Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/31289
Title: Kinetic analysis of salting activation of a subtilisin-like halophilic protease
Authors: Okamoto, Debora N. [UNIFESP]
Kondo, Marcia Y. [UNIFESP]
Santos, Jorge A. N. [UNIFESP]
Nakajima, Sawa
Hiraga, Kazumi
Oda, Kohei
Juliano, Maria A. [UNIFESP]
Juliano, Luiz [UNIFESP]
Gouvea, Iuri E. [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
Kyoto Inst Technol
Keywords: Peptidase
Serine protease
Proton inventory
Issue Date: 1-Feb-2009
Publisher: Elsevier B.V.
Citation: Biochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1794, n. 2, p. 367-373, 2009.
Abstract: The secreted extracellular subtilase SR5-3 from Halobacillus sp. bacterium, isolated from the high-salt environment of Thai fish sauce. was utilized as a model halophilic serine protease. the dependence of salt activation on the size and structure of substrates was evaluated assaying the enzyme with Suc-AAPF-MCA and with the Fluorescence Resonance Energy Transfer (FRET) peptide Abz-AAPFSSKQ-EDDnp. Solvent isotope effects (SIE) and the thermodynamic parameters for activation of the hydrolysis of Suc-AAPF-MCA and Abz-AAPFSSKQ-EDDnp by SR5-3 protease in the presence of salts were also performed. All the obtained results support the notion that the salting out effect is responsible for the halophilic character of SR5-3, and the magnitude of its hydrolytic activity is mainly derived from the improvement of catalytic and/or interaction steps depending on the nature and size of the substrates, principally if they occupy the substrate prime subsites. (C) 2008 Published by Elsevier B.V.
URI: http://repositorio.unifesp.br/handle/11600/31289
ISSN: 1570-9639
Other Identifiers: http://dx.doi.org/10.1016/j.bbapap.2008.10.017
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