A novel chimeric amine dehydrogenase shows altered substrate specificity compared to its parent enzymes

Chemical Communications

Volumn 50, Issue 95, 2014, Pages 14953-14955

  Bommarius, Bettina R ^a   Schürmann, Martin ^b   Bommarius, Andreas S ^a,c  

^a Georgia Institute of Technology   (United States)

^b DSM RESOLVE   (Netherlands)

^c GEORGIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETOPHENONE; ADAMANTANE DERIVATIVE; AMINE DEHYDROGENASE; BENZYLAMINE; CHIMERIC PROTEIN; ETHYLAMINE; KETONE; LEUCINE; PHENYLALANINE; AMINE; HYBRID PROTEIN; LEUCINE DEHYDROGENASE; OXIDOREDUCTASE; PHENYLALANINE OXIDASE;

AMINATION; AMINO ACID SEQUENCE; ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; DOMAIN SHUFFLING; ENZYME KINETICS; ENZYME SPECIFICITY; PROTEIN STRUCTURE; TEMPERATURE; CHEMISTRY; GENETICS;

AMINATION; AMINES; AMINO ACID OXIDOREDUCTASES; KETONES; LEUCINE DEHYDROGENASE; RECOMBINANT FUSION PROTEINS; SUBSTRATE SPECIFICITY;

EID: 84908628081     PISSN: 13597345     EISSN: 1364548X     Source Type: Journal    
DOI: 10.1039/c4cc06527a     Document Type: Article

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