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References (55)
-
Aleksandar Bijelić, Matthias Pretzler, C. Molitor, Florime Zekiri, Annette Rompel (2015)
Kristallstruktur einer pflanzlichen Tyrosinase aus Walnussblättern: die Bedeutung “substratlenkender Aminosäurereste” für die EnzymspezifitätAngewandte Chemie, 127
-
Ismaya (2011)
575Acta Cryst. F, 67
-
W. Ismaya, H. Rozeboom, M. Schurink, C. Boeriu, H. Wichers, B. Dijkstra (2011)
Crystallization and preliminary X-ray crystallographic analysis of tyrosinase from the mushroom Agaricus bisporus.Acta crystallographica. Section F, Structural biology and crystallization communications, 67 Pt 5
-
F. Gandía-Herrero, M. Jiménez-Atiénzar, J. Cabanes, F. García-Carmona, J. Escribano (2005)
Differential activation of a latent polyphenol oxidase mediated by sodium dodecyl sulfate.Journal of agricultural and food chemistry, 53 17
-
A. Mayer, E. Harel, R. Ben-Shaul (1966)
Assay of catechol oxidase—a critical comparison of methodsPhytochemistry, 5
-
Kabsch (2010)
125Acta Cryst. D, 66
-
W. Flurkey, Jennifer Inlow (2008)
Proteolytic processing of polyphenol oxidase from plants and fungi.Journal of inorganic biochemistry, 102 12
-
M. Pretzler, A. Bijelic, A. Rompel (2015)
Fungal Tyrosinases: Why Mushrooms Turn Brown -
Y. Matoba, T. Kumagai, A. Yamamoto, H. Yoshitsu, M. Sugiyama (2006)
Crystallographic Evidence That the Dinuclear Copper Center of Tyrosinase Is Flexible during Catalysis*Journal of Biological Chemistry, 281
-
C. Ramsden, P. Riley (2014)
Tyrosinase: the four oxidation states of the active site and their relevance to enzymatic activation, oxidation and inactivation.Bioorganic & medicinal chemistry, 22 8
-
A. Bijelic, M. Pretzler, C. Molitor, Florime Zekiri, A. Rompel (2015)
The Structure of a Plant Tyrosinase from Walnut Leaves Reveals the Importance of “Substrate-Guiding Residues” for Enzymatic SpecificityAngewandte Chemie (International Ed. in English), 54
-
M. Pretzler, A. Rompel (2017)
What causes the different functionality in type-III-copper enzymes? A state of the art perspectiveInorganica Chimica Acta
-
C. Molitor, S. Mauracher, A. Rompel (2015)
Crystallization and preliminary crystallographic analysis of latent, active and recombinantly expressed aurone synthase, a polyphenol oxidase, from Coreopsis grandifloraActa Crystallographica. Section F, Structural Biology Communications, 71
-
M. Pretzler, A. Bijelic, A. Rompel (2017)
Heterologous expression and characterization of functional mushroom tyrosinase (AbPPO4)Scientific Reports, 7
-
Florime Zekiri, A. Bijelic, C. Molitor, A. Rompel
Structural Biology Communications Crystallization and Preliminary X-ray Crystallographic Analysis of Polyphenol Oxidase from Juglans Regia (jrppo1) -
Cornelia Kaintz, R. Mayer, F. Jirsa, H. Halbwirth, A. Rompel (2015)
Site-directed mutagenesis around the CuA site of a polyphenol oxidase from Coreopsis grandiflora (cgAUS1)Febs Letters, 589
-
Cornelia Kaintz, C. Molitor, J. Thill, I. Kampatsikas, C. Michael, H. Halbwirth, A. Rompel (2014)
Cloning and functional expression in E. coli of a polyphenol oxidase transcript from Coreopsis grandiflora involved in aurone formationFebs Letters, 588
-
Mor Goldfeder, M. Kanteev, Sivan Isaschar-Ovdat, N. Adir, A. Fishman (2014)
Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteinsNature Communications, 5
-
Gandía-Herrero (2005)
601Biol. Chem., 386
-
Lan Tran, J. Taylor, C. Constabel (2012)
The polyphenol oxidase gene family in land plants: Lineage-specific duplication and expansionBMC Genomics, 13
-
S. Altschul, W. Gish, W. Miller, E. Myers, D. Lipman (1990)
Basic local alignment search tool.Journal of molecular biology, 215 3
-
C. Molitor, S. Mauracher, Sanela Pargan, R. Mayer, H. Halbwirth, A. Rompel (2015)
Latent and active aurone synthase from petals of C. grandiflora: a polyphenol oxidase with unique characteristicsPlanta, 242
-
M. Sendovski, M. Kanteev, Vered Ben-Yosef, N. Adir, A. Fishman (2011)
First structures of an active bacterial tyrosinase reveal copper plasticity.Journal of molecular biology, 405 1
-
Gandía-Herrero (2005)
6825J. Agric. Food Chem., 53
-
Altschul (1990)
403J. Mol. Biol., 215
-
(2014)
Nature Commun -
C. Molitor, S. Mauracher, A. Rompel (2016)
Aurone synthase is a catechol oxidase with hydroxylase activity and provides insights into the mechanism of plant polyphenol oxidasesProceedings of the National Academy of Sciences, 113
-
Bijelic (2015)
14677Angew. Chem. Int. Ed., 54
-
A. Mayer (2006)
Polyphenol oxidases in plants and fungi: going places? A review.Phytochemistry, 67 21
-
H. Mason (1948)
The chemistry of melanin; mechanism of the oxidation of dihydroxyphenylalanine by tyrosinase.The Journal of biological chemistry, 172 1
-
M. Sugumaran, Kalliappan Nellaiappan (1991)
Lysolecithin--a potent activator of prophenoloxidase from the hemolymph of the lobster, Homarus americanas.Biochemical and biophysical research communications, 176 3
-
M. Kanteev, Mor Goldfeder, A. Fishman (2015)
Structure–function correlations in tyrosinasesProtein Science, 24
-
S. Mauracher, Al-Oweini, U. Kortz, A. Rompel
Structural Biology Communications Crystallization and Preliminary X-ray Crystallographic Analysis of Latent Isoform Ppo4 Mushroom (agaricus Bisporus) Tyrosinase -
Goldfeder (2014)
4505Nature Commun., 5
-
Flurkey (2008)
2160J. Inorg. Biochem., 102
-
P. Evans (2011)
An introduction to data reduction: space-group determination, scaling and intensity statisticsActa Crystallographica Section D: Biological Crystallography, 67
-
Evans (2011)
282Acta Cryst. D, 67
-
J. Rodríguez-López, J. Tudela, R. Varón, F. García-Carmona, F. García-Cánovas (1992)
Analysis of a kinetic model for melanin biosynthesis pathway.The Journal of biological chemistry, 267 6
-
S. Mauracher, C. Molitor, R. Al-Oweini, U. Kortz, A. Rompel (2014)
Latent and active abPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystalActa Crystallographica Section D: Biological Crystallography, 70
-
I. Kampatsikas, A. Bijelic, M. Pretzler, A. Rompel (2017)
Three recombinantly expressed apple tyrosinases suggest the amino acids responsible for mono- versus diphenolase activity in plant polyphenol oxidasesScientific Reports, 7
-
C. Molitor, A. Bijelic, A. Rompel (2016)
In situ formation of the first proteinogenically functionalized [TeW6O24O2(Glu)]7– structure reveals unprecedented chemical and geometrical features of the Anderson-type clusterChemical Communications (Cambridge, England), 52
-
Kaintz (2015)
789FEBS Lett., 589
-
Cornelia Kaintz, S. Mauracher, A. Rompel (2014)
Type-3 copper proteins: recent advances on polyphenol oxidases.Advances in protein chemistry and structural biology, 97
-
Ismaya (2011)
5477Biochemistry, 50
-
Kaintz (2014)
1Adv. Protein Chem. Struct. Biol., 97
-
E. Valero, F. García-Carmona (1992)
pH-induced kinetic co-operativity of a thylakoid-bound polyphenol oxidase.The Biochemical journal, 286 ( Pt 2)
-
Bijelic (2015)
14889Angew. Chem., 127
-
Kaintz (2014)
3417FEBS Lett., 588
-
Florime Zekiri, C. Molitor, S. Mauracher, C. Michael, R. Mayer, C. Gerner, A. Rompel (2014)
Purification and characterization of tyrosinase from walnut leaves (Juglans regia)Phytochemistry, 101
-
F. Gandía-Herrero, M. Jiménez-Atiénzar, J. Cabanes, F. García-Carmona, J. Escribano (2005)
Evidence for a common regulation in the activation of a polyphenol oxidase by trypsin and sodium dodecyl sulfate, 386
-
T. Klabunde, C. Eicken, J. Sacchettini, B. Krebs (1998)
Crystal structure of a plant catechol oxidase containing a dicopper centerNature Structural Biology, 5
-
V. Virador, Juan Grajeda, A. Blanco-Labra, E. Mendiola‐Olaya, Gary Smith, A. Moreno, J. Whitaker (2010)
Cloning, sequencing, purification, and crystal structure of Grenache (Vitis vinifera) polyphenol oxidase.Journal of agricultural and food chemistry, 58 2
-
M. Winn, C. Ballard, K. Cowtan, E. Dodson, P. Emsley, P. Evans, R. Keegan, E. Krissinel, A. Leslie, A. Mccoy, S. McNicholas, G. Murshudov, N. Pannu, E. Potterton, H. Powell, R. Read, A. Vagin, K. Wilson (2011)
Overview of the CCP4 suite and current developmentsActa Crystallographica Section D: Biological Crystallography, 67
-
P. Karplus, K. Diederichs (2012)
Linking Crystallographic Model and Data QualityScience, 336
-
W. Ismaya, H. Rozeboom, A. Weijn, J. Mes, F. Fusetti, H. Wichers, B. Dijkstra (2011)
Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits and interaction with tropolone.Biochemistry, 50 24
- Publisher
- Wiley
- Copyright
- Copyright © 2017 Wiley Subscription Services
- ISSN
- 2053-230X
- eISSN
- 2053-230X
- DOI
- 10.1107/S2053230X17010822
- pmid
- 28777094
- Publisher site
- See Article on Publisher Site
Abstract
Tyrosinases are type 3 copper enzymes that belong to the polyphenol oxidase (PPO) family and are able to catalyze both the ortho‐hydroxylation of monophenols and their subsequent oxidation to o‐quinones, which are precursors for the biosynthesis of colouring substances such as melanin. The first plant pro‐tyrosinase from Malus domestica (MdPPO1) was recombinantly expressed in its latent form (56.4 kDa) and mutated at four positions around the catalytic pocket which are believed to influence the activity of the enzyme. Mutating the amino acids, which are known as activity controllers, yielded the mutants MdPPO1‐Ala239Thr and MdPPO1‐Leu243Arg, whereas mutation of the so‐called water‐keeper and gatekeeper residues resulted in the mutants MdPPO1‐Glu234Ala and MdPPO1‐Phe259Ala, respectively. The wild‐type enzyme and two of the mutants, MdPPO1‐Ala239Thr and MdPPO1‐Phe259Ala, were successfully crystallized, leading to single crystals that diffracted to 1.35, 1.55 and 1.70 Å resolution, respectively. All crystals belonged to space group P212121, exhibiting similar unit‐cell parameters: a = 50.70, b = 80.15, c = 115.96 Å for the wild type, a = 50.58, b = 79.90, c = 115.76 Å for MdPPO1‐Ala239Thr and a = 50.53, b = 79.76, c = 116.07 Å for MdPPO1‐Phe259Ala. In crystallo activity tests with the crystals of the wild type and the two mutants were performed by adding the monophenolic substrate tyramine and the diphenolic substrate dopamine to crystal‐containing drops. The effects of the mutation on the activity of the enzyme were observed by colour changes of the crystals owing to the conversion of the substrates to dark chromophore products.
Journal
Acta Crystallographica Section F – Wiley
Published: Jan 1, 2017
Keywords: ; ; ; ;