PMID:7663946
| Citation |
Bravo, J, Verdaguer, N, Tormo, J, Betzel, C, Switala, J, Loewen, PC and Fita, I (1995) Crystal structure of catalase HPII from Escherichia coli. Structure 3:491-502 |
|---|---|
| Abstract |
Catalase is a ubiquitous enzyme present in both the prokaryotic and eukaryotic cells of aerobic organisms. It serves, in part, to protect the cell from the toxic effects of small peroxides. Escherichia coli produces two catalases, HPI and HPII, that are quite distinct from other catalases in physical structure and catalytic properties. HPII, studied in this work, is encoded by the katE gene, and has been characterized as an oligomeric, monofunctional catalase containing one cis-heme d prosthetic group per subunit of 753 residues. |
| Links | |
| Keywords |
Amino Acid Sequence; Animals; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Binding Sites; Catalase/chemistry; Catalase/genetics; Cattle; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/genetics; Fungal Proteins/chemistry; Heme/chemistry; Hydrogen Bonding; Liver/enzymology; Micrococcus/enzymology; Models, Molecular; Molecular Sequence Data; Penicillium/enzymology; Protein Conformation; Proteus mirabilis/enzymology; Sequence Alignment; Sequence Homology, Amino Acid; Structure-Activity Relationship |
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