B. T., Kuret, J. (August 1993) Isolation and properties of YCK2, a Saccharomyces cerevisiae homolog of casein kinase-1. Arch Biochem Biophys, 305 (1). pp. 47-53. ISSN 0003-9861 (Print)
Abstract
A soluble fragment of YCK2, a casein kinase-1 isoform from Saccharomyces cerevisiae, has been purified and characterized in vitro. The procedure enriches enzyme activity to a final specific activity of 4.7 mumol min-1 mg-1 (when assayed with casein as substrate). Structural analysis reveals that the preparation arises from N-terminal modification and C-terminal proteolysis of the initially synthesized 546-residue protein, consisting of residues 2-495 +/- 1. Kinetic analysis demonstrates that YCK2 is similar to casein kinase-1 isolated from other organisms in its inability to use GTP as nucleotide substrate, in its sensitivity to heparin and ribofuranosyl-benzimidazole inhibitors, and in its peptide substrate selectivity. The enzyme is unusual, however, in that it is insensitive to the potent mammalian casein kinase-1 inhibitor N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide.
Item Type: | Paper |
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Uncontrolled Keywords: | Amino Acid Sequence Benzimidazoles/pharmacology Casein Kinase I Casein Kinases Chemistry, Physical Comparative Study Enzyme Stability Guanosine Triphosphate/metabolism Heparin/pharmacology Isoquinolines/pharmacology Kinetics Molecular Sequence Data Protein Kinases/chemistry/ isolation & purification/metabolism Research Support, U.S. Gov't, P.H.S. Saccharomyces cerevisiae/ enzymology Saccharomyces cerevisiae Proteins Substrate Specificity |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase biotechnology > chromatography > protein purification organism description > yeast |
CSHL Authors: | |
Communities: | CSHL labs > Stillman lab |
Depositing User: | Matt Covey |
Date: | 15 August 1993 |
Date Deposited: | 21 Apr 2016 18:25 |
Last Modified: | 21 Apr 2016 18:25 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/32484 |
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