Hidden Activities of Tyrosine Phenol-Lyase and Tryptophan Indole-Lyase: Recombinant PLP-Dependent C–C Lyases as New Biocatalysts for Antimicrobial Thiosulfinate Generation
Vitalia V. Kulikova, Svetlana V. Revtovich, Kseniya P. Levshina, Yaroslav V. Kozmenko, Natalya V. Anufrieva, Elena A. Morozova, Pavel N. Solyev
TL;DR
This paper discovers new enzyme activities that can produce antimicrobial compounds from specific amino acid derivatives.
Contribution
First demonstration that C–C lyases can act as C–S lyases to synthesize thiosulfinates from cysteine sulfoxides.
Findings
TPL and Trpase, along with MGL, can degrade petiveriin into thiosulfinates.
Enzyme-generated thiosulfinates show antimicrobial activity against pathogens like Candida albicans and Staphylococcus aureus.
Abstract
Background: Lyases are used in a wide scope of applications, making them invaluable tools in both industrial biotechnology and molecular biology. Many examples of lyases belong to the extensive family of pyridoxal 5′-phosphate (PLP)-dependent enzymes, which catalyze numerous reactions involved in amino acid metabolism, like tryptophan indole-lyase (Trpase or Tnase), tyrosine phenol-lyase (TPL), and methionine γ-lyase (MGL). Beyond their role in physiological processes, these lyases can also facilitate the synthesis of other biologically active products from non-canonical substrates. Objectives: Up till now there were only two C–S lyases known for the thiosulfinates’ biosynthesis from S-substituted L-cysteine sulfoxides—alliinase and MGL. Our study reveals for the first time that C–C lyases are capable of C–S lyase activity in reactions with S-alkyl, S-allyl and S-benzyl cysteine…
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Taxonomy
TopicsNitrogen and Sulfur Effects on Brassica · Sulfur Compounds in Biology · Folate and B Vitamins Research