Structural insights into the substrate specificity and activity of ervatamins, the papain-like cysteine proteases from a tropical plant, Ervatamia coronaria

FEBS Journal

Volumn 275, Issue 3, 2008, Pages 421-434

  Ghosh, Raka ^a   Chakraborty, Sibani ^a   Chakrabarti, Chandana ^a   Dattagupta, Jiban Kanti ^a   Biswas, Sampa ^a  

^a SAHA INSTITUTE OF NUCLEAR PHYSICS   (India)

Author keywords

3D structures; Inhibitor complexes; Multiple enzymes; Plant cysteine proteases; Proteolytic activity

Indexed keywords

CYSTEINE PROTEINASE; ERVATAMIN A; ERVATAMIN B; ERVATAMIN C; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; PAPAIN; UNCLASSIFIED DRUG;

AMINO ACID COMPOSITION; AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; HYDROPHOBICITY; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL;

APOCYNACEAE; BINDING SITES; COMPUTER SIMULATION; CYSTEINE ENDOPEPTIDASES; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PAPAIN; PLANT PROTEINS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ANALYSIS, DNA; SUBSTRATE SPECIFICITY;

TABERNAEMONTANA DIVARICATA;

EID: 38349070259     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06211.x     Document Type: Article

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