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This list contains a list of sub-classes for the seventh group of Enzyme Commission numbers, EC 7, translocases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.
The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. [1] As a system of enzyme nomenclature, every EC number is associated with a recommended name for the corresponding enzyme-catalyzed reaction. EC numbers do not specify enzymes but enzyme-catalyzed reactions.
Thus, the two substrates of this enzyme are N-acyl-L-amino acid and H 2 O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acyl-L-amino acid ...
Enzymes are listed here by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system: Category:Oxidoreductases (EC 1) ( Oxidoreductase )
Main menu. Main menu. move to ... Download as PDF; Printable version; In other projects ... Appearance. move to sidebar hide. Amino acids are listed by type ...
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is aromatic-amino-acid:2-oxoglutarate aminotransferase. Other names in common use include aromatic amino acid aminotransferase, aromatic aminotransferase, and ArAT.
Temperature: ~35-40 °C (storage at 6 °C keeps enzyme stable for ~1 week) Absence of carbonyl, sulfhydryl, or Cu 2+ or Co 2+ reagents/compounds; Enzyme catalyzes reaction best with branched chain amino acids (in order from most activity to least: isoleucine, leucine, valine) Enzyme also shows minimal activity with methionine, cysteine, and ...
These enzymes can be identified by a conserved HEXXH motif in their active site. This motif is crucial for the enzyme's function, as the histidine amino acids within the motif coordinate (bind) the metal ion, which then uses hydrolysis to break the peptide bond between the first amino acid and the rest of the protein. [9]