Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad

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

Volumn 110, Issue 28, 2013, Pages 11302-11307

  Zeiler, Evelyn ^a   List, Anja ^b   Alte, Ferdinand ^b   Gersch, Malte ^a   Wachtel, Rudolf ^a   Poreba, Marcin ^c   Drag, Marcin ^c   Groll, Michael ^b   Sieber, Stephan A ^a  

^a Munich Center for Integrated Protein Science   (Germany)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^c WROCLAW UNIVERSITY OF TECHNOLOGY   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; ASPARTIC ACID; CASEINOLYTIC PROTEASE P1; CASEINOLYTIC PROTEASE P2; PROTEINASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ESCHERICHIA COLI; HYDROLYSIS; LISTERIA MONOCYTOGENES; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE; STAPHYLOCOCCUS AUREUS; WILD TYPE;

AMINO ACID SEQUENCE; CASEINS; CATALYSIS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE HYDROLASES; PROTEOLYSIS; SEQUENCE HOMOLOGY, AMINO ACID;

ESCHERICHIA COLI; LISTERIA MONOCYTOGENES; STAPHYLOCOCCUS AUREUS;

EID: 84879956667     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1219125110     Document Type: Article

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