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Characterizations of acylagmatine amidohydrolase and carboxypeptidase from Fusarium anguioides.

Characterizations of acylagmatine amidohydrolase and carboxypeptidase from Fusarium anguioides. Research Abstract Details 

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  • Characterizations of acylagmatine amidohydrolase and carboxypeptidase from Fusarium anguioides. Abstract Text:

    y takahashiY Takahashi,t shiraiT Shirai,s ishiiS Ishii,

    Previously an enzyme, named acylagmatine amidohydrolase, hydrolyzing bleomycin B2 to bleomycinic acid and agmatine was found in the mycelia of Fusarium anguioides Sherbakoff. In this work the enzyme was purified further, but not completely. The crude enzyme preparation hydrolyzed various acylagmatines and also peptidyl arginine, but the latter activity could be separated from acylagmatine amidohydrolase activity by gel filtration on Sephadex G-100. The enzyme was inhibited by PCMB and its molecular weight was estimated as 65,000 by gel filtration. It showed substrate specificity with respect to the alkyl-chain length of the amine moiety. The other hydrolase fraction with activity toward Bz-Gly-Arg was found to be of a sort of carboxypeptidase, which preferentially hydrolyzed peptides with arginine or lysine at the carboxyl terminus, including bradykinin, but liberated neutral amino acids as well from the terminus when the penultimate residue of the substrates was phenylalanine. With Bz-Gly-Arg as substrate Fusarium carboxypeptidase was sensitive to chelating agents but not to diisopropyfluorophosphate, and its molecular weight was estimated to be 145,000.

    Characterizations of acylagmatine amidohydrolase and carboxypeptidase from Fusarium anguioides. Publishing Authors By Initials

    y takahashiY Takahashi,t shiraiT Shirai,s ishiiS Ishii,

    For similar proteins research abstracts see: proteins research

    PUBMED ID PMID:

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    Characterizations of acylagmatine amidohydrolase and carboxypeptidase from Fusarium anguioides. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 77

    Page Numbers: 823-30

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Apr

    YEAR: 1975

    Characterizations of acylagmatine amidohydrolase and carboxypeptidase from Fusarium anguioides. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Characterizations of acylagmatine amidohydrolase and carboxypeptidase from Fusarium anguioides. Keywords Mesh Terms:

    KEYWORDS: Proteins

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Characterizations of acylagmatine amidohydrolase and carboxypeptidase from Fusarium anguioides. Information

    Substance Name: Amidohydrolases

    Registry Number: EC 3.5.-

    Grant and Affiliation Information for Characterizations of acylagmatine amidohydrolase and carboxypeptidase from Fusarium anguioides.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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