The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad

Proceedings of the National Academy of Sciences of the United States of America

Volumn 97, Issue 26, 2000, Pages 14097-14102

  Håkansson, Kjell ^a   Wang, Andrew H J ^a   Miller, Charles G ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

Peptidase E; Protease; Protein crystallography; Serine hydrolase

Indexed keywords

DIPEPTIDASE; MICROSOMAL AMINOPEPTIDASE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SALMONELLA TYPHIMURIUM;

CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DIPEPTIDASES; GLUTAMIC ACID; HISTIDINE; MODELS, MOLECULAR; PROTEIN STRUCTURE, SECONDARY; SALMONELLA TYPHIMURIUM; SERINE;

EID: 0034687682     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.260376797     Document Type: Article

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