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3.) Isoenzymes of alkaline phosphatase: [7] Six isoenzymes have been identified. The enzyme is a monomer, the isoenzymes are due to the differences in the carbohydrate content (sialic acid residues). The most important ALP isoenzymes are α 1-ALP, α 2-heat labile ALP, α 2-heat stable ALP, pre-β ALP and γ-ALP.
FMO3 is the main flavin-containing monooxygenase isoenzyme that is expressed in the liver of adult humans. [ 8 ] [ 9 ] [ 10 ] The human FMO3 enzyme catalyzes several types of reactions, including: the N -oxygenation of primary, secondary, and tertiary amines ; [ 9 ] [ 11 ] the S -oxygenation of nucleophilic sulfur -containing compounds; [ 9 ...
Hexosaminidase (EC 3.2.1.52, β-acetylaminodeoxyhexosidase, N-acetyl-β-D-hexosaminidase, N-acetyl-β-hexosaminidase, N-acetyl hexosaminidase, β-hexosaminidase, β-acetylhexosaminidinase, β-D-N-acetylhexosaminidase, β-N-acetyl-D-hexosaminidase, β-N-acetylglucosaminidase, hexosaminidase A, N-acetylhexosaminidase, β-D-hexosaminidase) is an enzyme involved in the hydrolysis of terminal N ...
Enolase 1 (ENO1), more commonly known as alpha-enolase, is a glycolytic enzyme expressed in most tissues, one of the isozymes of enolase.Each isoenzyme is a homodimer composed of 2 alpha, 2 gamma, or 2 beta subunits, and functions as a glycolytic enzyme.
Reaction catalyzed by lactate dehydrogenase. Lactate dehydrogenase catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD +.It converts pyruvate, the final product of glycolysis, to lactate when oxygen is absent or in short supply, and it performs the reverse reaction during the Cori cycle in the liver.
Aldolase B is a homotetrameric enzyme, composed of four subunits with molecular weights of 36 kDa with local 222 symmetry. Each subunit has a molecular weight of 36 kDa and contains an eight-stranded α/β barrel, which encloses lysine 229 (the Schiff-base forming amino acid that is key for catalysis).
The mechanism of ring closure is complex, but involves an aldol condensation at C-2 and C-7.. Metabolic engineering has improved production of DAHP by Escherichia coli. [1] The first step, condensation of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate (DAHP) from PEP/E4P, uses three isoenzymes AroF, AroG, and AroH. [2]
The S-adenosylmethionine synthetase enzyme is found in almost every organism bar parasites which obtain AdoMet from their host. Isoenzymes are found in bacteria, budding yeast and even in mammalian mitochondria. Most MATs are homo-oligomers and the majority are tetramers.