Assessing the catalytic activity of three different sources of tyrosinase: A study of the oxidation of mono- and difluorinated monophenols
No Thumbnail
Authors
Martin, Leona B.Nikodinović-Runić, Jasmina
McMahon, Aoife M.
Vijgenboom, Erik
O'Connor, Kevin E.
Article (Published version)
Metadata
Show full item recordAbstract
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-fluorophenolSource:
Enzyme and Microbial Technology, 2008, 43, 3, 297-301Publisher:
- Elsevier Science Inc, New York
DOI: 10.1016/j.enzmictec.2008.03.010
ISSN: 0141-0229
WoS: 000258217800011
Scopus: 2-s2.0-46749111362
Collections
Institution/Community
Inovacioni centar / Innovation CentreTY - JOUR AU - Martin, Leona B. AU - Nikodinović-Runić, Jasmina AU - McMahon, Aoife M. AU - Vijgenboom, Erik AU - O'Connor, Kevin E. PY - 2008 UR - https://cherry.chem.bg.ac.rs/handle/123456789/960 AB - 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 turnover 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. PB - Elsevier Science Inc, New York T2 - Enzyme and Microbial Technology T1 - Assessing the catalytic activity of three different sources of tyrosinase: A study of the oxidation of mono- and difluorinated monophenols VL - 43 IS - 3 SP - 297 EP - 301 DO - 10.1016/j.enzmictec.2008.03.010 ER -
@article{ author = "Martin, Leona B. and Nikodinović-Runić, Jasmina and McMahon, Aoife M. and Vijgenboom, Erik and O'Connor, Kevin E.", year = "2008", abstract = "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 turnover 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.", publisher = "Elsevier Science Inc, New York", journal = "Enzyme and Microbial Technology", title = "Assessing the catalytic activity of three different sources of tyrosinase: A study of the oxidation of mono- and difluorinated monophenols", volume = "43", number = "3", pages = "297-301", doi = "10.1016/j.enzmictec.2008.03.010" }
Martin, L. B., Nikodinović-Runić, J., McMahon, A. M., Vijgenboom, E.,& O'Connor, K. E.. (2008). Assessing the catalytic activity of three different sources of tyrosinase: A study of the oxidation of mono- and difluorinated monophenols. in Enzyme and Microbial Technology Elsevier Science Inc, New York., 43(3), 297-301. https://doi.org/10.1016/j.enzmictec.2008.03.010
Martin LB, Nikodinović-Runić J, McMahon AM, Vijgenboom E, O'Connor KE. Assessing the catalytic activity of three different sources of tyrosinase: A study of the oxidation of mono- and difluorinated monophenols. in Enzyme and Microbial Technology. 2008;43(3):297-301. doi:10.1016/j.enzmictec.2008.03.010 .
Martin, Leona B., Nikodinović-Runić, Jasmina, McMahon, Aoife M., Vijgenboom, Erik, O'Connor, Kevin E., "Assessing the catalytic activity of three different sources of tyrosinase: A study of the oxidation of mono- and difluorinated monophenols" in Enzyme and Microbial Technology, 43, no. 3 (2008):297-301, https://doi.org/10.1016/j.enzmictec.2008.03.010 . .