Structural and Functional Roles of Asparagine 175 in the Cysteine Protease Papain
Open Access
- 1 July 1995
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (28) , 16645-16652
- https://doi.org/10.1074/jbc.270.28.16645
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Structure of papain refined at 1.65 Å resolutionJournal of Molecular Biology, 1984
- Effect of cysteine-25 on the ionization of histidine-159 in papain as determined by proton nuclear magnetic resonance spectroscopy. Evidence for a histidine-159-cysteine-25 ion pair and its possible role in catalysisBiochemistry, 1981
- Proton Equilibria in the Binding of Zn2+ and of Methylmercuric Iodide to PapainEuropean Journal of Biochemistry, 1976
- Potentiometric determination of ionizations at the active site of papainBiochemistry, 1976
- Binding of chloromethyl ketone substrate analogs to crystalline papainBiochemistry, 1976
- Mercaptide—imidazolium ion‐pair: The reactive nucleophile in papain catalysisFEBS Letters, 1974
- 14 Papain and Other Plant Sulfhydryl Proteolytic EnzymesPublished by Elsevier ,1971
- The Structure of PapainAdvances in Protein Chemistry, 1971
- Structure of PapainNature, 1968
- A STUDY OF SOME THIOL ESTER HYDROLYSES AS MODELS FOR THE DEACYLATION STEP OF PAPAIN-CATALYSED HYDROLYSESBiochemical Journal, 1965