@article{4b6ce86bf60d4e9a9df9325cf8e46bf6,
title = "The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase",
abstract = "The Gal6 protease is in a class of cysteine peptidases identified by their ability to inactivate the anti-cancer drug bleomycin. The protein forms a barrel structure with the active sites embedded in a channel as in the proteasome. In Gal6 the C termini lie in the active site clefts. We show that Gal6 acts as a carboxypeptidase on its C terminus to convert itself to an aminopeptidase and peptide ligase. The substrate specificity of the peptidase activity is determined by the position of the C terminus of Gal6 rather than the sequence of the substrate. We propose a model to explain these diverse activities and Gal6's singular ability to inactivate bleomycin.",
author = "Wenjin Zheng and Johnston, {Stephen Albert} and Leemor Joshua-Tor",
note = "Funding Information: We thank Julie Rosenbaum for protein purification and crystallizations, Dr. Malcolm Capel (at beamline X12B), Dr. Lonny Berman (at beamline X25), and Dr. Felix Frolow for help and support with data collection at the National Synchrotron Light Source at Brookhaven National Laboratory. We thank Dr. David Corey, Dr. Clive Slaughter, and Dr. Meg Phillips (University of Texas-Southwestern) for help and lab facilities. We thank the Johnston and Joshua-Tor labs and Dr. Winship Herr for comments and suggestions. This work was supported by grants from National Institutes of Health (CA67982) and Tobacco Research Council (4247) to S. A. J., a Molecular Cardiology Training Fellowship of NIHLB to W. Z., and National Institutes of Health (R01-CA71746), the Arnold and Mabel Beckman Foundation, the Robertson Research Fund, and the Cold Spring Harbor Association Fellowship to L. J.",
year = "1998",
month = apr,
day = "3",
doi = "10.1016/S0092-8674(00)81150-2",
language = "English (US)",
volume = "93",
pages = "103--109",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "1",
}