Crystal structure of a feruloyl esterase belonging to the tannase family: A disulfide bond near a catalytic triad

Proteins: Structure, Function and Bioinformatics

Volumn 82, Issue 10, 2014, Pages 2857-2867

  Suzuki, Kentaro ^a   Hori, Akane ^b   Kawamoto, Kazusa ^b   Thangudu, Ratna Rajesh ^c,d   Ishida, Takuya ^a   Igarashi, Kiyohiko ^a   Samejima, Masahiro ^a   Yamada, Chihaya ^a   Arakawa, Takatoshi ^a   Wakagi, Takayoshi ^a   Koseki, Takuya ^b   Fushinobu, Shinya ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b YAMAGATA UNIVERSITY   (Japan)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

^d ESAC Inc   (United States)

Author keywords

Alpha beta hydrolase fold; Aspergillus oryzae; Carboxylesterase; Catalytic triad; Disulfide; Enzyme structure; ESTHER database; Lipase; X ray crystallography

Indexed keywords

CYSTEINE; FERULOYL ESTERASE; HISTIDINE; HYDROLASE; SERINE; TANNASE; UNCLASSIFIED DRUG; ARCHAEAL PROTEIN; BACTERIAL PROTEIN; CARBOXYLESTERASE; CYSTINE; FUNGAL PROTEIN; LIGAND; MUTANT PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; ASPERGILLUS ORYZAE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; MOLECULAR DOCKING; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYMOLOGY; GENETICS; METABOLISM; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN DATABASE; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT;

ASPERGILLUS ORYZAE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARCHAEAL PROTEINS; ASPERGILLUS ORYZAE; BACTERIAL PROTEINS; BIOCATALYSIS; CARBOXYLIC ESTER HYDROLASES; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CYSTINE; DATABASES, PROTEIN; FUNGAL PROTEINS; LIGANDS; MODELS, MOLECULAR; MOLECULAR DOCKING SIMULATION; MUTANT PROTEINS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

EID: 84928330089     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24649     Document Type: Article

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