The “Rhodanese” Fold and Catalytic Mechanism of 3-Mercaptopyruvate Sulfurtransferases: Crystal Structure of SseA from Escherichia coli
- 9 December 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 335 (2) , 583-593
- https://doi.org/10.1016/j.jmb.2003.10.072
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Escherichia coli GlpE Is a Prototype Sulfurtransferase for the Single-Domain Rhodanese Homology SuperfamilyStructure, 2001
- Characterization of two sulfurtransferase isozymes from Arabidopsis thalianaEuropean Journal of Biochemistry, 2000
- The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme familiesJournal of Molecular Biology, 2000
- Characterization of a sulfurtransferase from Arabidopsis thalianaEuropean Journal of Biochemistry, 2000
- Role of Amino Acid Residues in the Active Site of Rat Liver Mercaptopyruvate SulfurtransferasePublished by Elsevier ,1996
- Cytosolic Mercaptopyruvate Sulfurtransferase Is Evolutionarily Related to Mitochondrial Rhodanese.Journal of Biological Chemistry, 1995
- The sulfurtransferasesFundamental and Applied Toxicology, 1983
- The covalent and tertiary structure of bovine liver rhodaneseNature, 1978
- Steady-state kinetics of 3-mercaptopyruvate sulfurtransferase from bovine kidneyArchives of Biochemistry and Biophysics, 1978
- β-MERCAPTOPYRUVATE, A SUBSTRATE FOR RHODANESEJournal of Biological Chemistry, 1953