The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase

Cell

Volumn 93, Issue 1, 1998, Pages 103-109

  Zheng, Wenjin ^a   Johnston, Stephen Albert ^a   Joshua Tor, Leemor ^b  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b Howard Hughes Medical Institute Cold Spring Harbor Laboratory Cold Spring Harbor   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE; BLEOMYCIN; BLEOMYCIN HYDROLASE; CARBOXYPEPTIDASE; CYSTEINE PROTEINASE; LIGASE; PROTEINASE; UNCLASSIFIED DRUG;

BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; DRUG BINDING; DRUG INACTIVATION; ENZYME ACTIVE SITE; ENZYME MECHANISM; NONHUMAN; PRIORITY JOURNAL; REVIEW;

EID: 0032478519     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81150-2     Document Type: Article

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