The alpha subunit of nitrile hydratase is sufficient for catalytic activity and post-translational modification

Biochemistry

Volumn 53, Issue 24, 2014, Pages 3990-3994

  Nelp, Micah T ^a   Astashkin, Andrei V ^a   Breci, Linda A ^a   McCarty, Reid M ^a   Bandarian, Vahe ^a  

^a University of Arizona   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; MASS SPECTROMETRY;

CATALYTIC EFFICIENCIES; COORDINATION ENVIRONMENT; HETERODIMERIC ENZYMES; NATURAL SUBSTRATES; POST-TRANSLATIONAL MODIFICATIONS; STEADY-STATE KINETICS; STREPTOMYCES RIMOSUS; SUBSTRATE SPECIFICITY;

CYANIDES;

HYDROLYASE; NICOTINIC ACID; NITRILE HYDRATASE; NITRILE HYDRATASE ALPHA SUBUNIT; RECOMBINANT PROTEIN; SANGIVAMYCIN; TOYJ PROTEIN; TOYJKL PROTEIN; TOYOCAMYCIN; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROTEIN PURIFICATION; STEADY STATE; STREPTOMYCES RIMOSUS;

ACTINOMYCETALES; BACTERIAL PROTEINS; CATALYSIS; HYDRO-LYASES; KINETICS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN SUBUNITS; PYRIDINES; RECOMBINANT PROTEINS;

EID: 84903153895     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500260j     Document Type: Article

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