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ProductsBack/Amastatin . hydrochloride [100938-10-1]
Chemical Structure
Chemical Structure
Chemical Structure

Amastatin . hydrochloride [100938-10-1]

Research Use Only
AG-CP3-7003
AdipoGen Life Sciences
CAS Number100938-10-1
DownloadMSDS
Product group Chemicals
Estimated Purity>98%
Molecular Weight474.6 . 36.5
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Overview

  • Supplier
    AdipoGen Life Sciences
  • Product Name
    Amastatin . hydrochloride [100938-10-1]
  • Delivery Days Customer
    10
  • CAS Number
    100938-10-1
  • Certification
    Research Use Only
  • Estimated Purity
    >98%
  • Molecular Formula
    C21H38N4O8 . HCl
  • Molecular Weight
    474.6 . 36.5
  • Scientific Description
    Chemical. CAS: 100938-10-1. Formula: C21H38N4O8 . HCl. MW: 474.6 . 36.5. Synthetic. Slow, tight binding and competitive aminopeptidase (AP) inhibitor. Inhibits cytosolic leucine aminopeptidase, microsomal aminopeptidase M and bacterial leucine aminopeptidase, human serum aminopeptidase A (AP-A), aminopeptidase N (AP-N), tyrosine aminopeptidase, but not aminopeptidase B (AP-B). Amastatin is without effect on trypsin, papain, chymotrypsin, elastase, pepsin or thermolysin. Inhibits completely the Suc-Ala-Ala-Pro-Leu-pNA amidolytic enzyme. Slightly inhibits the formation of angiotensin III (Ang III) from Angiotensin II through AP-A, but significantly increases the potency of angiotensin III and-angiotensin I. Moderate inhibitor of mitochondrial intermediate peptidase (MIP). Weak inhibitor of simian immunodeficiency virus protease (SIV-PR). - Slow, tight binding and competitive aminopeptidase (AP) inhibitor. Inhibits cytosolic leucine aminopeptidase, microsomal aminopeptidase M and bacterial leucine aminopeptidase, human serum aminopeptidase A (AP-A), aminopeptidase N (AP-N), tyrosine aminopeptidase, but not aminopeptidase B (AP-B). Amastatin is without effect on trypsin, papain, chymotrypsin, elastase, pepsin or thermolysin. Inhibits completely the Suc-Ala-Ala-Pro-Leu-pNA amidolytic enzyme. Slightly inhibits the formation of angiotensin III (Ang III) from Angiotensin II through AP-A, but significantly increases the potency of angiotensin III and [des-Asp1]-angiotensin I. Moderate inhibitor of mitochondrial intermediate peptidase (MIP). Weak inhibitor of simian immunodeficiency virus protease (SIV-PR). ANPEP (aminopeptidase N) is a host receptor targeted by porcine epidemic diarrhoea virus, human coronavirus 229E, feline coronavirus, canine coronavirus, transmissible gastroenteritis virus and infectious bronchitis virus. These viruses all belong to coronaviridae. ANPEP is therefore investigated as a potential target for SARS-CoV-2 infections.
  • SMILES
    [Cl-].CC(C)C[C@@H]([NH3+])[C@H](O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(O)=O)C(O)=O
  • Storage Instruction
    -20°C,2°C to 8°C
  • UNSPSC
    12352200

References

  • Amastatin, an inhibitor of aminopeptidase A, produced by actinomycetes: T. Aoyagi, et al.; J. Antibiot. 31, 636 (1978)
  • Inhibition of aminopeptidases by amastatin and bestatin derivatives. Effect of inhibitor structure on slow-binding processes: D.H. Rich, et al.; J. Med. Chem. 27, 417 (1984)
  • The slow, tight binding of bestatin and amastatin to aminopeptidases: S.H. Wilkes & J.M. Prescott; J. Biol. Chem. 260, 13154 (1985)
  • Inhibition of aminopeptidases by peptides containing ketomethylene and hydroxyethylene amide bond replacements: S.L. Harbeson & D.H. Rich; J. Med. Chem. 32, 1378 (1989)
  • Role of aminopeptidase activity in the regulation of the pressor activity of circulating angiotensins: S. Ahmad & P.E. Ward; J. Pharmacol. Exp. Ther. 252, 643 (1990)
  • Purification and biochemical characterization of recombinant simian immunodeficiency virus protease and comparison to human immunodeficiency virus type 1 protease: S.K. Grant, et al.; Biochemistry 30, 8424 (1991)
  • Rat liver mitochondrial intermediate peptidase (MIP): purification and initial characterization: F. Kalousek, et al.; EMBO J. 11, 2803 (1992)
  • Vasopressin and amastatin induce V(1)-receptor-mediated suppression of excitatory transmission in the rat parabrachial nucleus: X. Chen & Q.J. Pittman; J. Neurophysiol. 82, 1689 (1999)
  • Inhibitors on an elastase-like enzyme activity catalyzing Suc-Ala-Ala-Pro-Leu-pNA amidolysis in human seminal plasma: Y. Matsuda, et al.; Arch. Androl. 44, 1 (2000)
  • The most potent organophosphorus inhibitors of leucine aminopeptidase. Structure-based design, chemistry, and activity: J. Grembecka, et al.; J. Med. Chem. 46, 2641 (2003)