Amastatin
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| Systematic (IUPAC) name | |
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(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-3-Amino-2-hydroxy-5-methylhexanoyl]amino]-3-methylbutanoyl]amino]-3-methylbutanoyl]amino]butanedioic acid
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| 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 |
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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]
- ^ John Buckingham (2 December 1993). Dictionary of Natural Products. CRC Press. pp. 197–. ISBN 978-0-412-46620-5.
- ^ 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.
- ^ Peter Boger; Gerhard Sandmann (31 July 1989). Target Sites of Herbicide Action. CRC Press. pp. 203–. ISBN 978-0-8493-4985-0.
- ^ Thomas Scott; Eric Ian Mercer (1997). Concise Encyclopedia Biochemistry and Molecular Biology. Walter de Gruyter. pp. 35–. ISBN 978-3-11-014535-9.
- ^ 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.
- ^ Graham Barrett (6 December 2012). Chemistry and Biochemistry of the Amino Acids. Springer Science & Business Media. pp. 28–. ISBN 978-94-009-4832-7.
- ^ 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.
- ^ 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.
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