Effect of site-directed mutations on processing and activity of gamma-glutamyltranspeptidase of Escherichia coli K-12.

Effect of site-directed mutations on processing and activity of gamma-glutamyltranspeptidase of Escherichia coli K-12. Research Abstract Details 

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Effect of site-directed mutations on processing and activity of gamma-glutamyltranspeptidase of Escherichia coli K-12. Abstract Text:

W Hashimoto,H Suzuki,K Yamamoto,H Kumagai,

gamma-Glutamyltranspeptidase [EC 2.3.2.2] of Escherichia coli K-12 is thought to be synthesized from a single precursor polypeptide into a heterodimeric form through post-translational processing. Cells of a gamma-glutamyltranspeptidase-overproducing transformant of E. coli K-12 were fractionated and the localization of the enzyme was examined by Western blot analysis. The periplasmic fraction only contained the mature form of gamma-glutamyltranspeptidase, membrane fraction only contained the precursor of gamma-glutamyltranspeptidase, and no precursor of gamma-glutamyltranspeptidase was detected in the cytoplasmic fraction. Amino acid residues at the cleavage site for processing into the large and small subunits were substituted by site-directed mutagenesis. The processing phenotypes of six mutants were examined by Western blot analysis, and their gamma-glutamyltranspeptidase activities were measured. Mutations at the N-terminal amino acid residues of the small subunit (Thr-391, Thr-392, and His-393) prevented the maturation of the enzyme and the immature mutants exhibited no enzymatic activity. A mutation at the C-terminal residue of the large subunit (Gln-390) had less effect on the processing and enzymatic activity. These results suggest that the sequence of threonyl-threonyl-histidinyl residues at the N-terminal of the small subunit is very important for the processing of E. coli K-12 gamma-glutamyltranspeptidase and this processing is essential to the expression of gamma-glutamyltranspeptidase activity of E. coli K-12.

Effect of site-directed mutations on processing and activity of gamma-glutamyltranspeptidase of Escherichia coli K-12. Publishing Authors By Initials

W Hashimoto,H Suzuki,K Yamamoto,H Kumagai,

For similar enzymes and coenzymes: enzymes: transferases: acyltransferases: aminoacyltransferases: gamma-glutamyltransferase research abstracts see: enzymes and coenzymes: enzymes: transferases: acyltransferases: aminoacyltransferases: gamma-glutamyltransferase research

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Effect of site-directed mutations on processing and activity of gamma-glutamyltranspeptidase of Escherichia coli K-12. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 118

Page Numbers: 75-80

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1995

Effect of site-directed mutations on processing and activity of gamma-glutamyltranspeptidase of Escherichia coli K-12. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Effect of site-directed mutations on processing and activity of gamma-glutamyltranspeptidase of Escherichia coli K-12. Keywords Mesh Terms:

KEYWORDS: gamma-Glutamyltransferase

MESH TERMS: metabolism

Chemical & Substance for Abstract: Effect of site-directed mutations on processing and activity of gamma-glutamyltranspeptidase of Escherichia coli K-12. Information

Substance Name: gamma-Glutamyltransferase

Registry Number: EC 2.3.2.2

Grant and Affiliation Information for Effect of site-directed mutations on processing and activity of gamma-glutamyltranspeptidase of Escherichia coli K-12.

AFFILIATION: Department of Food Science and Technology, Faculty of Agriculture, Kyoto University.

Country: JAPAN

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MEDLINETA: J Biochem

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