Involvement of Val 315 located in the C-terminal region of thermolysin in its expression in Escherichia coli and its thermal stability.

Kojima, Kenji; Nakata, Hiroki; Inouye, Kuniyo

Kojima, Kenji; Nakata, Hiroki; Inouye, Kuniyo.

Affiliation

Kojima K; Laboratory of Enzyme Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Nakata H; Laboratory of Enzyme Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Inouye K; Laboratory of Enzyme Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan. Electronic address: inouye@kais.kyoto-u.ac.jp.

Biochim Biophys Acta ; 1844(2): 330-8, 2014 Feb.

Article in En | MEDLINE | ID: mdl-24192395

Subject(s)

Escherichia coli/genetics; Thermolysin/chemistry; Thermolysin/genetics; Valine/physiology; Acrylates/metabolism; Bacillus/enzymology; Caseins/metabolism; Dipeptides/metabolism; Enzyme Stability; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Hydrolysis; Models, Molecular; Mutagenesis, Site-Directed; Protein Folding; Protein Structure, Tertiary; Thermolysin/metabolism

Key words

C-terminal region; CBB; CC; CD; Circular dichroism; Coomassie Brilliant Blue; Correlation coefficient; DA; Degree of activation; EA; Enzyme expression; Enzyme stability; Expression amount; FAGLA; HC; Hydropathy; N-[3-(2-Fury)acryloyl]-glycyl-l-leucine amide; PU; Proteolytic unit; REA; RHC; Relative expression amount; Relative α-helix content; Site-directed mutagenesis; Thermolysin; WT; Wild-type thermolysin; α-helix content

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Valine / Thermolysin / Escherichia coli Type of study: Prognostic_studies Language: En Journal: Biochim Biophys Acta Year: 2014 Type: Article Affiliation country: Japan

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