Mechanism of the binding of Z–L-tryptophan and Z–L-phenylalanine to thermolysin and stromelysin-1 in aqueous solutions-Reference-Cited by-同舟云学术

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Mechanism of the binding of Z–L-tryptophan and Z–L-phenylalanine to thermolysin and stromelysin-1 in aqueous solutions

Published:2012-02 Issue:2 Volume:1824 Page:303-310
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Ceruso Mariangela,Howe Nicole,Malthouse J. Paul G.

Funder

Science Foundation Ireland

Programme for Research in Third-Level Institutions (PRTLI-3)

Wellcome Trust

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference38 articles.

1. Studies on the specificity of Bacillus subtilis neutral protease with synthetic substrates;Feder;Biochemistry,1967

2. Comparison of the subsite specificity of the mammalian neutral endopeptidase 24.11 (enkephalinase) to the bacterial neutral endopeptidase thermolysin;Hersh;J. Biol. Chem.,1986

3. Substrate and inhibitor studies of thermolysin-like neutral metalloendopeptidase from kidney membrane fractions. Comparison with bacterial thermolysin;Pozsgay;Biochemistry,1986

4. pH and temperature dependences of thermolysin catalysis. Catalytic role of zinc-coordinated water;Kunugi;Eur. J. Biochem.,1982

5. Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysis;Kester;Biochemistry,1977

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2. Purified proteases of two Antarctic bacteria: from screening to characterization;Antarctic Science;2021-10-20

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