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Temperature also affects chlorophyllase activity. Wheat chlorophyllase is active from 25 to 75 °C. The enzyme is inactivated at temperatures above 85 °C. Wheat chlorophyllase is stable 20 °C higher than other chlorophyllases. These other chlorophyllases can stay active at temperatures up to 55 °C. [11]
Enzyme activity. An enzyme's name is often derived from its substrate or the chemical reaction it catalyzes, with the word ending in -ase. [1]: 8.1.3 Examples are lactase, alcohol dehydrogenase and DNA polymerase. Different enzymes that catalyze the same chemical reaction are called isozymes. [1]: 10.3
The enzyme phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic acid.: [1] L -phenylalanine = trans -cinnamate + NH 3 Phenylalanine ammonia lyase (PAL) is the first and committed step in the phenyl propanoid pathway and is therefore involved in the biosynthesis of the polyphenol ...
T. aquaticus is a bacterium that lives in hot springs and hydrothermal vents, and Taq polymerase was identified [1] as an enzyme able to withstand the protein-denaturing conditions (high temperature) required during PCR. [2] Therefore, it replaced the DNA polymerase from E. coli originally used in PCR. [3]
In fact, its catalytic activity is more effective than platinum, which is the best-known catalyst for the H 2 evolution reaction. [38] Among three different types of hydrogenases, [FeFe] hydrogenases is considered as a strong candidate for an integral part of the solar H 2 production system since they offer an additional advantage of high TOF ...
Ribbon representation of the Streptomyces lividans β-1,4-endoglucanase catalytic domain - an example from the family 12 glycoside hydrolases [1]. Cellulase (EC 3.2.1.4; systematic name 4-β-D-glucan 4-glucanohydrolase) is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides:
There seem to be three different classes of GS: [18] [19] [20] Class I enzymes (GSI) are specific to prokaryotes, and are oligomers of 12 identical subunits. [21] The activity of GSI-type enzyme is controlled by the adenylation of a tyrosine residue. The adenylated enzyme is inactive. [22]
While this enzyme has not been purified from human tissue, the activity was shown to be present in human blood serum. [ 17 ] [ 18 ] The acetoacetate decarboxylase activity is mainly attributed to human serum albumin , however, the activity is about 10 − 4 {\displaystyle 10^{-4}} times that of real acetoacetate decarboxylase ( C. acetobutylicum ).