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A minor species of a type I casein kinase from yeast phosphorylating threonine residues of protein substrate.

作者信息

Szyszka R, Kudlicki W, Grankowski N, Gasior E

出版信息

Biochim Biophys Acta. 1985 Jan 28;838(1):171-4. doi: 10.1016/0304-4165(85)90263-6.

DOI:10.1016/0304-4165(85)90263-6
PMID:3917689
Abstract

Protein kinase of Mr 23 000 was isolated from yeast and purified to apparent homogeneity. The enzyme preferentially phosphorylated casein and phosvitin in the presence of ATP as a phosphoryl donor. Its activity was neither affected by cyclic nucleotides nor by heparin. The kinase displayed practically the same substrate specificity as a typical casein kinase I from yeast (Kudlicki, W., Szyszka, R., Paleń, E. and Gasior, E. (1980) Biochim. Biophys. Acta 633, 376-385) except that it phosphorylated threonine instead of serine residues in protein substrates.

摘要

相似文献

1
A minor species of a type I casein kinase from yeast phosphorylating threonine residues of protein substrate.
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引用本文的文献

1
Fip1--an essential component of the Saccharomyces cerevisiae polyadenylation machinery is phosophorylated by protein kinase CK2.Fip1（酿酒酵母多聚腺苷酸化机制的一个重要组成部分）被蛋白激酶CK2磷酸化。
Mol Cell Biochem. 2006 Jun;286(1-2):191-7. doi: 10.1007/s11010-005-9104-4. Epub 2006 Feb 22.
2
Two genes in Saccharomyces cerevisiae encode a membrane-bound form of casein kinase-1.酿酒酵母中的两个基因编码酪蛋白激酶-1的膜结合形式。
Mol Biol Cell. 1992 Mar;3(3):275-86. doi: 10.1091/mbc.3.3.275.