Recombinant Bovine Catalase (CAT), partial

1. Enzyme activity assay and molecular docking revealed that the activity of CAT was slightly inhibited in the presence of Sudan dyes. In comparison, the binding of Sudan II with CAT was slightly stronger than Sudan IV. Also, Sudan II and Sudan IV showed a different impact on the microenvironment of aromatic amino acid residues. PMID: 28613393
2. the decrease in accessible surface area and increase in pKa of important lysine residues were considered as predominant factors in decreased glycation of bovine liver catalase by curcumin. PMID: 28668706
3. ITC confirms the stability of bovine liver catalase (BLC)upon gemini combination. Docking provides support to fluorescence results by presenting the localization site of m-E2-m surfactants near to aromatic residues (mainly Tyr, Trp and Phe) PMID: 27060016
4. Data show that liver catalase is able to tolerate very high levels of the modifying alpha-oxoaldehyde methylglyoxal so that its essential enzymatic function is not impaired. PMID: 26715035
5. The structure of bovine liver catalase determined from a single crystal at 3.2 A resolution by MicroED, is reported. PMID: 25303172
6. These maps demonstrate that it is indeed possible to build atomic models from such crystals and even to determine the charged states of amino acid residues in the Ca(2+)-binding sites of Ca(2+)-ATPase and that of the iron atom in the heme in catalase. PMID: 25730881
7. Data indicate compatible osmolytes, proline, xylitol, and valine destabilize the denatured form of the catalase enzyme and, therefore, increase its disaggregation and thermal stability. PMID: 23249140
8. Flavonoid inhibition of catalase activity is, at least partially, due to the formation of hydrogen bonds between catalase and the flavonoid. PMID: 23567286
9. Comparison of deoxyferrous and oxyferrous complexes of cAOS and MAP with bovine liver catalase elucidates unresolved mechanistic questions in the catalytic cycles of these enzymes PMID: 22104301
10. Catalase is not influenced by the solvent during the catalytic reaction, which represents a lower energy barrier to be crossed in the overall energetics of the reaction, a fact that contributes to the high turnover rate of catalase. PMID: 21529340
11. At room temperature (25.0 degrees C) and higher, the addition of high concentrations of polymer is found to significantly enhance the affinity of SOD for catalase. PMID: 20682270
12. Immunohistochemistry in rectus abdominis muscle from foetuses at 180 and 260 days post-conception PMID: 12441094
13. study of bovine liver catalase and [14C]NADPH and [14C]NADH revealed that unbound NADPH or NADH are substrates for an internal reductase and transhydrogenase reaction respectively PMID: 15456401
14. Overexpression of catalase prevents the stimulation of reactive oxygen species and angiotensinogen mRNA in tubules owing to elevated glucose or angiotensin II in transgenic diabetic mice. PMID: 17342175
15. CAT transgenic mice became obese and hyperglycemic but had normal blood pressure and attenuated albuminuria compared with diabetic mice. PMID: 17977949
16. The structure of the active site of liver catalase B chain (PDB 4BLC) in the radical state (tyrosyl radical) was studied using EPR. PMID: 19639135
17. Data show that acriflavine induced in vitro a profound change in the structure of catalase so that the enzyme could no longer function. PMID: 19723068

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KEGG: bta:531682

STRING: 9913.ENSBTAP00000027941

UniGene: Bt.48925