Biochemical and structural properties of chimeras constructed by exchange of cofactor-binding domains in alcohol dehydrogenases from thermophilic and mesophilic microorganisms

Biochemistry

Volumn 49, Issue 9, 2010, Pages 1943-1953

  Goihberg, Edi ^a   Peretz, Moshe ^a   Tel Or, Shoshana ^a   Dym, Orly ^b   Shimon, Linda ^c   Frolow, Felix ^d   Burstein, Yigal ^a,c  

^a Department of Organic Chemistry ^*  (Israel)

^b Israel Structural Proteomics Center   (Israel)

^c WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^d TEL AVIV UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

3D STRUCTURE; ALCOHOL DEHYDROGENASE; BINDING DOMAIN; CHIMERIC PROTEINS; COFACTORS; DOMAIN EXCHANGE; ELECTROSTATIC INTERACTIONS; ENTAMOEBA HISTOLYTICA; MESOPHILIC; MESOPHILIC BACTERIA; MESOPHILIC COUNTERPARTS; PROLINE RESIDUES; PROTOZOAN PARASITES; THERMAL STABILITY; THERMOPHILIC ENZYMES; THREE DIMENSIONAL (3D) STRUCTURES;

ENZYMES; OLIGOMERIZATION; THERMOGRAVIMETRIC ANALYSIS; THREE DIMENSIONAL;

THERMODYNAMIC STABILITY;

ALCOHOL DEHYDROGENASE; CHIMERIC PROTEIN; PROLINE;

ALPHA CHAIN; ARTICLE; CHIMERA; CLOSTRIDIUM BEIJERINCKII; CONTROLLED STUDY; DIMERIZATION; ELECTRICITY; ENTAMOEBA HISTOLYTICA; ENZYME PURIFICATION; ENZYME STRUCTURE; GENE OVEREXPRESSION; HORSE; LIVER; MOLECULAR CLONING; MOLECULAR INTERACTION; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTOZOON; SITE DIRECTED MUTAGENESIS; SUBSTITUTION REACTION; THERMOANAEROBACTER; THERMOANAEROBACTER BROCKII; THERMOPHILE; THERMOSTABILITY;

ALCOHOL OXIDOREDUCTASES; ANIMALS; BACTERIAL PROTEINS; CLOSTRIDIUM BEIJERINCKII; CRYSTALLOGRAPHY, X-RAY; ENTAMOEBA HISTOLYTICA; ENZYME STABILITY; MUTAGENESIS, SITE-DIRECTED; MUTANT CHIMERIC PROTEINS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTOZOAN PROTEINS; TEMPERATURE; THERMOANAEROBACTER;

BACTERIA (MICROORGANISMS); CLOSTRIDIUM; ENTAMOEBA HISTOLYTICA; EQUIDAE; PROTOZOA; THERMOANAEROBACTER;

EID: 77749255402     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi901730x     Document Type: Article

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