This domain is found at the C-terminus of a variety of large catalase enzymes from bacteria. Structurally it is related to class I glutamine amidotransferase domains. The precise molecular function of this domain is uncertain. [1]. 10488114. Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli. Mate MJ, Sevinc MS, Hu B, Bujons J, Bravo J, Switala J, Ens W, Loewen PC, Fita I;. J Biol Chem. 1999;274:27717-27725. [2]. 11455600. Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli. Melik-Adamyan W, Bravo J, Carpena X, Switala J, Mate MJ, Fita I, Loewen PC;. Proteins. 2001;44:270-281. [3]. 7663946. Crystal structure of catalase HPII from Escherichia coli. Bravo J, Verdaguer N, Tormo J, Betzel C, Switala J, Loewen PC, Fita I;. Structure. 1995;3:491-502. [4]. 12777389. An electrical potential in the access channel of catalases enhances catalysis. Chelikani P, Carpena X, Fita I, Loewen PC;. J Biol Chem. 2003;278:31290-31296. [5]. 21332158. Modulation of heme orientation and binding by a single residue in catalase HPII of Escherichia coli. Jha V, Louis S, Chelikani P, Carpena X, Donald LJ, Fita I, Loewen PC;. Biochemistry. 2011;50:2101-2110. [6]. 22172685. Mutation of Phe413 to Tyr in catalase KatE from Escherichia coli leads to side chain damage and main chain cleavage. Jha V, Donald LJ, Loewen PC;. Arch Biochem Biophys. 2012;525:207-214. [7]. 24223139. Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex. Yonekura K, Watanabe M, Kageyama Y, Hirata K, Yamamoto M, Maki-Yonekura S;. PLoS One. TRUNCATED at 1650 bytes (from Pfam)
- Date:
- 2024-10-16