Distal side tryptophan, tyrosine and methionine in catalase-peroxidases are covalently linked in solution
- 27 August 2003
- journal article
- Published by Wiley in FEBS Letters
- Vol. 552 (2-3) , 135-140
- https://doi.org/10.1016/s0014-5793(03)00901-3
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Total Conversion of Bifunctional Catalase-Peroxidase (KatG) to Monofunctional Peroxidase by Exchange of a Conserved Distal Side TyrosinePublished by Elsevier ,2003
- Distal Site Aspartate Is Essential in the Catalase Activity of Catalase-PeroxidasesBiochemistry, 2003
- Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7Å resolutionJournal of Molecular Biology, 2003
- The 2.0 Å crystal structure of catalase-peroxidase from Haloarcula marismortuiNature Structural & Molecular Biology, 2002
- The role of distal tryptophan in the bifunctional activity of catalase-peroxidasesBiochemical Society Transactions, 2001
- Effect of Distal Cavity Mutations on the Formation of Compound I in Catalase-PeroxidasesJournal of Biological Chemistry, 2000
- Catalase-Peroxidase from the Cyanobacterium Synechocystis PCC 6803: Cloning, Overexpression in Escherichia coli, and Kinetic CharacterizationBiological Chemistry, 1999
- Crystal structure of recombinant pea cytosolic ascorbate peroxidaseBiochemistry, 1995
- Superfamily of plant, fungal and bacterial peroxidasesCurrent Opinion in Structural Biology, 1992
- Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamilyBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991