The Unusual Active Site of Gal6/Bleomycin Hydrolase Can Act as a Carboxypeptidase, Aminopeptidase, and Peptide Ligase
Open Access
- 1 April 1998
- Vol. 93 (1) , 103-109
- https://doi.org/10.1016/s0092-8674(00)81150-2
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- cDNA Cloning and Expression of Chicken Aminopeptidase H, Possessing Endopeptidase as well as Aminopeptidase ActivityEuropean Journal of Biochemistry, 1997
- Lactobacillus delbrueckii subsp. lactis DSM7290 pepG gene encodes a novel cysteine aminopeptidaseMicrobiology, 1997
- Autocatalytic Subunit Processing Couples Active Site Formation in the 20S Proteasome to Completion of AssemblyCell, 1996
- Human Bleomycin Hydrolase: Molecular Cloning, Sequencing, Functional Expression, and Enzymatic CharacterizationBiochemistry, 1996
- Crystal Structure of a Conserved Protease That Binds DNA: the Bleomycin Hydrolase, Gal6Science, 1995
- MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresJournal of Applied Crystallography, 1991
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- A fast algorithm for rendering space-filling molecule picturesJournal of Molecular Graphics, 1988
- Crystallographic refinement by simulated annealingJournal of Molecular Biology, 1988
- Bleomycin-resistant cells contain increased bleomycin-hydrolase activitiesBiochemical and Biophysical Research Communications, 1981