Biochemical characterization of thermostable ω-transaminase from Sphaerobacter thermophilus and its application for producing aromatic β- and γ-amino acids

Enzyme and Microbial Technology

Volumn 87-88, Issue , 2016, Pages 52-60

  Mathew, Sam ^a   Nadarajan, Saravanan Prabhu ^b   Chung, Taeowan ^a   Park, Hyun Ho ^a   Yun, Hyungdon ^b  

^a Yeungnam University   (South Korea)

^b Konkuk University   (South Korea)

Author keywords

Asymmetric synthesis; Beta amino acid; Gamma amino acid; Kinetic resolution; Thermostable enzyme; Transaminase

Indexed keywords

AMINO ACIDS; ENZYME ACTIVITY; SUBSTRATES;

ASYMMETRIC SYNTHESIS; BETA AMINO ACIDS; BIOCHEMICAL CHARACTERIZATION; ENANTIOMERIC EXCESS; KINETIC RESOLUTION; OMEGA-TRANSAMINASES; SUBSTRATE SPECIFICITY; THERMOSTABLE ENZYMES;

ENZYMES;

AMINOTRANSFERASE; AROMATIC AMINO ACID; BETA AMINO ACID; GAMMA AMINO ACID; OMEGA TRANSAMINASE; PHENYLALANINE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN;

AMINO ACID SYNTHESIS; ARTICLE; ASYMMETRIC SYNTHESIS; BIOCATALYST; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STABILITY; EUBACTERIUM; HIGH TEMPERATURE; PROTEIN EXPRESSION; SPHAEROBACTER THERMOPHILUS; THERMOPHILIC BACTERIUM; THERMOSTABILITY; AMINO ACID SUBSTITUTION; BACTERIAL GENE; BIOCATALYSIS; BIOSYNTHESIS; CHEMISTRY; CHLOROFLEXI; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR MODEL; SITE DIRECTED MUTAGENESIS; STEREOISOMERISM; TEMPERATURE;

AMINO ACID SUBSTITUTION; AMINO ACIDS, AROMATIC; BACTERIAL PROTEINS; BIOCATALYSIS; CATALYTIC DOMAIN; CHLOROFLEXI; ENZYME STABILITY; GENES, BACTERIAL; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; STEREOISOMERISM; SUBSTRATE SPECIFICITY; TEMPERATURE; TRANSAMINASES;

EID: 84959524314     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2016.02.013     Document Type: Article

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