@article{VaajeKolstadHoustonRaoetal.2004,
  author    = {Vaaje-Kolstad, G. and Houston, Douglas R. and Rao, F. V. and Peter, Martin G. and Synstad, Bjoenar and van Aalten, Daan M. F. and Eijsink, Vincent G. H.},
  title     = {Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin},
  issn      = {1570-9639},
  year      = {2004},
  abstract  = {Catalysis by ChiB, a family 18 chitinase from Serratia marcescens, involves a conformational change of Asp142 which is part of a characteristic D140XD142XE144 sequence motif In the free enzyme Asp142 points towards Asp140, whereas it rotates towards the catalytic acid, Glu144, upon ligand binding. Mutation of Asp142 to Asn reduced k(cat) and affinity for allosamidin, a competitive inhibitor. The X-ray structure of the D142N mutant showed that Asn142 points towards Glu144 in the absence of a ligand. The active site also showed other structural adjustments (Tyr10, Ser93) that had previously been observed in the wild-type enzyme upon substrate binding. The X-ray structure of a complex of D142N with allosamidin, a pseudotrisaccharide competitive inhibitor, was essentially identical to that of the wild-type enzyme in complex with the same compound. Thus, the reduced allosamidin affinity in the mutant is not caused by structural changes but solely by the loss of electrostatic interactions with Asp142. The importance of electrostatics was further confirmed by the pH dependence of catalysis and allosamidin inhibition. The pH-dependent apparent affinities for allosamidin were not correlated with k(cat), indicating that it is probably better to view the inhibitor as a mimic of the oxazolinium ion reaction intermediate than as a transition state analogue. (C) 2003 Elsevier B.V. All rights reserved},
  language  = {en}
}
@article{PeterWollenberger1997,
  author    = {Peter, Martin G. and Wollenberger, Ursula},
  title     = {Phenol-oxidizing enzymes : mechanisms and applications},
  year      = {1997},
  language  = {en}
}
@article{EinarssonBahrkeSigurdssonetal.2013,
  author    = {Einarsson, Jon M. and Bahrke, Sven and Sigurdsson, Bjarni Thor and Ng, Chuen-How and Petersen, Petur Henry and Sigurjonsson, Olafur E. and Jonsson, Halldor and Gislason, Johannes and Thormodsson, Finnbogi R. and Peter, Martin G.},
  title     = {Partially acetylated chitooligosaccharides bind to YKL-40 and stimulate growth of human osteoarthritic chondrocytes},
  series = {Biochemical and biophysical research communications},
  volume    = {434},
  journal   = {Biochemical and biophysical research communications},
  number    = {2},
  publisher = {Elsevier},
  address   = {San Diego},
  issn      = {0006-291X},
  doi       = {10.1016/j.bbrc.2013.02.122},
  pages     = {298 -- 304},
  year      = {2013},
  abstract  = {Recent evidences indicating that cellular kinase signaling cascades are triggered by oligomers of N-acetylglucosamine (ChOS) and that condrocytes of human osteoarthritic cartilage secrete the inflammation associated chitolectin YKL-40, prompted us to study the binding affinity of partially acetylated ChOS to YKL-40 and their effect on primary chondrocytes in culture. Extensive chitinase digestion and filtration of partially deacetylated chitin yielded a mixture of ChOS (Oligomin(TM)) and further ultrafiltration produced T-ChOS(TM), with substantially smaller fraction of the smallest sugars. YKL-40 binding affinity was determined for the different sized homologues, revealing micromolar affinities of the larger homologues to YKL-40. The response of osteoarthritic chondrocytes to Oligomin(TM) and T-ChOS(TM) was determined, revealing 2- to 3-fold increases in cell number. About 500 mu g/ml was needed for Oligomin(TM) and around five times lower concentration for T-ChOS(TM), higher concentrations abolished this effect for both products. Addition of chitotriose inhibited cellular responses mediated by larger oligosaccharides. These results, and the fact that the partially acetylated T-ChOS(TM) homologues should resist hydrolysis, point towards a new therapeutic concept for treating inflammatory joint diseases.},
  language  = {en}
}
@article{KaatzStrefferWollenbergeretal.1999,
  author    = {Kaatz, Helvi and Streffer, Katrin and Wollenberger, Ursula and Peter, Martin G.},
  title     = {Inhibition of mushroom tyrosinase by kojic acid octanoates},
  year      = {1999},
  language  = {en}
}
@article{CederkvistZamfirBahrkeetal.2006,
  author    = {Cederkvist, F. Henning and Zamfir, Alina D. and Bahrke, Sven and Eijsink, Vincent G. H. and Sorlie, Morten and Peter-Katalinic, Jasna and Peter, Martin G.},
  title     = {Identification of a high-affinity-binding oligosaccharide by (+) nanoelectrospray quadrupole time-of-flight tandem mass spectrometry of a noncovalent enzyme-ligand complex},
  issn      = {1433-7851},
  doi       = {10.1002/anie.200503168},
  year      = {2006},
  language  = {en}
}
@article{StrefferKaatzBaueretal.1998,
  author    = {Streffer, Katrin and Kaatz, Helvi and Bauer, Christian G. and Makower, Alexander and Schulmeister, Thomas and Scheller, Frieder W. and Peter, Martin G. and Wollenberger, Ursula},
  title     = {Application of a sensitive catechol detector for determination of tyrosinase inhibitors},
  year      = {1998},
  language  = {en}
}