McMahon, Aoife M.

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  • McMahon, Aoife M. (1)
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Assessing the catalytic activity of three different sources of tyrosinase: A study of the oxidation of mono- and difluorinated monophenols

Martin, Leona B.; Nikodinović-Runić, Jasmina; McMahon, Aoife M.; Vijgenboom, Erik; O'Connor, Kevin E.

(Elsevier Science Inc, New York, 2008)

TY  - 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 . .
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