Enzyme adaptation to alkaline pH: Atomic resolution (1.08 Å) structure of phosphoserine aminotransferase from Bacillus alcalophilus

Protein Science

Volumn 14, Issue 1, 2005, Pages 97-110

  Dubnovitsky, Anatoly P ^a   Kapetaniou, Evangelia G ^a   Papageorgiou, Anastassios C ^a,b  

^a UNIVERSITY OF TURKU   (Finland)

^b TURKU CENTRE FOR BIOTECHNOLOGY   (Finland)

Author keywords

Alkaliphilicity; Phosphoserine; Protein stability; Pyridoxal 5 phosphate; Schiff base; X ray crystallography

Indexed keywords

AMINOTRANSFERASE; PHOSPHOSERINE; PHOSPHOSERINE AMINOTRANSFERASE; PYRIDOXAL 5 PHOSPHATE; SCHIFF BASE; UNCLASSIFIED DRUG;

ADAPTATION; ALKALINITY; ARTICLE; BACILLUS; BACILLUS ALCALOPHILUS; BINDING SITE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; HYDROGEN BOND; HYDROPHILICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN STABILITY; RESIDUE ANALYSIS; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

ADAPTATION, PHYSIOLOGICAL; AMINO ACID SEQUENCE; BACILLUS; ENZYME ACTIVATION; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SURFACE PROPERTIES; TRANSAMINASES; VITAMIN B 6;

BACILLUS ALCALOPHILUS; BACILLUS CIRCULANS SUBSP. ALKALOPHILUS; ESCHERICHIA COLI;

EID: 11144221715     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041029805     Document Type: Article

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