EC Number   |
General Information |
Reference |
|---|
    1.11.1.6 | evolution |
EsCAT contains a highly conserved proximal active-site signature motif (60FDRERIPERVVHAKGAL76) and a proximal heme-ligand signature motif (350RLFSYNDTH358) and exhibits high similarity with other reported CATs |
725156 |
| 1.11.1.6 | evolution |
the dismutation reaction of H2O2 in microorganisms has evolved in three phylogenetically unrelated protein types: monofunctional catalase, catalase-peroxidase and Mn-catalase, phylogenetic analysis, overview. PktA is a clade 3 catalase. The active sites with His65, Ser104, and Asn138, binding sites of the distal region of heme with Val106, Thr128, and Phe143, and proximal sites of heme with Tyr348 and Arg355 are well conserved |
-, 725159 |
| 1.11.1.6 | malfunction |
catalase-negative mutant ROA3 exhibits impaired growth, with the extent of impairment increasing with decreasing temperature, and no growth is detected at 4°C. Aerobic growth in liquid is impaired at 4°C, especially under aeration, but not at higher temperatures (10, 25, or 37°C) |
-, 710945 |
| 1.11.1.6 | malfunction |
the recombinant enzyme shows reduced catalase activity and thermal stability, overview |
-, 724454 |
| 1.11.1.6 | more |
catalase form III protein and crystal structure analysis, overview |
723827 |
| 1.11.1.6 | more |
conserved catalytic active residues are His71, Asn144, and Tyr354 |
725932 |
| 1.11.1.6 | more |
homology modelling, overview |
725096 |
| 1.11.1.6 | more |
reaction mechanism of catalase activity, overview. The iron in the active site is in an uncoupled high-spin ferric oxidation state. The metal ions can be reduced back to the di-ferrous state with dithionite but the deaminase activity is not recovered. Therefore, addition of an excess of H2O2 to [FeII/FeII]-ADEec irreversibly modifies the protein and stabilizes the [FeIII/FeIII] state |
726446 |
| 1.11.1.6 | more |
structure-function analysis, overview. H55 and Y338 in the active site are crucial for the activity. The distal heme ligand binding domain 46RERIPERVVHAKG58 encompasses the essential distal histidine residue, and the proximal heme ligand binding domain 334R-F-Y-D340 harbors the essential proximal tyrosine residue. Other catalase specific motifs are 126VGNNTP131, 107RDXRGFAXKFYT118, and 92RFSTV96. Tyr117 from sequence 107RDXRGFAXKFYT118 is crucial for activity |
724180 |
| 1.11.1.6 | more |
the enzyme exhibits an extraordinarily high catalase activity, active sites residues are His65, Ser104, and Asn138 |
-, 725159 |
