Amastatin

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Amastatin
Amastatin.svg
Systematic (IUPAC) name
(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-3-Amino-2-hydroxy-5-methylhexanoyl]amino]-3-methylbutanoyl]amino]-3-methylbutanoyl]amino]butanedioic acid
Identifiers
CAS Number 67655-94-1
ATC code None
PubChem CID 439518
ChemSpider 388612
Chemical data
Formula C21H38N4O8
Molar mass 474.54842 g/mol
3D model (Jmol) Interactive image

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.[1] It specifically inhibits leucyl aminopeptidase, alanyl aminopeptidase (aminopeptidase M/N), bacterial leucyl aminopeptidase (Aeromonas proteolytica aminopeptidase), leucyl/cystinyl aminopeptidase (oxytocinase/vasopressinase),[2] and, to a lesser extent, glutamyl aminopeptidase (aminopeptidase A),[3] as well as other aminopeptidases.[4] It does not inhibit arginyl aminopeptidase (aminopeptidase B).[5][6] Amastatin has been found to potentiate the central nervous system effects of oxytocin and vasopressin in vivo.[7] It also inhibits the degradation of met-enkephalin, dynorphin A, and other endogenous peptides.[8]

See also[edit]

References[edit]

  1. ^ John Buckingham (2 December 1993). Dictionary of Natural Products. CRC Press. pp. 197–. ISBN 978-0-412-46620-5. 
  2. ^ Nakanishi Y, Nomura S, Okada M, Ito T, Katsumata Y, Kikkawa F, Hattori A, Tsujimoto M, Mizutani S (2000). "Immunoaffinity purification and characterization of native placental leucine aminopeptidase/oxytocinase from human placenta". Placenta. 21 (7): 628–34. doi:10.1053/plac.2000.0564. PMID 10985965. 
  3. ^ Peter Boger; Gerhard Sandmann (31 July 1989). Target Sites of Herbicide Action. CRC Press. pp. 203–. ISBN 978-0-8493-4985-0. 
  4. ^ Thomas Scott; Eric Ian Mercer (1997). Concise Encyclopedia Biochemistry and Molecular Biology. Walter de Gruyter. pp. 35–. ISBN 978-3-11-014535-9. 
  5. ^ Hamao Umezawa (9 May 2014). Small Molecular Immunomodifiers of Microbial Origin: Fundamental and Clinical Studies of Bestatin. Elsevier Science. pp. 10–. ISBN 978-1-4831-9033-4. 
  6. ^ Graham Barrett (6 December 2012). Chemistry and Biochemistry of the Amino Acids. Springer Science & Business Media. pp. 28–. ISBN 978-94-009-4832-7. 
  7. ^ Meisenberg G, Simmons WH (1984). "Amastatin potentiates the behavioral effects of vasopressin and oxytocin in mice". Peptides. 5 (3): 535–9. doi:10.1016/0196-9781(84)90083-4. PMID 6540873. 
  8. ^ Oka T, Hiranuma T, Liu XF, Ohgiya N, Iwao K, Matsumiya T (1993). "[Enkephalin-inactivating enzymes]". Nippon Yakurigaku Zasshi (in Japanese). 101 (4): 197–207. PMID 8390390.