Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp. I5 suggest reasons for thermal instability

Protein Engineering

Volumn 10, Issue 6, 1997, Pages 665-672

  Wallon, Gerlind ^a,c   Lovett, Susan T ^a   Magyar, Csaba ^b   Svingor, Adam ^b   Szilagyi, Andras ^b   Zàvodszky, Pèter ^b   Ringe, Dagmar ^a   Petsko, Gregory A ^a  

^a BRANDEIS UNIVERSITY   (United States)

^b INSTITUTE OF ENZYMOLOGY   (Hungary)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Cold adaptation; Homology model; Isopropylmalate dehydrogenase; Psychrotroph; Sequence

Indexed keywords

3 ISOPROPYLMALATE DEHYDROGENASE; BACTERIAL ENZYME; PROLINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; ENZYME STABILITY; ENZYME STRUCTURE; MOLECULAR INTERACTION; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; THERMOSTABILITY; VIBRIO;

BACTERIA (MICROORGANISMS); VIBRIO; VIBRIO SP.;

EID: 0030860701     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/10.6.665     Document Type: Article

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