The Laccase of Myrothecium roridum VKM F-3565: A New Look at Fungal Laccase Tolerance to Neutral and Alkaline Conditions.

Autor: Renfeld ZV; G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Pushchino Center for Biological Research, Russian Academy of Sciences, Prosp. Nauki 5, Pushchino, Moscow Region, 142290, Russian Federation., Chernykh AM; G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Pushchino Center for Biological Research, Russian Academy of Sciences, Prosp. Nauki 5, Pushchino, Moscow Region, 142290, Russian Federation., Egorova Shebanova AD; G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Pushchino Center for Biological Research, Russian Academy of Sciences, Prosp. Nauki 5, Pushchino, Moscow Region, 142290, Russian Federation., Baskunov BP; G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Pushchino Center for Biological Research, Russian Academy of Sciences, Prosp. Nauki 5, Pushchino, Moscow Region, 142290, Russian Federation., Gaidina AS; G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Pushchino Center for Biological Research, Russian Academy of Sciences, Prosp. Nauki 5, Pushchino, Moscow Region, 142290, Russian Federation., Myasoedova NM; G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Pushchino Center for Biological Research, Russian Academy of Sciences, Prosp. Nauki 5, Pushchino, Moscow Region, 142290, Russian Federation., Moiseeva OV; G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Pushchino Center for Biological Research, Russian Academy of Sciences, Prosp. Nauki 5, Pushchino, Moscow Region, 142290, Russian Federation., Kolomytseva MP; G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Pushchino Center for Biological Research, Russian Academy of Sciences, Prosp. Nauki 5, Pushchino, Moscow Region, 142290, Russian Federation.
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2023 Feb 14; Vol. 24 (4), pp. e202200600. Date of Electronic Publication: 2023 Jan 18.
DOI: 10.1002/cbic.202200600
Abstrakt: Most of the currently known fungal laccases show their maximum activity under acidic environmental conditions. It is known that a decrease in the activity of a typical laccase at neutral or alkaline pH values is the result of an increase in the binding of the hydroxide anion to the T2/T3 copper center, which prevents the transfer of an electron from the T1 Cu to the trinuclear copper center. However, evolutionary pressure has resolved the existing limitations in the catalytic mechanism of laccase, allowing such enzymes to be functionally active under neutral/alkaline pH conditions, thereby giving fungi an advantage for their survival. Combined molecular and biochemical studies, homological modeling, calculation of the electrostatic potential on the Connolly surface at pH 5.0 and 7.0, and structural analysis of the novel alkaliphilic laccase of Myrothecium roridum VKM F-3565 and alkaliphilic and acidophilic fungal laccases with a known structure allowed a new intramolecular channel near the one of the catalytic aspartate residues at T2-copper atom to be found. The amino acid residues of alkaliphilic laccases forming this channel can presumably serve as proton donors for catalytic aspartates under neutral conditions, thus ensuring proper functioning. For the first time for ascomycetous laccases, the production of new trimeric products of phenylpropanoid condensation under neutral conditions has been shown, which could have a potential for use in pharmacology.
(© 2022 Wiley-VCH GmbH.)
Databáze: MEDLINE
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