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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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Alanopine dehydrogenase

Alanopine dehydrogenase (EC 1.5.1.17) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2,2'-iminodipropanoate:NAD+ oxidoreductase (L-alanine-forming).

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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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Alcohol sulfotransferase

Alcohol sulfotransferase is an enzyme that catalyzes the sulfate conjugation of primary and secondary alcohols including many hormones, neurotransmitters, drugs, and xenobiotic compounds.

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Aldose reductase

Aldose reductase is an NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. It is primarily known for catalyzing the reduction of glucose to sorbitol, the first step in polyol pathway of glucose metabolism.

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Alglucerase

Alglucerase is a modified form of human β-glucocerebrosidase where the non-reducing ends of the oligosaccharide chains have been terminated with mannose residues.It is given intravenously in the treatment of Type 1 Gaucher's disease although it has been largely replaced by Cerezyme which is produced by Recombinant DNA technology.

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Alkaline Phophatase

Alkaline phosphatase (ALP, ALKP) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase.

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Alkaline protease

Alkaline proteases hydrolyze proteins and break them down into more soluble polypeptides or free amino acids. As a result of the combined effect of surfactants and enzymes, stubborn stains can be removed from fibers.Alkaline proteases are the most widely used enzymes in the detergent industry. They remove protein stains such as grass, blood, egg, and human sweat.

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Allyl-alcohol dehydrogenase

Allyl-alcohol dehydrogenase (EC 1.1.1.54) 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 allyl-alcohol:NADP+ oxidoreductase.

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Alpha-Amylase

Alpha-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. Alpha-Amylase is the major form of amylase found in humans and other mammals.Alpha-Amylase is also present in seeds containing starch as a food reserve, and is secreted by many fungi.Alpha-Although found in many tissues, amylase is most prominent in pancreatic juice and saliva, each of which has its own isoform of human α-amylase.Alpha-Amylase is found in saliva and breaks starch into maltose and dextrin.Alpha-Amylases contain a number of distinct protein domains. The catalytic domain has a structure consisting of an eight-stranded alpha/beta barrel that contains the active site, interrupted by a ~70-amino acid calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.

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