Difference between revisions of "Part:BBa K137067"
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Latest revision as of 12:14, 7 August 2021
katG
This is one of the two catalases from E. coli.
Information contributed by City of London UK (2021)
Part information is collated here to help future users of the BioBrick registry.
Metadata:
- Group: City of London UK 2021
- Author: Lucas Ng
- Summary: Added information collated from existing scientific studies
katG is a bifunctional enzyme, displaying both catalase activity and broad-spectrum peroxidase activity. Additionally, it has roles as a NADH oxidase, INH lyase and isonicotinoyl-NAD synthase. [1]
It's cofactor is heme B (iron-protoporphyrin IX), of which it binds two groups per tetramer [2].
Following biosynthesis, the N-terminus is blocked. Furthermore, the three residue Trp-Tyr-Met cross-link forms, which is important for its activity as a catalase[2].
Catalase reaction
The optimum pH is 7.5 [1] [2]:
| pH | KM (mM) | Vmax (µmol/min/mg enzyme) |
|---|---|---|
| 5.5-6.0 | 35 | 3730 |
| 7.0 | 4.2 | 2220 |
| 7.5 | 3.9 |
Peroxidase reaction
The optimum pH is 4.25 [1] [2]:
- With H2O2, KM = 60 µM
- With ABTS, KM = 24 µM and Vmax = 18 µmol/min/mg enzyme
References
- ↑ 1.0 1.1 1.2 Singh, Rahul, Ben Wiseman, Taweewat Deemagarn, Vikash Jha, Jacek Switala, and Peter C. Loewen. 2008. “Comparative Study of Catalase-Peroxidases (KatGs).” Archives of Biochemistry and Biophysics 471 (2): 207–14. https://doi.org/10.1016/j.abb.2007.12.008.
- ↑ 2.0 2.1 2.2 2.3 Claiborne, A., and I. Fridovich. 1979. “Purification of the O-Dianisidine Peroxidase from Escherichia Coli B. Physicochemical Characterization and Analysis of Its Dual Catalatic and Peroxidatic Activities.” The Journal of Biological Chemistry 254 (10): 4245–52. https://pubmed.ncbi.nlm.nih.gov/374409.
- ↑ “Rhea - Annotated Reactions Database.” n.d. Rhea. Accessed July 26, 2021. https://www.rhea-db.org/rhea/30275.
- ↑ “Rhea - Annotated Reactions Database.” n.d. Rhea. Accessed July 26, 2021. https://www.rhea-db.org/rhea/20309.