Detail of "65189-71-1"

Reference

Protein kinase C phosphorylates the synthetic peptide Arg-Arg-Lys-Ala-Ser-Gly-Pro-Pro-Val in the presence of phospholipid plus either calcium or a phorbol ester tumor promoter

Protein kinase C phosphorylates the synthetic peptide Arg-Arg-Lys-Ala-Ser-Gly-Pro-Pro-Val in the presence of phospholipid plus either calcium or a phorbol ester tumor promoter. O'Brian, Catherine A.; Lawrence, David S.; Kaiser, E. Thomas; Weinstein, I. Bernard (Div. Environ. Sci., Columbia Univ., New York, NY 10032, USA). Biochem. Biophys. Res. Commun., 124(1), 296-302 (English) 1984. CODEN: BBRCA9. ISSN: 0006-291X. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) The synthetic nonapeptide Arg-Arg-Lys-Ala-Ser-Gly-Pro-Pro-Val [93511-94-5] is a substrate for in vitro phosphorylation by a partially purified prepn. of rat brain protein kinase C [9026-43-1], with a Km of ~130 mM. The closely related peptide kemptide [65189-71-1] was a much weaker substrate, bovine serum albumin was not a substrate and the peptide Arg-Arg-Lys-Ala-Ala-Gly-Pro-Pro-Val [93491-41-9] was a weak inhibitor of the enzyme. Protein kinase C-catalyzed phosphorylation of histone III-S and the nonapeptide are regulated by identical mechanisms since with both substrates the reaction required added phospholipid and either Ca (1 mM) or TPA (I) [16561-29-8] (200 nM). Thus, polypeptides contg. multiple basic residues followed by the sequence Ala-Ser can be substrates for TPA-stimulated phosphorylation by protein kinase C.

Resolution of a higher plant protein kinase similar to the catalytic subunit of cyclic AMP-dependent protein kinase

Resolution of a higher plant protein kinase similar to the catalytic subunit of cyclic AMP-dependent protein kinase. Polya, G. M.; Chung, R.; Menting, J. 65189-71-1 and 9026-43-1 are also occured in this study. (Dep. Biochem., La Trobe Univ., Bundoora 3083, Australia). Plant Sci. (Limerick, Irel.), 79(1), 37-45 (English) 1991. CODEN: PLSCE4. ISSN: 0168-9452. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) A protein kinase partially purified from petunia (Petunia hybrida var. Old Glory Blue) petals by cation exchange and gel filtration catalyzed the phosphorylation of kemptide (LRRASLG), a synthetic peptide substrate for cAMP-dependent protein kinase. The kemptide kinase (mol. wt., 30,000) (I) was a basic protein and was inhibited by the regulatory subunit of bovine cAMP-dependent protein kinase in a cAMP-reversible fashion as is the catalytic subunit of animal cAMP-dependent protein kinase. I was inhibited by prepns. of inhibitor proteins of mammalian cAMP-dependent protein kinase but was not affected by Ca2+-calmodulin, cAMP, or low concns. of heparin. I was Ca2+-independent. However, a basic Ca2+-dependent protein kinase (mol. wt., 50,000) that phosphorylates casein, histones, and myosin light chain-derived synthetic peptide (KKRAARATSNVFA-NH2), but not kemptide, was also present in petunia petals. .