Activation of recombinantly expressed l-Amino Acid Oxidase from Rhizoctonia solani by Sodium Dodecyl Sulfate
Hahn K, Hertle Y, Bloess S, Kottke T, Hellweg T, Fischer von Mollard G (2017)
Molecules 22(12): 2272.
Zeitschriftenaufsatz
| Veröffentlicht | Englisch
Download
Autor*in
Abstract / Bemerkung
l-Amino acid oxidases (l-AAO) catalyze the oxidative deamination of l-amino acids to the corresponding α-keto acids. The non-covalently bound cofactor FAD is reoxidized by oxygen under formation of hydrogen peroxide. We expressed an active l-AAO from the fungus Rhizoctonia solani as a fusion protein in E. coli. Treatment with small amounts of the detergent sodium dodecyl sulfate (SDS) stimulated the activity of the enzyme strongly. Here, we investigated whether other detergents and amphiphilic molecules activate 9His-rsLAAO1. We found that 9His-rsLAAO1 was also activated by sodium tetradecyl sulfate. Other detergents and fatty acids were not effective. Moreover, effects of SDS on the oligomerization state and the protein structure were analyzed. Native and SDS-activated 9His-rsLAAO1 behaved as dimers by size-exclusion chromatography. SDS treatment induced an increase in hydrodynamic radius as observed by size-exclusion chromatography and dynamic light scattering. The activated enzyme showed accelerated thermal inactivation and an exposure of additional protease sites. Changes in tryptophan fluorescence point to a more hydrophilic environment. Moreover, FAD fluorescence increased and a lower concentration of sulfites was sufficient to form adducts with FAD. Taken together, these data point towards a more open conformation of SDS-activated l-amino acid oxidase facilitating access to the active site.
Stichworte
l-amino acid oxidase;
activation;
SDS;
active conformation;
conformational change;
photon correlation spectroscopy (PCS)
Erscheinungsjahr
2017
Zeitschriftentitel
Molecules
Band
22
Ausgabe
12
Art.-Nr.
2272
Urheberrecht / Lizenzen
ISSN
1420-3049
Finanzierungs-Informationen
Open-Access-Publikationskosten wurden durch die Deutsche Forschungsgemeinschaft und die Universität Bielefeld gefördert.
Page URI
https://pub.uni-bielefeld.de/record/2916083
Zitieren
Hahn K, Hertle Y, Bloess S, Kottke T, Hellweg T, Fischer von Mollard G. Activation of recombinantly expressed l-Amino Acid Oxidase from Rhizoctonia solani by Sodium Dodecyl Sulfate. Molecules. 2017;22(12): 2272.
Hahn, K., Hertle, Y., Bloess, S., Kottke, T., Hellweg, T., & Fischer von Mollard, G. (2017). Activation of recombinantly expressed l-Amino Acid Oxidase from Rhizoctonia solani by Sodium Dodecyl Sulfate. Molecules, 22(12), 2272. doi:10.3390/molecules22122272
Hahn, Katharina, Hertle, Yvonne, Bloess, Svenja, Kottke, Tilman, Hellweg, Thomas, and Fischer von Mollard, Gabriele. 2017. “Activation of recombinantly expressed l-Amino Acid Oxidase from Rhizoctonia solani by Sodium Dodecyl Sulfate”. Molecules 22 (12): 2272.
Hahn, K., Hertle, Y., Bloess, S., Kottke, T., Hellweg, T., and Fischer von Mollard, G. (2017). Activation of recombinantly expressed l-Amino Acid Oxidase from Rhizoctonia solani by Sodium Dodecyl Sulfate. Molecules 22:2272.
Hahn, K., et al., 2017. Activation of recombinantly expressed l-Amino Acid Oxidase from Rhizoctonia solani by Sodium Dodecyl Sulfate. Molecules, 22(12): 2272.
K. Hahn, et al., “Activation of recombinantly expressed l-Amino Acid Oxidase from Rhizoctonia solani by Sodium Dodecyl Sulfate”, Molecules, vol. 22, 2017, : 2272.
Hahn, K., Hertle, Y., Bloess, S., Kottke, T., Hellweg, T., Fischer von Mollard, G.: Activation of recombinantly expressed l-Amino Acid Oxidase from Rhizoctonia solani by Sodium Dodecyl Sulfate. Molecules. 22, : 2272 (2017).
Hahn, Katharina, Hertle, Yvonne, Bloess, Svenja, Kottke, Tilman, Hellweg, Thomas, and Fischer von Mollard, Gabriele. “Activation of recombinantly expressed l-Amino Acid Oxidase from Rhizoctonia solani by Sodium Dodecyl Sulfate”. Molecules 22.12 (2017): 2272.
Alle Dateien verfügbar unter der/den folgenden Lizenz(en):
Creative Commons Namensnennung 4.0 International Public License (CC-BY 4.0):
Volltext(e)
Name
Access Level
Open Access
Zuletzt Hochgeladen
2019-09-06T09:18:55Z
MD5 Prüfsumme
58e00cff065f670488acf77b45b13e19
Daten bereitgestellt von European Bioinformatics Institute (EBI)
2 Zitationen in Europe PMC
Daten bereitgestellt von Europe PubMed Central.
The Pseudoalteromonas luteoviolacea L-amino Acid Oxidase with Antimicrobial Activity Is a Flavoenzyme.
Andreo-Vidal A, Sanchez-Amat A, Campillo-Brocal JC., Mar Drugs 16(12), 2018
PMID: 30545033
Andreo-Vidal A, Sanchez-Amat A, Campillo-Brocal JC., Mar Drugs 16(12), 2018
PMID: 30545033
36 References
Daten bereitgestellt von Europe PubMed Central.
The oxidation of various synthetic alpha-amino-acids by mammalian d-amino-acid oxidase, l-amino-acid oxidase of cobra venom and the l- and d-amino-acid oxidases of Neurospora crassa.
Bender AE, Krebs HA., Biochem. J. 46(2), 1950
PMID: 16748663
Bender AE, Krebs HA., Biochem. J. 46(2), 1950
PMID: 16748663
A new bacterial -amino acid oxidase with a broad substrate specificity: Purification and characterization
Geueke B., Hummel W.., 2002
Geueke B., Hummel W.., 2002
Identification of nitrogen mineralization enzymes, L-amino acid oxidases, from the ectomycorrhizal fungi Hebeloma spp. and Laccaria bicolor.
Nuutinen JT, Timonen S., Mycol. Res. 112(Pt 12), 2008
PMID: 18675352
Nuutinen JT, Timonen S., Mycol. Res. 112(Pt 12), 2008
PMID: 18675352
L-amino acid oxidase as biocatalyst: a dream too far?
Pollegioni L, Motta P, Molla G., Appl. Microbiol. Biotechnol. 97(21), 2013
PMID: 24077723
Pollegioni L, Motta P, Molla G., Appl. Microbiol. Biotechnol. 97(21), 2013
PMID: 24077723
A novel L-amino acid oxidase from Trichoderma harzianum ETS 323 associated with antagonism of Rhizoctonia solani.
Yang CA, Cheng CH, Lo CT, Liu SY, Lee JW, Peng KC., J. Agric. Food Chem. 59(9), 2011
PMID: 21456553
Yang CA, Cheng CH, Lo CT, Liu SY, Lee JW, Peng KC., J. Agric. Food Chem. 59(9), 2011
PMID: 21456553
New biotech applications from evolved D-amino acid oxidases.
Pollegioni L, Molla G., Trends Biotechnol. 29(6), 2011
PMID: 21397351
Pollegioni L, Molla G., Trends Biotechnol. 29(6), 2011
PMID: 21397351
Natural occurrence and industrial applications of D-amino acids: an overview.
Martinez-Rodriguez S, Martinez-Gomez AI, Rodriguez-Vico F, Clemente-Jimenez JM, Las Heras-Vazquez FJ., Chem. Biodivers. 7(6), 2010
PMID: 20564568
Martinez-Rodriguez S, Martinez-Gomez AI, Rodriguez-Vico F, Clemente-Jimenez JM, Las Heras-Vazquez FJ., Chem. Biodivers. 7(6), 2010
PMID: 20564568
2-Keto acids based biosynthesis pathways for renewable fuels and chemicals.
Tashiro Y, Rodriguez GM, Atsumi S., J. Ind. Microbiol. Biotechnol. 42(3), 2014
PMID: 25424696
Tashiro Y, Rodriguez GM, Atsumi S., J. Ind. Microbiol. Biotechnol. 42(3), 2014
PMID: 25424696
L-Amino acid oxidases from microbial sources: types, properties, functions, and applications.
Hossain GS, Li J, Shin HD, Du G, Liu L, Chen J., Appl. Microbiol. Biotechnol. 98(4), 2013
PMID: 24352734
Hossain GS, Li J, Shin HD, Du G, Liu L, Chen J., Appl. Microbiol. Biotechnol. 98(4), 2013
PMID: 24352734
Heterologous expression of Rhodococcus opacus L-amino acid oxidase in Streptomyces lividans.
Geueke B, Hummel W., Protein Expr. Purif. 28(2), 2003
PMID: 12699695
Geueke B, Hummel W., Protein Expr. Purif. 28(2), 2003
PMID: 12699695
SO-LAAO, a novel L-amino acid oxidase that enables Streptococcus oligofermentans to outcompete Streptococcus mutans by generating H2O2 from peptone.
Tong H, Chen W, Shi W, Qi F, Dong X., J. Bacteriol. 190(13), 2008
PMID: 18469105
Tong H, Chen W, Shi W, Qi F, Dong X., J. Bacteriol. 190(13), 2008
PMID: 18469105
L-Amino acid oxidase of the fungus Hebeloma cylindrosporum displays substrate preference towards glutamate.
Nuutinen JT, Marttinen E, Soliymani R, Hilden K, Timonen S., Microbiology (Reading, Engl.) 158(Pt 1), 2011
PMID: 21998160
Nuutinen JT, Marttinen E, Soliymani R, Hilden K, Timonen S., Microbiology (Reading, Engl.) 158(Pt 1), 2011
PMID: 21998160
Recombinant expression and characterization of a L-amino acid oxidase from the fungus Rhizoctonia solani.
Hahn K, Neumeister K, Mix A, Kottke T, Groger H, Fischer von Mollard G., Appl. Microbiol. Biotechnol. 101(7), 2016
PMID: 27986991
Hahn K, Neumeister K, Mix A, Kottke T, Groger H, Fischer von Mollard G., Appl. Microbiol. Biotechnol. 101(7), 2016
PMID: 27986991
Berne B.J., Pecora R.., 1976
A constrained regularization method for inverting data represented by linear algebraic or integral-equations
Provencher S.W.., 1982
Provencher S.W.., 1982
CONTIN—A general-purpose constrained regularization program for inverting noisy linear algebraic and integral-equations
Provencher S.W.., 1982
Provencher S.W.., 1982
The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule.
Hellweg T, Hinssen H, Eimer W., Biophys. J. 65(2), 1993
PMID: 8218904
Hellweg T, Hinssen H, Eimer W., Biophys. J. 65(2), 1993
PMID: 8218904
Measurement of rotational diffusion coefficient of lysozyme by depolarized light scattering—Configuration of lysozyme in solution
Dubin S.B., Clark N.A., Benedek G.B.., 1971
Dubin S.B., Clark N.A., Benedek G.B.., 1971
Molecular shape of vinculin in aqueous solution.
Eimer W, Niermann M, Eppe MA, Jockusch BM., J. Mol. Biol. 229(1), 1993
PMID: 8421297
Eimer W, Niermann M, Eppe MA, Jockusch BM., J. Mol. Biol. 229(1), 1993
PMID: 8421297
Mukerjee P., Mysels K.J.., 1971
Ionic surfactant aggregates in saline solutions: sodium dodecyl sulfate (SDS) in the presence of excess sodium chloride (NaCl) or calcium chloride (CaCl(2)).
Sammalkorpi M, Karttunen M, Haataja M., J Phys Chem B 113(17), 2009
PMID: 19344100
Sammalkorpi M, Karttunen M, Haataja M., J Phys Chem B 113(17), 2009
PMID: 19344100
An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum.
Deleage G, Geourjon C., Comput. Appl. Biosci. 9(2), 1993
PMID: 8481823
Deleage G, Geourjon C., Comput. Appl. Biosci. 9(2), 1993
PMID: 8481823
Tryptophan fluorescence study of conformational transitions of the oxidized and reduced form of thioredoxin.
Holmgren A., J. Biol. Chem. 247(7), 1972
PMID: 4552684
Holmgren A., J. Biol. Chem. 247(7), 1972
PMID: 4552684
A new method of preparation of D-amino acid oxidase apoprotein and a conformational change after its combination with flavin adenine dinucleotide.
Massey V, Curti B., J. Biol. Chem. 241(14), 1966
PMID: 4380447
Massey V, Curti B., J. Biol. Chem. 241(14), 1966
PMID: 4380447
The reactivity of flavoproteins with sulfite. Possible relevance to the problem of oxygen reactivity.
Massey V, Muller F, Feldberg R, Schuman M, Sullivan PA, Howell LG, Mayhew SG, Matthews RG, Foust GP., J. Biol. Chem. 244(15), 1969
PMID: 4389773
Massey V, Muller F, Feldberg R, Schuman M, Sullivan PA, Howell LG, Mayhew SG, Matthews RG, Foust GP., J. Biol. Chem. 244(15), 1969
PMID: 4389773
Active-site probes of flavoproteins.
Massey V, Hemmerich P., Biochem. Soc. Trans. 8(3), 1980
PMID: 7399046
Massey V, Hemmerich P., Biochem. Soc. Trans. 8(3), 1980
PMID: 7399046
Effect of ionic detergents, nonionic detergents, and chaotropic agents on polyphenol oxidase activity from dormant saffron (Crocus sativus L.) corms.
Saeidian S, Keyhani E, Keyhani J., J. Agric. Food Chem. 55(9), 2007
PMID: 17407318
Saeidian S, Keyhani E, Keyhani J., J. Agric. Food Chem. 55(9), 2007
PMID: 17407318
On the latency and nature of phenoloxidase present in the left colleterial gland of the cockroach Periplaneta americana.
Sugumaran M, Nellaiappan K., Arch. Insect Biochem. Physiol. 15(3), 1990
PMID: 2134024
Sugumaran M, Nellaiappan K., Arch. Insect Biochem. Physiol. 15(3), 1990
PMID: 2134024
On the presence of prophenoloxidase in the hemolymph of the horseshoe crab, Limulus.
Nellaiappan K, Sugumaran M., Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 113(1), 1996
PMID: 8936050
Nellaiappan K, Sugumaran M., Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 113(1), 1996
PMID: 8936050
A detergent-activated tyrosinase from Xenopus-laevis 2. Detergent activation and binding
Wittenberg C., Triplett E.L.., 1985
Wittenberg C., Triplett E.L.., 1985
Spinach Thylakoid Polyphenol Oxidase : ISOLATION, ACTIVATION, AND PROPERTIES OF THE NATIVE CHLOROPLAST ENZYME.
Golbeck JH, Cammarata KV., Plant Physiol. 67(5), 1981
PMID: 16661805
Golbeck JH, Cammarata KV., Plant Physiol. 67(5), 1981
PMID: 16661805
The conformational state of polyphenol oxidase from field bean (Dolichos lablab) upon SDS and acid-pH activation.
Kanade SR, Paul B, Rao AG, Gowda LR., Biochem. J. 395(3), 2006
PMID: 16393141
Kanade SR, Paul B, Rao AG, Gowda LR., Biochem. J. 395(3), 2006
PMID: 16393141
Activation of a latent mushroom (Agaricus bisporus) tyrosinase isoform by sodium dodecyl sulfate (SDS). Kinetic properties of the SDS-activated isoform.
Espin JC, Wichers HJ., J. Agric. Food Chem. 47(9), 1999
PMID: 10552678
Espin JC, Wichers HJ., J. Agric. Food Chem. 47(9), 1999
PMID: 10552678
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.
Bradford MM., Anal. Biochem. 72(), 1976
PMID: 942051
Bradford MM., Anal. Biochem. 72(), 1976
PMID: 942051
Analysis of macromolecular polydispersity in intensity correlation spectroscopy—Method of cumulants
Koppel D.E.., 1972
Koppel D.E.., 1972
The use of circular dichroism in the investigation of protein structure and function.
Kelly SM, Price NC., Curr. Protein Pept. Sci. 1(4), 2000
PMID: 12369905
Kelly SM, Price NC., Curr. Protein Pept. Sci. 1(4), 2000
PMID: 12369905
Export
Markieren/ Markierung löschen
Markierte Publikationen
Web of Science
Dieser Datensatz im Web of Science®Quellen
PMID: 29261108
PubMed | Europe PMC
Suchen in