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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. Increase in α 2-heat labile ALP suggests hepatitis whereas pre-β ALP indicates bone diseases.
Enolase is a member of the large enolase superfamily.It has a molecular weight of 82,000–100,000 daltons depending on the isoform. [3] [4] In human alpha enolase, the two subunits are antiparallel in orientation so that Glu 20 of one subunit forms an ionic bond with Arg 414 of the other subunit. [3]
The software release life cycle is the process of developing, testing, and distributing a software product (e.g., an operating system).It typically consists of several stages, such as pre-alpha, alpha, beta, and release candidate, before the final version, or "gold", is released to the public.
Humans express four epoxide hydrolase isozymes: mEH, sEH, EH3, and EH4. These isozymes are known (mEH and sEH) or presumed (EH3 and EH4) to share a common structure that includes containing an Alpha/beta hydrolase fold and a common reaction mechanism wherein they add water to epoxides to form vicinal cis (see (cis-trans isomerism); see (epoxide#Olefin (alkene) oxidation using organic peroxides ...
Phenylalanine hydroxylase (PAH) (EC 1.14.16.1) is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine.PAH is one of three members of the biopterin-dependent aromatic amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin (BH 4, a pteridine cofactor) and a non-heme iron for catalysis.
The protein contains a beta sheet stacked on two alpha helices described by CATH as an Alpha-Beta Plait fold. The active site sits between sheet and helices and contains an arginine and an asparagine. [4] Most structures are monomeric [5]
Phosphodiesterase 1, PDE1, EC 3.1.4.1, systematic name oligonucleotide 5 ′-nucleotidohydrolase) is a phosphodiesterase enzyme also known as calcium- and calmodulin-dependent phosphodiesterase.
α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process: [2]