Assessing the catalytic activity of three different sources of tyrosinase: A study of the oxidation of mono- and difluorinated monophenols
AuthorsMartin, Leona B.
McMahon, Aoife M.
O'Connor, Kevin E.
Article (Published version)
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Tyrosinase (tyr) purified from Pseudomonas putida F6, Streptomyces antibioticus, and Agaricus bisporus (mushroom) oxidises 3 regioisomers of fluorophenol as well as 3,4-difluorophenol (3,4FP). The catalytic efficiency (k(cat)/K-m) of tyrosinase towards any one substrate is different for each enzyme source. Oftentimes a large difference in affinity (K-m), and turnover (k(cat)) is observed for different enzyme sources with the same substrate. The best catalytic efficiency towards a fluorinated substrate was observed for P putida F6 tyr with 4-fluorophenol (4FP). The presence of a second fluorine on the aromatic ring (3,4FP) resulted in a decrease in the catalytic efficiency of all three enzymes compared to values for 4FP. However, the Km value for 3,4FP decreased for P. putida F6 tyr indicating a higher affinity for P. putida F6 tyr for 3,4FP compared to 4FP. Furthermore the k(cat) value for 3,4FP increased for mushroom tyr in comparison to the value for 4FP indicating a higher maximum t...urnover of 3,4FP compared to 4FP for mushroom tyr. All three sources of tyr exhibited lower catalytic efficiencies for 3-fluorophenol (3FP) and 2-fluorophenol (2FP) compared to 4FP. However, the K-m value for 2FP was lower than that for 3FP for both S. antibioticus and mushroom tyr indicating a higher affinity for 2FP over 3FP. (C) 2008 Elsevier Inc. All rights reserved.
Keywords:Pseudomonas putida F6 / Streptomyces antibioticus / Agaricus bisporus (mushroom) / tyrosinase / 4-fluorophenol / 3,4-difluorophenol / 3-fluorophenol / 2-fluorophenol
Source:Enzyme and Microbial Technology, 2008, 43, 3, 297-301
- Elsevier Science Inc, New York