Search results
Results from the WOW.Com Content Network
5′-Nucleotidase (EC 3.1.3.5) is an enzyme which catalyzes the phosphorylytic cleavage of 5′-nucleotides. [2] Although originally found in snake venom, [ 3 ] the activity of 5'nucleotidase has been described for bacteria and plant cells, and is widely distributed in vertebrate tissue. [ 4 ]
5' Nucleotidase (5NT) is a glycoprotein found throughout the body, in the cytoplasmic membrane, catalyzing the conversion to inorganic phosphates from nucleoside-5-phosphate. Its level is raised in conditions such as obstructive jaundice, parenchymal liver disease, liver metastases, and bone disease.
Gamma-glutamyltransferase (also γ-glutamyltransferase, GGT, gamma-GT, gamma-glutamyl transpeptidase; [1] EC 2.3.2.2) is a transferase (a type of enzyme) that catalyzes the transfer of gamma-glutamyl functional groups from molecules such as glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate).
The soluble forms are further subclassified based on the criterion mentioned above. mdN and cdN are mitochondrial and cytosolic 5'-3'-pyrimidine nucleotidases. cN-I is a cytosolic nucleotidase(cN) characterized by its affinity toward AMP as its substrate. cN-II is identified by its affinity toward either IMP or GMP or both. cN-III is a ...
Cholestasis is a condition where the flow of bile from the liver to the duodenum is impaired. [1] The two basic distinctions are: [1] obstructive type of cholestasis, where there is a mechanical blockage in the duct system that can occur from a gallstone or malignancy, and
The GGTLA1 enzyme consists of a heavy and a light chain and is able to hydrolyze the gamma-glutamyl moiety of glutathione. It converts leukotriene C4 to leukotriene D4, however, it doesn't convert synthetic substrates that are commonly used to assay GGT. Its amino acid sequence shows an overall similarity of 39.5% with human GGT. [8]
Get AOL Mail for FREE! Manage your email like never before with travel, photo & document views. Personalize your inbox with themes & tabs. You've Got Mail!
Purine degradation takes place mainly in the liver of humans and requires an assortment of enzymes to degrade purines to uric acid. First, the nucleotide will lose its phosphate through 5'-nucleotidase. The nucleoside, adenosine, is then deaminated and hydrolyzed to form hypoxanthine via adenosine deaminase and nucleosidase respectively.