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Amastatin

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Chemical compound

Pharmaceutical compound

Amastatin
Clinical data

ATC code	None
Identifiers
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
CAS Number	67655-94-1
PubChemCID	439518
ChemSpider	388612
KEGG	C01552
CompTox Dashboard(EPA)	DTXSID10987015
ECHA InfoCard	100.131.532
Chemical and physical data
Formula	C₂₁H₃₈N₄O₈
Molar mass	474.555 g·mol⁻¹
3D model (JSmol)	Interactive image
SMILES CC(C)CC(C(C(=O)NC(C(C)C)C(=O)NC(C(C)C)C(=O)NC(CC(=O)O)C(=O)O)O)N
InChI InChI=1S/C21H38N4O8/c1-9(2)7-12(22)17(28)20(31)25-16(11(5)6)19(30)24-15(10(3)4)18(29)23-13(21(32)33)8-14(26)27/h9-13,15-17,28H,7-8,22H2,1-6H3,(H,23,29)(H,24,30)(H,25,31)(H,26,27)(H,32,33)/t12-,13+,15+,16+,17+/m1/s1 Key:QFAADIRHLBXJJS-ZAZJUGBXSA-N

Amastatin, also known as3-amino-2-hydroxy-5-methylhexanoyl-L-valyl-L-valyl-L-aspartic acid, is anaturally occurring, competitive and reversibleaminopeptidase inhibitor that was isolated fromStreptomyces sp. ME 98-M3.^[1] It specifically inhibitsleucyl 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 inhibitarginyl aminopeptidase (aminopeptidase B).^[5]^[6] Amastatin has been found to potentiate thecentral nervous system effects ofoxytocin andvasopressinin vivo.^[7] It also inhibits the degradation ofmet-enkephalin,dynorphin A, and otherendogenous peptides.^[8]

It contains the unusual amino acidStatine.

References

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^Buckingham J (2 December 1993)."Amastatins".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, et al. (September 2000). "Immunoaffinity purification and characterization of native placental leucine aminopeptidase/oxytocinase from human placenta".Placenta.21 (7):628–634.doi:10.1053/plac.2000.0564.PMID 10985965.
^Schloss JV (31 July 1989)."Modern Aspects of Enzyme Inhibition with Particular Emphasis on Reaction-Intermediate Analogs and Other Potent, Reversible Inhibitors". In Boger P, Sandmann G (eds.).Target Sites of Herbicide Action. CRC Press. pp. 203–.ISBN 978-0-8493-4985-0.
^Scott T, Mercer EI (1997).Concise Encyclopedia Biochemistry and Molecular Biology. Walter de Gruyter. pp. 35–.ISBN 978-3-11-014535-9.
^Umezawa H (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.
^Drey CN (6 December 2012)."Beta and Higher Homologous Amino Acids". In Barrett G (ed.).Chemistry and Biochemistry of the Amino Acids. Springer Science & Business Media. pp. 28–.doi:10.1007/978-94-009-4832-7_3.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):535–539.doi:10.1016/0196-9781(84)90083-4.PMID 6540873.S2CID 3881661.
^Oka T, Hiranuma T, Liu XF, Ohgiya N, Iwao K, Matsumiya T (April 1993)."[Enkephalin-inactivating enzymes]".Nihon Yakurigaku Zasshi. Folia Pharmacologica Japonica (in Japanese).101 (4):197–207.doi:10.1254/fpj.101.4_197.PMID 8390390.