Transferase

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Related to Transferases: Lyases, Ligases, Hydrolases, Isomerases

transferase

[′tranz·fə‚rās]
(biochemistry)
Any of various enzymes that catalyze the transfer of a chemical group from one molecule to another.

Transferase

 

any of a class of enzymes that catalyze the transfer of a chemical group from one compound (the donor) to another (the acceptor). Transferases are common in plant and animal tissues, as well as in microorganisms. They play a leading role in intermediary metabolism, participating in the transformations of carbohydrates, amino acids, nucleic acids, lipids, and other biologically important compounds.

The transferase class includes more than 450 enzymes, divided by the chemical nature of the group being transferred into subclasses. Examples include the subclasses that catalyze the transfer of single-carbon groups (methyltransferases), glycosyl groups (glycosyltransferases), nitrogen-bearing groups (aminotransferases, or transaminases), and phosphate groups (phosphotransferases). The transferases of the various subclasses have different coenzymes.

The mechanism of the catalytic action of the transferases studied to date includes the formation of an intermediate made up of the enzyme and group being transferred. For example, in the transfer of the acetyl radical (CH3CO—), an acetylated enzyme is formed in the first stage of the reaction, followed by the transfer of the radical to the acceptor and the liberation of the enzyme. The names of transferases are formed according to the sequence dononacceptor-transferred group-transferase. For example, the enzyme that catalyzes the transfer of the phosphate group from adenosinetriphosphate (ATP) to creatine is called ATP:creatine-phosphotransferase. Several transferases have been obtained in crystalline form.

REFERENCES

Nomenklatura fermentov. Moscow, 1966. (Translated from English.)
Kretovich, V. L. Vvedenie v enzimologiiu, 2nd ed. Moscow, 1974.

V. V. ZUEVSKII

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Structure, catalytic mechanism, and evolution of the glutathione transferases.
Hence, the present work is carried out to determine the effect of fluoride intoxication on amino transferase enzyme activity in fresh water cat fish, Clarias batrachus.
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This novel post-translational modification is catalyzed by AMP transferases containing a so-called Fido motif that has been found across prokaryotes and eukaryotes, in over 2700 putative bacterial and mammalian proteins.
He covers chiral discrimination in the active site of oxidoreductases, transferases and chiral discrimination, the influence of chirality on the hydrolysis reactions within the active site of hydrolases, the influence of chirality on the reactions in the active site of lyases, and chiral discrimination in the active site of ligases.
Mice deficient in glutathione transferase zeta/maleylacetoacetate isomerase exhibit a range of pathological changes and elevated expression of alpha, mu, and pi class glutathione transferases.