Brain histone kinase: The structure, the substrate specificity and the mechanism of action

1976 ◽  
Vol 14 ◽  
pp. 407-444 ◽  
Author(s):  
E.S. Severin ◽  
M.V. Nesterova ◽  
N.N. Gulyaev ◽  
S.V. Shlyapnikov
Keyword(s):  
Substrate Specificity ◽  
Mechanism Of Action ◽  
Histone Kinase

scholarly journals Aldehyde Dehydrogenase Inhibitors: a Comprehensive Review of the Pharmacology, Mechanism of Action, Substrate Specificity, and Clinical Application

2012 ◽  
Vol 64 (3) ◽  
pp. 520-539 ◽  
Author(s):  
Vindhya Koppaka ◽  
David C. Thompson ◽  
Ying Chen ◽  
Manuel Ellermann ◽  
Kyriacos C. Nicolaou ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Clinical Application ◽  
Aldehyde Dehydrogenase ◽  
Mechanism Of Action ◽  
Comprehensive Review

Properties of Chlorophyllase from Capsicum annuum L. Fruits

2001 ◽  
Vol 56 (11-12) ◽  
pp. 1015-1021 ◽  
Author(s):  
Dámaso Hornero-Méndez ◽  
María Isabel Mínguez-Mosquera
Keyword(s):  
Substrate Specificity ◽  
Capsicum Annuum ◽  
Mechanism Of Action ◽  
Substrate Recognition ◽  
Substrate Inhibition ◽  
Inhibitory Effect ◽  
Hplc Separation ◽  
Substrate Complex ◽  
Enzyme Substrate

Abstract The in vitro properties of semi-purified chlorophyllase (chlorophyll-chlorophyllido hy­drolase, EC 3.1.1.14) from Capsicum annuum fruits have been studied. The enzym e showed an optimum of activity at pH 8.5 and 50 °C. Substrate specificity was studied for chlorophyll (Chi) a, Chi b, pheophytin (Phe) a and Phe b, with Km values of 10.70, 4.04, 2.67 and 6.37 μᴍ respectively. Substrate inhibition was found for Phe b at concentrations higher than 5 μᴍ. Chlorophyllase action on Chi a' and Chi b' was also studied but no hydrolysis was observed, suggesting that the mechanism of action depends on the configuration at C-132 in the chloro­ phyll molecule, with the enzyme acting only on compounds with R132 stereochemistry. The effect of various metals (Mg2+, Hg2+, Cu2+, Zn2+, Co , Fe2+ and Fe3+) was also investigated, and a general inhibitory effect was found, this being more marked for Hg2+ and Fe2+. Func­tional groups such as -SH and -S-S-seem ed to participate in the formation o f the enzyme-substrate complex. Chelating ion and the carbonyl group at C3 appeared to be important in substrate recognition by the enzyme. The method for measuring Chlase activity, including HPLC separation of substrate and product, has been optimized.

scholarly journals The intrinsic substrate specificity of a cyclic nucleotide-independent protein (histone) kinase

FEBS Letters ◽  
1982 ◽  
Vol 144 (2) ◽  
pp. 223-225 ◽  
Author(s):  
T. Romhányi ◽  
J. Seprödi ◽  
Mészáros Gy ◽  
F. Antoni ◽  
A. Faragó
Keyword(s):  
Substrate Specificity ◽  
Cyclic Nucleotide ◽  
Histone Kinase ◽  
Independent Protein
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