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L-pipecolate oxidase (EC 1.5.3.7) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-pipecolate:oxygen 1,6-oxidoreductase.This enzyme participates in lysine degradation.
Lysine decarboxylase is an enzyme which converts lysine to cadaverine.
Malate dehydrogenase (EC 1.1.1.37) is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH.
Manganese Peroxidase is a hemoprotein involved in the oxidative degradation of lignin in white-rot basidiomycetes. It catalyzes the oxidation of Mn(II) to Mn(III) by H2O2. The highly reactive Mn(III) is stabilized via chelation in the presence of dicarboxylic acid.
Metalloendopeptidase is an enzyme that functions as a metalloproteinase endopeptidase.
Penicillin G Acylase (EC 3.5.1.11) is a enzyme derived from Escherichia coli.Penicillin G acylase has many applications, from the hydrolysis of penicillin G (production of 6-aminopenicillanic acid) to the synthesis of semi-synthetic antibiotics.It is widely used in synthesis of antibiotics such as ampicillin, amoxicillin, cloxacillin, cephalexin, and cefatoxime.
Peptidyl transferase is an aminoacyltransferase (EC 2.3.2.12) as well as the primary enzymatic function of the ribosome which forms peptide links between adjacent amino acids using tRNAs during the translation process of protein biosynthesis. Peptidyl transferases are not limited to translation but there are relatively few enzymes with this function.
Prolyl endopeptidase (PREP) or prolyl oligopeptidase (EC 3.4.21.26), sometimes post-proline cleaving enzyme) is a large cytosolic enzyme that belongs to a distinct class of serine peptidases. The enzyme is involved in the maturation and degradation of peptide hormones and neuropeptides.
Protein phosphatases are a group of enzymes, found ubiquitously, which are responsible for the dephosphorylation of various proteins and enzymes in a cell. This role is an extremely important one since protein phosphorylation and dephosphorylation is required for the regulation of a large number of cellular activities.
Pyruvate carboxylase (PC) is an enzyme of the ligase class that catalyzes the reversible carboxylation of pyruvate to form oxaloacetate (OAA). PC plays a crucial role in gluconeogenesis and lipogenesis, in the biosynthesis of neurotransmitters, and in glucose-induced insulin secretion by pancreatic islets.
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