Protease C of Erwinia chrysanthemi: the crystal structure and role of amino acids Y228 and E189
- 23 November 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 314 (2) , 187-193
- https://doi.org/10.1006/jmbi.2001.5124
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Kinetic Characterization of the Serralysins: A Divergent Catalytic Mechanism Pertaining to Astacin-Type MetalloproteasesBiochemistry, 1997
- Structure of astacin with a transition-state analogue inhibitorNature Structural & Molecular Biology, 1996
- The Metzincin-Superfamily of Zinc-PeptidasesPublished by Springer Nature ,1996
- Crystal Structure of a Complex BetweenSerratia marcescensMetallo-protease and an Inhibitor fromErwinia chrysanthemiJournal of Molecular Biology, 1995
- Crystal Structure of the 50 Kda Metallo Protease from Serratia marcescensJournal of Molecular Biology, 1994
- Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’FEBS Letters, 1993
- Refined 1·8 Å X-ray Crystal Structure of Astacin, a Zinc-endopeptidase from the Crayfish Astacus astacus L.: Structure Determination, Refinement, Molecular Structure and Comparison with ThermolysinJournal of Molecular Biology, 1993
- Protease Secretion by Erwinia chrysanthemiJournal of Biological Chemistry, 1989
- The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis.Published by Elsevier ,1988
- A Correlation of Reaction RatesJournal of the American Chemical Society, 1955