TY  - JOUR
AU  - Brooks, Sarah J.
AU  - Nikodinović-Runić, Jasmina
AU  - Martin, Leona
AU  - Doyle, Evelyn M.
AU  - O'Sullivan, Timothy
AU  - Guiry, Patrick J.
AU  - Coulombel, Lydie
AU  - Li, Zhi
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1352
AB  - 1-(3,4-Dihydroxyphenyl) ethanol was produced biocatalytically for the first time using mushroom tyrosinase. 4-Ethylphenol at 1 mM was consumed over 12 min giving 0.23 mM 4-ethylcatechol and 0.36 mM (R/S)-1-(3,4-dihydroxyphenyl) ethanol (ee 0.5 %). Mushroom tyrosinase consumed 4-ethylphenol at 6.7 mu mol min(-1) mg protein(-1) while the rates of formation of 4-ethylcatechol and 1-(3,4-dihydroxyphenyl) ethanol were 1.1 and 1.9 mu mol min(-1) mg protein(-1). Addition of the ascorbic acid, as a reducing agent to biotransformation reactions, increased 4-ethylcatechol formation by 340 %. However, accumulation of 1-(3,4-dihydroxyphenyl) ethanol was not observed in the presence of ascorbic acid. While the 1-(3,4-dihydroxyphenyl) ethanol was racemic, it is the first chiral product produced by tyrosinase starting from a non-chiral substrate.
PB  - Springer, Dordrecht
T2  - Biotechnology Letters
T1  - Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase
VL  - 35
IS  - 5
SP  - 779
EP  - 783
DO  - 10.1007/s10529-013-1148-z
ER  - 

@article{
author = "Brooks, Sarah J. and Nikodinović-Runić, Jasmina and Martin, Leona and Doyle, Evelyn M. and O'Sullivan, Timothy and Guiry, Patrick J. and Coulombel, Lydie and Li, Zhi and O'Connor, Kevin E.",
year = "2013",
abstract = "1-(3,4-Dihydroxyphenyl) ethanol was produced biocatalytically for the first time using mushroom tyrosinase. 4-Ethylphenol at 1 mM was consumed over 12 min giving 0.23 mM 4-ethylcatechol and 0.36 mM (R/S)-1-(3,4-dihydroxyphenyl) ethanol (ee 0.5 %). Mushroom tyrosinase consumed 4-ethylphenol at 6.7 mu mol min(-1) mg protein(-1) while the rates of formation of 4-ethylcatechol and 1-(3,4-dihydroxyphenyl) ethanol were 1.1 and 1.9 mu mol min(-1) mg protein(-1). Addition of the ascorbic acid, as a reducing agent to biotransformation reactions, increased 4-ethylcatechol formation by 340 %. However, accumulation of 1-(3,4-dihydroxyphenyl) ethanol was not observed in the presence of ascorbic acid. While the 1-(3,4-dihydroxyphenyl) ethanol was racemic, it is the first chiral product produced by tyrosinase starting from a non-chiral substrate.",
publisher = "Springer, Dordrecht",
journal = "Biotechnology Letters",
title = "Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase",
volume = "35",
number = "5",
pages = "779-783",
doi = "10.1007/s10529-013-1148-z"
}

Brooks, S. J., Nikodinović-Runić, J., Martin, L., Doyle, E. M., O'Sullivan, T., Guiry, P. J., Coulombel, L., Li, Z.,& O'Connor, K. E.. (2013). Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase. in Biotechnology Letters
Springer, Dordrecht., 35(5), 779-783.
https://doi.org/10.1007/s10529-013-1148-z

Brooks SJ, Nikodinović-Runić J, Martin L, Doyle EM, O'Sullivan T, Guiry PJ, Coulombel L, Li Z, O'Connor KE. Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase. in Biotechnology Letters. 2013;35(5):779-783.
doi:10.1007/s10529-013-1148-z .

Brooks, Sarah J., Nikodinović-Runić, Jasmina, Martin, Leona, Doyle, Evelyn M., O'Sullivan, Timothy, Guiry, Patrick J., Coulombel, Lydie, Li, Zhi, O'Connor, Kevin E., "Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase" in Biotechnology Letters, 35, no. 5 (2013):779-783,
https://doi.org/10.1007/s10529-013-1148-z . .

TY  - JOUR
AU  - Nikodinović-Runić, Jasmina
AU  - Martin, Leona B.
AU  - Babu, Ramesh P.
AU  - Blau, Werner
AU  - O'Connor, Kevin E.
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1008
AB  - Two melanin-overproducing Pseudomonas putida F6 mutants were generated using transposon (Tn5) mutagenesis. Mutants were disrupted in a transcriptional regulator (TR) and a homogentisate 1,2-dioxygenase (HDO) gene. Colonies of mutant F6-TR overproduced a black pigment on solid medium. The same mutant (F6-TR) had a 3.7-fold higher tyrosinase activity compared with the wild-type strain when induced with ferulic acid. However in tyrosine uptake assays whole cells of the mutant strain F6-TR consumed eight times less tyrosine compared with the wild-type strain. Mutant F6-HDO produced a diffusible red pigment into the growth medium. Pigment production by mutant F6-HDO is sixfold higher than the wild-type strain. The biomass yield of mutant F6-HDO grown on tyrosine as the sole source of carbon and energy was 1.2-fold lower than the wild-type strain. While the growth of the wild-type strain was completely inhibited by 5 min of exposure to UV light (254 nm) both mutant strains showed survival rates  gt  30%. Mutant F6-HDO was able to tolerate higher concentrations of hydrogen peroxide (H(2)O(2)) exhibiting 1.5 times smaller zones of inhibition at 10 mM H(2)O(2) compared with mutant F6-TR and the wild-type strain. The pigments produced by all strains were purified and confirmed to be melanins.
PB  - Wiley-Blackwell Publishing, Inc, Malden
T2  - FEMS Microbiology Letters / Federation of European Microbiological Societies
T1  - Characterization of melanin-overproducing transposon mutants of Pseudomonas putida F6
VL  - 298
IS  - 2
SP  - 174
EP  - 183
DO  - 10.1111/j.1574-6968.2009.01716.x
ER  - 

@article{
author = "Nikodinović-Runić, Jasmina and Martin, Leona B. and Babu, Ramesh P. and Blau, Werner and O'Connor, Kevin E.",
year = "2009",
abstract = "Two melanin-overproducing Pseudomonas putida F6 mutants were generated using transposon (Tn5) mutagenesis. Mutants were disrupted in a transcriptional regulator (TR) and a homogentisate 1,2-dioxygenase (HDO) gene. Colonies of mutant F6-TR overproduced a black pigment on solid medium. The same mutant (F6-TR) had a 3.7-fold higher tyrosinase activity compared with the wild-type strain when induced with ferulic acid. However in tyrosine uptake assays whole cells of the mutant strain F6-TR consumed eight times less tyrosine compared with the wild-type strain. Mutant F6-HDO produced a diffusible red pigment into the growth medium. Pigment production by mutant F6-HDO is sixfold higher than the wild-type strain. The biomass yield of mutant F6-HDO grown on tyrosine as the sole source of carbon and energy was 1.2-fold lower than the wild-type strain. While the growth of the wild-type strain was completely inhibited by 5 min of exposure to UV light (254 nm) both mutant strains showed survival rates  gt  30%. Mutant F6-HDO was able to tolerate higher concentrations of hydrogen peroxide (H(2)O(2)) exhibiting 1.5 times smaller zones of inhibition at 10 mM H(2)O(2) compared with mutant F6-TR and the wild-type strain. The pigments produced by all strains were purified and confirmed to be melanins.",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "FEMS Microbiology Letters / Federation of European Microbiological Societies",
title = "Characterization of melanin-overproducing transposon mutants of Pseudomonas putida F6",
volume = "298",
number = "2",
pages = "174-183",
doi = "10.1111/j.1574-6968.2009.01716.x"
}

Nikodinović-Runić, J., Martin, L. B., Babu, R. P., Blau, W.,& O'Connor, K. E.. (2009). Characterization of melanin-overproducing transposon mutants of Pseudomonas putida F6. in FEMS Microbiology Letters / Federation of European Microbiological Societies
Wiley-Blackwell Publishing, Inc, Malden., 298(2), 174-183.
https://doi.org/10.1111/j.1574-6968.2009.01716.x

Nikodinović-Runić J, Martin LB, Babu RP, Blau W, O'Connor KE. Characterization of melanin-overproducing transposon mutants of Pseudomonas putida F6. in FEMS Microbiology Letters / Federation of European Microbiological Societies. 2009;298(2):174-183.
doi:10.1111/j.1574-6968.2009.01716.x .

Nikodinović-Runić, Jasmina, Martin, Leona B., Babu, Ramesh P., Blau, Werner, O'Connor, Kevin E., "Characterization of melanin-overproducing transposon mutants of Pseudomonas putida F6" in FEMS Microbiology Letters / Federation of European Microbiological Societies, 298, no. 2 (2009):174-183,
https://doi.org/10.1111/j.1574-6968.2009.01716.x . .

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 . .