Related Research Articles
Erepsin is a mixture of enzymes contained in a protein fraction found in the intestinal juices that digest peptones into amino acids. It is produced and secreted by the intestinal glands in the ileum and the pancreas, but it is also found widely in other cells. It is, however, a term now rarely used in scientific literature as more precise terms are preferred.
Microbial collagenase is an enzyme. This enzyme catalyses the following chemical reaction
Cytosol alanyl aminopeptidase is an enzyme.
Leucyl/cystinyl aminopeptidase, also known as cystinyl aminopeptidase (CAP), insulin-regulated aminopeptidase (IRAP), human placental leucine aminopeptidase (PLAP), oxytocinase, and vasopressinase, is an enzyme of the aminopeptidase group that in humans is encoded by the LNPEP gene.
Leucyl aminopeptidases are enzymes that preferentially catalyze the hydrolysis of leucine residues at the N-terminus of peptides and proteins. Other N-terminal residues can also be cleaved, however. LAPs have been found across superkingdoms. Identified LAPs include human LAP, bovine lens LAP, porcine LAP, Escherichia coli LAP, and the solanaceous-specific acidic LAP (LAP-A) in tomato.
Leukotriene A4 hydrolase, also known as LTA4H is a human gene. The protein encoded by this gene is a bifunctional enzyme which converts leukotriene A4 to leukotriene B4 and acts as an aminopeptidase.
Dipeptidyl peptidase I is an enzyme. This enzyme catalyses the following chemical reaction
Organophosphorus acid anhydrolase (OPAA) is an enzyme that been shown to be particularly effective in detoxifying organophosphorus-containing compounds, such as deadly nerve gas used in chemical warfare. The enzyme is found in a diverse range of organisms, including protozoa, squid and clams, mammals, and soil bacteria. A highly active form of the enzyme is typically isolated from the marine bacteria Alteromonas undina for laboratory study. This form is both halophilic and thermophilic, making it particularly useful for detoxification applications. A slightly less active variant of OPAA has also been isolated in mung beans and slime mold duckweed.
Prolyl aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Xaa-Pro aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Clostridial aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Aminopeptidase Y is an enzyme. This enzyme catalyses the following chemical reaction
Aminopeptidase Ey is an enzyme. This enzyme catalyses differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyse peptides of four or five residues that contain Pro in the P1' position
Aminopeptidase S is an enzyme. This enzyme catalyses the following chemical reaction
Acylaminoacyl-peptidase is an enzyme. This enzyme catalyses the following chemical reaction
Xaa-Pro dipeptidyl-peptidase (EC 3.4.14.11, X-prolyl dipeptidyl aminopeptidase, PepX, X-prolyl dipeptidyl peptidase is an enzyme. It catalyses the following chemical reaction
Pyroglutamyl-peptidase I (EC 3.4.19.3, also known as Pyrrolidonyl peptidase, is an enzyme found in bacteria, plants and animals.
Pyroglutamyl-peptidase II is an enzyme. This enzyme catalyses the following chemical reaction
Penicillopepsin is an enzyme. This enzyme catalyses the following chemical reaction
Amastatin, also known as 3-amino-2-hydroxy-5-methylhexanoyl-L-valyl-L-valyl-L-aspartic acid, is a naturally occurring, competitive and reversible aminopeptidase inhibitor that was isolated from Streptomyces sp. ME 98-M3. It specifically inhibits leucyl aminopeptidase, alanyl aminopeptidase, bacterial leucyl aminopeptidase, leucyl/cystinyl aminopeptidase (oxytocinase/vasopressinase), and, to a lesser extent, glutamyl aminopeptidase, as well as other aminopeptidases. It does not inhibit arginyl aminopeptidase. Amastatin has been found to potentiate the central nervous system effects of oxytocin and vasopressin in vivo. It also inhibits the degradation of met-enkephalin, dynorphin A, and other endogenous peptides.
References
- ↑ Prescott JM, Wilkes SH (November 1966). "Aeromonas aminopeptidase: purification and some general properties". Archives of Biochemistry and Biophysics. 117 (2): 328–36. doi:10.1016/0003-9861(66)90420-6. PMID 4961737.
- ↑ Dick AJ, Matheson AT, Wang JH (November 1970). "A ribosomal-bound aminopeptidase in Escherichia coli B: purification and properties". Canadian Journal of Biochemistry. 48 (11): 1181–8. doi:10.1139/o70-184. PMID 4920230.
- ↑ Rabier D, Desmazeaud MJ (1973). "[Inventory of different intracellular peptidase activities in Streptococcus thermophilus. Purification and properties of a dipeptide hydrolase and an aminopeptidase]". Biochimie. 55 (4): 389–404. doi:10.1016/s0300-9084(73)80204-4. PMID 4749719.
