Pepstatin-insenstive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides.

Pepstatin-insenstive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides. Research Abstract Details 

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Pepstatin-insenstive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides. Abstract Text:

K Morihara,H Tsuzuki,S Murao,K Oda,

A kinetic study was conducted on the acid proteases A-1 and A-2 from Scytalidium lignicolum using synthetic peptides as substrates. Almost maximum activity was attained with N-acylated tetrapeptides as the molecular size of substrates was increased. Suitable amino acid residues were required at the P1-P2 and P1'-P2' positions [notation of Schechter and Berger (14)]. Hydrophobic or bulky residues such as leucine were specifically required at the P1 and P1' positions, with the specificity at the latter position being considerably lower than that at the former. For catalysis, the presence of certain amino acid residues at the P2 and P2' positions was essential, mainly in relation to kcat. An inhibition study supported this view. Stringent stereospecificity was observed at the P2 and P2' positions, but the side chain specificity was low. Study of the B enzyme from the same organism was very difficult owing to its low activity against the peptides used. The Scytalidium acid proteases A-1, A-2, and B showed considerably different behavior against peptide substrates in comparison with usual acid proteases, which are senstive to pepstatin.

Pepstatin-insenstive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides. Publishing Authors By Initials

K Morihara,H Tsuzuki,S Murao,K Oda,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research

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Pepstatin-insenstive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 85

Page Numbers: 661-8

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Mar

YEAR: 1979

Pepstatin-insenstive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Pepstatin-insenstive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides. Keywords Mesh Terms:

KEYWORDS: Structure-Activity Relationship

MESH TERMS: enzymology

Chemical & Substance for Abstract: Pepstatin-insenstive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides. Information

Substance Name: Peptide Hydrolases

Registry Number: EC 3.4.-

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Country: JAPAN

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MEDLINETA: J Biochem

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