Search results
Results from the WOW.Com Content Network
Flavin-containing monooxygenase 3 (FMO3), also known as dimethylaniline monooxygenase [N-oxide-forming] 3 and trimethylamine monooxygenase, is a flavoprotein enzyme (EC 1.14.13.148) that in humans is encoded by the FMO3 gene.
Initial efforts to purify and characterize proteases using hemoglobin transpired at a time when the word "cathepsin" indicated a single enzyme; [28] the existence of multiple, distinct cathepsin family members (e.g. B, H, L) did not appear to be understood at the time. However, by 1937 Bergmann and colleagues began to differentiate cathepsins ...
Tyrosine hydroxylase or tyrosine 3-monooxygenase is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA). [ 5 ] [ 6 ] It does so using molecular oxygen (O 2 ), as well as iron (Fe 2+ ) and tetrahydrobiopterin as cofactors .
This list contains a list of sub-classes for the seventh group of Enzyme Commission numbers, EC 7, translocases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.
Pectinase enzymes used today are naturally produced by fungi and yeasts (50%), insects, bacteria and microbes (35%) and various plants (15%), [4] but cannot be synthesized by animal or human cells. [5] In plants, pectinase enzymes hydrolyze pectin that is found in the cell wall, allowing for new growth and changes to be made.
Hyaluronidases are a family of enzymes that catalyse the degradation of hyaluronic acid. Karl Meyer classified these enzymes in 1971, into three distinct groups, a scheme based on the enzyme reaction products. [1] The three main types of hyaluronidases are two classes of eukaryotic endoglycosidase hydrolases and a prokaryotic lyase-type of ...
An exoenzyme, or extracellular enzyme, is an enzyme that is secreted by a cell and functions outside that cell. Exoenzymes are produced by both prokaryotic and eukaryotic cells and have been shown to be a crucial component of many biological processes. Most often these enzymes are involved in the breakdown of larger macromolecules.
Pymol-generated image of E1 subunit of pyruvate dehydrogenase complex in E. Coli. The E1 subunit, called the pyruvate dehydrogenase subunit, is either a homodimer (comprising two “α” chains, e.g. in Escherichia coli) or a heterotetramer of two different chains (two “α” and two “β” chains).