Role of the N-terminal domain of endoinulinase from Arthrobacter sp. S37 in regulation of enzyme catalysis

Journal of Biochemistry

Volumn 138, Issue 1, 2005, Pages 27-33

  Kim, Kyoung Yun ^a   Rhee, Sangkee ^a   Kim, Su Il ^a  

^a Seoul National University   (South Korea)

Author keywords

Dimerization; Endoinulinase; Family 32

Indexed keywords

ENDOINULINASE; GLYCOSIDASE; LAMININ; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTHROBACTER; ARTICLE; CATALYSIS; DIMERIZATION; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME STRUCTURE; GEL PERMEATION CHROMATOGRAPHY; GENE SEQUENCE; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ARTHROBACTER; CATALYSIS; CATALYTIC DOMAIN; CHROMATOGRAPHY, GEL; CONSERVED SEQUENCE; DIMERIZATION; GENE EXPRESSION REGULATION; GLYCOSIDE HYDROLASES; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

ARTHROBACTER SP.;

EID: 23344432527     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvi093     Document Type: Article

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