Catalytic properties of the Penicilium vitate catalase. Peroxidatic reaction of the enzyme

Authors

  • N. V. Latyshko Palladin Institute of Biochemistry, NAS of Ukraine 9, Leontovycha Str., Kyiv, Ukraine, 01601 Author
  • L. V. Gudkova Palladin Institute of Biochemistry, NAS of Ukraine 9, Leontovycha Str., Kyiv, Ukraine, 01601 Author
  • O. A. Gudkova Palladin Institute of Biochemistry, NAS of Ukraine 9, Leontovycha Str., Kyiv, Ukraine, 01601 Author

DOI:

https://doi.org/10.7124/bc.000590

Abstract

Peroxidatic activity of the P. vitale catalase with ethanol as a substrate was investigated. It was determined that the peroxidatic activity of the catalase (5–13 U/mg) was over a hundred times less the catalatic activity. Study of the steady-state kinetics showed that kinetic parameters of peroxidatic reaction -Km 5.9 mM and Vmax 0.22 mM/min were lower tlian estimated earlier kinetics of Jlitj catalytic reaction. However, the turnover number kcat -1.1·103 s–1 and catalatic efficiency kM/Km ratio 1.9·105 M s testify the catalase is rather effective peroxidase. The enzyme /fas the rate constant of the peroxidatic action equal to 2.4·104 s–1 M–1 as catalases of other origins.

References

Ramasarma T. Generation of H2O in biomembranes. Biochim Biophys Acta. 1982;694(1):69-93.

Gudkova LV, Kirilenko MT, Levitina TL, Kozlov EA. [Study of the subunit structure of catalase from Penicillium vitale]. Ukr Biokhim Zh. 1985;57(4):29-33.

Gudkova LV, Latyshko NV, Degtiarv RG, Guly? MF, Ianishpolvski? VV, Tertykh VA. [Immobilization of Penicillium vitale Pidopl. et Bilai catalase by inorganic carriers]. Ukr Biokhim Zh. 1980;52(5):614-23.

Vainshtein BK, Melik-Adamyan WR, Barynin VV, Vagin AA, Grebenko AI. Three-dimensional structure of the enzyme catalase. Nature. 1981;293(5831):411-2.

Fita I, Rossmann MG. The active center of catalase. J Mol Biol. 1985;185(1):21-37.

Kozlov EA, Levitina TL, Bobrovskaia MT, Gudkova LV, Latyshko NV, Radomski? NF. [Complete amino acid sequence of catalase from the fungus Penicillium vitale]. Bioorg Khim. 1998;24(3):163-70.

Latyshko NV, Gudkova LV. [The kinetic and catalytic properties of Penicillium vitale catalase]. Ukr Biokhim Zh. 1996;68(2):69-73.

Kulys JJ, Samalius AS, Svirmickas GJ. Electron exchange between the enzyme active center and organic metal. FEBS Lett. 1980;114(1):7-10.

Racker E. Spectrofotometric enzymatic methods for the determination aldehydes and ketoaldehydes. Methods Enzymol. 1957; 3: 293-6.

Samalyus AS. Functioning immobilized on conductive materials heme-containing enzymes: Auth Thesis...kand biol nauk. Vilnius, 1984. 19 p.

Oshino N, Oshino R, Chance B. The characteristics of the "peroxidatic" reaction of catalase in ethanol oxidation. Biochem J. 1973;131(3):555-63.

Klibanov AM, Semenov AN, Samokhin GP, Martinek K. Enzymatic reactions in water-organic mixtures: a criterion for choosing an optimal organic solvent. Bioorg Khim. 1978; 4 (1):82-8

Aebi H. Catalase. Methods of Enzymatic Analysis. New York: Acad, press, 1974. Vol. 2: 673-684.

Published

2000-11-20

Issue

Section

Structure and Function of Biopolymers