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Sucrose phosphorylase

Sucrose phosphorylase (E.C. 2.4.1.7) is an important enzyme in the metabolism of sucrose and regulation of other metabolic intermediates. Sucrose phosphorylase is in the class of hexosyltransferases. More specifically it has been placed in the retaining glycoside hydrolases family although it catalyzes a transglycosidation rather than hydrolysis. Sucrose phosphorylase catalyzes the conversion of sucrose to D-fructose and α-D-glucose-1-phosphate.

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Taurine dehydrogenase

Taurine dehydrogenase (EC 1.4.99.2) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with other acceptors. The systematic name of this enzyme class is taurine:acceptor oxidoreductase (deaminating). This enzyme participates in nitrogen metabolism.

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Thioredoxin reductase

Thioredoxin Reductases (TR, TrxR) (EC 1.8.1.9) are the only known enzymes to reduce thioredoxin (Trx). Thioredoxin reductase is a homodimer of 316-residue subuints that catalyzes the reduction of thioredoxin using NADPH as a reducing agent. It mediates the final step in the electron-transfer pathway for nucleoside diphosphate reduction.

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Tropinone reductase I

Tropinone reductase I (EC 1.1.1.206) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is tropine:NADP+ 3alpha-oxidoreductase.Tropinone reductase (ambiguous), and TR-I. This enzyme participates in alkaloid biosynthesis ii.

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4-oxoproline reductase

4-oxoproline reductase (EC 1.1.1.104) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-hydroxy-L-proline:NAD+ oxidoreductase.This enzyme participates in arginine and proline metabolism.

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Acetyl-CoA carboxylase

Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme that catalyzes the irreversible carboxylation of acetyl-CoA to produce malonyl-CoA through its two catalytic activities, biotin carboxylase (BC) and carboxyltransferase (CT). The most important function of ACC is to provide the malonyl-CoA substrate for the biosynthesis of fatty acids.

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Alanine aminopeptidase

Alanine aminopeptidase (EC 3.4.11.2) is an enzyme that is used as a biomarker to detect damage to the kidneys, and that may be used to help diagnose certain kidney disorders. It is found at high levels in the urine when there are kidney problems.

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Alcohol Dehydrogenases

Alcohol Dehydrogenases are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). The alcohol dehydrogenases comprise a group of several isozymes that catalyse the oxidation of primary and secondary alcohols to aldehydes and ketones, respectively, and also can catalyse the reverse reaction. Alcohol dehydrogenase is a dimer with a mass of 80 kDa. Alcohol dehydrogenase is also involved in the toxicity of other types of alcohol. Alcohol dehydrogenase activity varies between men and women, between young and old, and among populations from different areas of the world.

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Aspartate transaminase

Aspartate transaminase (AST) (EC 2.6.1.1) is similar to alanine transaminase (ALT) in that it is another enzyme associated with liver parenchymal cells.It facilitates the conversion of aspartate and alpha-ketoglutarate to oxaloacetate and glutamate, and vice-versa.

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Creatine Phosphokinase

Creatine kinase (CK), also known as creatine phosphokinase (CPK) or phospho-creatine kinase, is an enzyme (EC 2.7.3.2) expressed by various tissues and cell types. CK catalyses the conversion of creatine and consumes adenosine triphosphate (ATP) to create phosphocreatine and adenosine diphosphate (ADP). This CK enzyme reaction is reversible, such that also ATP can be generated from PCr and ADP.

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