Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature

EMBO Journal

Volumn 21, Issue 11, 2002, Pages 2509-2516

  Shin, Sejeong ^a   Lee, Tae Hee ^a   Ha, Nam Chul ^a   Koo, Hyun Min ^a   Kim, So yeon ^a   Lee, Heung Soo ^a   Kim, Yu Sam ^a   Oh, Byung Ha ^a  

^a Pohang University of Science and Technology (POSTECH)   (South Korea)

Author keywords

Amidase signature family; Catalytic mechanism; Crystal structure; New protein fold; Novel catalytic triad; Serine hydrolase

Indexed keywords

MALONAMIDASE E2; SERINE DEHYDRATASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BRADYRHIZOBIUM; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MECHANISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; STRUCTURE ACTIVITY RELATION;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BRADYRHIZOBIUM; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; IONS; LYSINE; MALONATES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID; SERINE; SUBSTRATE SPECIFICITY;

BRADYRHIZOBIUM; BRADYRHIZOBIUM JAPONICUM;

EID: 0037013923     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/21.11.2509     Document Type: Article

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