Structural insights into cold inactivation of tryptophanase and cold adaptation of subtilisin S41

Biopolymers

Volumn 89, Issue 5, 2008, Pages 354-359

  Almog, Orna ^a   Kogan, Anna ^a   de Leeuw, Marina ^a   Gdalevsky, Garik Y ^a   Cohen Luria, Rivka ^a   Parola, Abraham H ^a  

^a BEN GURION UNIVERSITY OF THE NEGEV   (Israel)

Author keywords

Crystal structure; Hyrophobic interactions; PLP dependent enzymes; Psychro meso and thermophilic organisms; Quaternary; Surface charge; Thermolabile

Indexed keywords

AMINES; AMINO ACIDS; CATALYSTS; ENZYMES; HYDROPHOBICITY; ORGANIC ACIDS; PROTEINS;

ACIDIC RESIDUES; AMINO-ACID SEQUENCES; CHARGED RESIDUES; COLD ADAPTATION; COLD ENVIRONMENTS; COLD TEMPERATURES; CRYSTAL STRUCTURE; HYDROPHOBIC RESIDUES; HYROPHOBIC INTERACTIONS; LOW TEMPERATURE; MESOPHILIC; MOLECULAR FEATURES; OLIGOMERIC ENZYMES; OPTIMAL ACTIVITY; PLP-DEPENDENT ENZYMES; PSYCHRO-MESO-AND THERMOPHILIC ORGANISMS; PYRIDOXAL PHOSPHATE; QUATERNARY; SPECIFIC INTERACTIONS; SPECIFIC SURFACES; STRUCTURAL INSIGHTS; SUBTILISIN; SURFACE CHARGE; THERMAL STABILITY; THERMOLABILE; TRYPTOPHANASE;

GENE ENCODING;

PHOSPHATE; POLYPEPTIDE; PROTEIN SUBUNIT; PROTEINASE; SUBTILISIN; TRYPTOPHANASE;

ACIDITY; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BIOTECHNOLOGY; COLD ACCLIMATIZATION; CRYSTAL STRUCTURE; DISSOCIATION; ENTROPY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME DEGRADATION; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; HYDROGEN BOND; HYDROPHILICITY; INCUBATION TEMPERATURE; LOW TEMPERATURE; NONHUMAN; PROTEIN ASSEMBLY; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; RESIDUE ANALYSIS; STRUCTURE ANALYSIS; THERMOSTABILITY; VIBRIO; ADAPTATION; CHEMICAL STRUCTURE; COLD; COMPARATIVE STUDY; ENZYME ACTIVATION; ENZYME STABILITY; PHYSIOLOGY; PROTEIN CONFORMATION; TEMPERATURE;

VIBRIO;

ADAPTATION, PHYSIOLOGICAL; COLD; ENZYME ACTIVATION; ENZYME STABILITY; MODELS, MOLECULAR; PROTEIN CONFORMATION; SUBTILISIN; TEMPERATURE; TRYPTOPHANASE;

EID: 46749089070     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.20866     Document Type: Article

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