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Membrane alanyl aminopeptidase also known as alanyl aminopeptidase (AAP) or aminopeptidase N (AP-N) is an enzyme that in humans is encoded by the ANPEP gene.
Aspergillopepsin I 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.
Methionine aminopeptidase 2 is an enzyme that in humans is encoded by the METAP2 gene.
The discovery of an orally inactive peptide from snake venom established the important role of angiotensin converting enzyme (ACE) inhibitors in regulating blood pressure. This led to the development of captopril, the first ACE inhibitor. When the adverse effects of captopril became apparent new derivates were designed. Then after the discovery of two active sites of ACE: N-domain and C-domain, the development of domain-specific ACE inhibitors began.
Dipeptidyl-peptidase 3 is an enzyme that in humans is encoded by the DPP3 gene.
Dipeptidase 1 (DPEP1), or renal dipeptidase, is a membrane-bound glycoprotein responsible for hydrolyzing dipeptides. It is found in the microsomal fraction of the porcine kidney cortex. It exists as a disulfide-linked homodimer that is glygosylphosphatidylinositol (GPI)-anchored to the renal brush border of the kidney. The active site on each homodimer is made up of a barrel subunit with binuclear zinc ions that are bridged by the Gly125 side-chain located at the bottom of the barrel.
Nuclear transition protein 2 is a protein that in humans is encoded by the TNP2 gene.
Methionine aminopeptidase 1 is an enzyme that in humans is encoded by the METAP1 gene.
Aminopeptidase B is an enzyme that in humans is encoded by the RNPEP gene.
Tripeptide aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction:
Aminopeptidase B is an enzyme. This enzyme catalyses the following chemical reaction
Bacterial leucyl aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Aminopeptidase S is an enzyme. This enzyme catalyses the following chemical reaction
Peptidyl-dipeptidase Dcp (EC 3.4.15.5, dipeptidyl carboxypeptidase (Dcp), dipeptidyl carboxypeptidase) is a metalloenzyme found in the cytoplasm of bacterium E. Coli responsible for the C-terminal cleavage of a variety of dipeptides and unprotected larger peptide chains. The enzyme does not hydrolyze bonds in which P1' is Proline, or both P1 and P1' are Glycine. Dcp consists of 680 amino acid residues that form into a single active monomer which aids in the intracellular degradation of peptides. Dcp coordinates to divalent zinc which sits in the pocket of the active site and is composed of four subsites: S1’, S1, S2, and S3, each subsite attracts certain amino acids at a specific position on the substrate enhancing the selectivity of the enzyme. The four subsites detect and bind different amino acid types on the substrate peptide in the P1 and P2 positions. Some metallic divalent cations such as Ni+2, Cu+2, and Zn+2 inhibit the function of the enzyme around 90%, whereas other cations such as Mn+2, Ca+2, Mg+2, and Co+2 have slight catalyzing properties, and increase the function by around 20%. Basic amino acids such as Arginine bind preferably at the S1 site, the S2 site sits deeper in the enzyme therefore is restricted to bind hydrophobic amino acids with phenylalanine in the P2 position. Dcp is divided into two subdomains (I, and II), which are the two sides of the clam shell-like structure and has a deep inner cavity where a pair of histidine residues bind to the catalytic zinc ion in the active site. Peptidyl-Dipeptidase Dcp is classified like Angiotensin-I converting enzyme (ACE) which is also a carboxypeptidase involved in blood pressure regulation, but due to structural differences and peptidase activity between these two enzymes they had to be examined separately. ACE has endopeptidase activity, whereas Dcp strictly has exopeptidase activity based on its cytoplasmic location and therefore their mechanisms of action are differentiated. Another difference between these enzymes is that the activity of Peptidyl-Dipeptidase Dcp is not enhanced in the presence of chloride anions, whereas chloride enhances ACE activity.
Snapalysin is an enzyme. This enzyme catalyses the following chemical reaction
Phosvitin is one of the egg yolk phosphoproteins known for being the most phosphorylated protein found in nature. Phosvitin isolation was first described by Mecham and Olcott in the year 1949. Recently it has been shown that disordered secondary structure of phosvitin orchestrates nucleation and growth of biomimetic bone like apatite.
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
- ↑ Ichishima E, Yamagata Y, Chiba H, Sawaguchi K, Tanaka T (1989). "Soluble and bound forms of aminopeptidase in hens egg-yolk". Agric. Biol. Chem. 53: 1867–1872. doi: 10.1271/bbb1961.53.1867 .
- ↑ Tanaka T, Ichishima E (May 1993). "Substrate specificity of aminopeptidase Ey from hen's (Gallus domesticus) egg yolk". Comparative Biochemistry and Physiology. B, Comparative Biochemistry. 105 (1): 105–10. doi:10.1016/0305-0491(93)90175-5. PMID 7684960.
- ↑ Tanaka T, Ichishima E (November 1993). "Molecular properties of aminopeptidase Ey as a zinc-metalloenzyme". The International Journal of Biochemistry. 25 (11): 1681–8. doi:10.1016/0020-711x(93)90528-m. PMID 8288037.
