@article{PeikowMaternPeteretal.2005, author = {Peikow, Dirk and Matern, Christa-Maria and Peter, Martin G. and Schilde, Uwe}, title = {Crystal structure of (1,4,7,10,13-pentaoxacyclopentadecane-O,O ',O '',O ''')(trifluoromethanesulfonato-O,O ')sodium, Na(C10H20O5)(CF3SO3)}, year = {2005}, abstract = {C11H20F3NaO8S, monoclinic, P121/nil (no. 11), a = 7.947(1) angstrom, b = 12.056(1) angstrom, c = 9.083(1) angstrom, P = 106.01 (1)degrees, V = 836.4 angstrom(3), Z = 2, R-gt(F) = 0.043, wR(ref)(F-2) = 0.120, T = 210 K.}, language = {en} } @article{AlarconAldereteAguilaetal.2005, author = {Alarcon, Julio and Alderete, Joel B. and Aguila, Sergio and Peter, Martin G.}, title = {Regio and stereoselective hydroxylation of alpha-agarofuran by biotransformation of rhizopus nigricans}, year = {2005}, abstract = {A new synthesis of 9 alpha-hydroxy-alpha-agarofuran (6 alpha) is described, using a microbiological hydroxylation alpha-agarofuran (5) as the key reaction. The stereochemistry of the biohydroxylation was determined on the basis of a NOESY-experiment and GIAO calculations at the B3LYP/cc-pVDZ level. A strong gamma-effect was observed at C15 of the agarofuran ring which was correctly predicted by the GIAO-B3LYP calculations}, language = {en} } @article{FotieNkengfackPeteretal.2004, author = {Fotie, J. and Nkengfack, A. E. and Peter, Martin G. and Heydenreich, Matthias and Fomum, Z. T.}, title = {Chemical constituents of the ethyl acetate extracts of the stem bark and fruits of Dichrostachys cinerea and the roots of Parkia bicolor}, issn = {1011-3924}, year = {2004}, abstract = {The antibacterial activities of ethyl acetate, methanol and aqueous extracts of the stem bark of Dichrostachys cinerea and the roots of Parkia bicolor have been evaluated. Ethyl acetate extracts have been investigated, studies that led to a series of known compounds, amongst which many are reported here for the very first time from both the species}, language = {en} } @article{BerthDautzenbergPeter1998, author = {Berth, Gisela and Dautzenberg, Herbert and Peter, Martin G.}, title = {Physica-chemical characterization of chitosans in dilute solution}, isbn = {2-907922-57-2}, year = {1998}, language = {en} } @article{VaajeKolstadVasellaPeteretal.2004, author = {Vaaje-Kolstad, G. and Vasella, A. and Peter, Martin G. and Netter, C. and Houston, Douglas R. and Westereng, B. and Synstad, Bjoenar and Eijsink, Vincent G. H. and van Aalten, Daan M. F.}, title = {Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono- delta-lactone}, issn = {0021-9258}, year = {2004}, abstract = {We describe enzymological and structural analyses of the interaction between the family 18 chitinase ChiB from Serratia marcescens and the designed inhibitor N,N'-diacetylchitobionoxime-N-phenylcarbamate (HM508). HM508 acts as a competitive inhibitor of this enzyme with a K-i in the 50 muM range. Active site mutants of ChiB show K-i values ranging from 1 to 200 muM, providing insight into some of the interactions that determine inhibitor affinity. Interestingly, the wild type enzyme slowly degrades HM508, but the inhibitor is essentially stable in the presence of the moderately active D142N mutant of ChiB. The crystal structure of the D142N-HM508 complex revealed that the two sugar moieties bind to the -2 and -1 subsites, whereas the phenyl group interacts with aromatic side chains that line the +1 and +2 subsites. Enzymatic degradation of HM508, as well as a Trp-->Ala mutation in the +2 subsite of ChiB, led to reduced affinity for the inhibitor, showing that interactions between the phenyl group and the enzyme contribute to binding. Interestingly, a complex of enzymatically degraded HM508 with the wild type enzyme showed a chitobiono-delta- lactone bound in the -2 and -1 subsites, despite the fact that the equilibrium between the lactone and the hydroxy acid forms in solution lies far toward the latter. This shows that the active site preferentially binds the E-4 conformation of the -1 sugar, which resembles the proposed transition state of the reaction}, language = {en} } @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{GermerMuggePeteretal.2003, author = {Germer, Antje and Mugge, Clemens and Peter, Martin G. and Rottmann, Antje and Kleinpeter, Erich}, title = {Solution- and bound-state conformational study of N,N',N''-triacetyl chitotriose and other analogous potential inhibitors of hevamine: Application of trNOESY and STD NMR spectroscopy}, year = {2003}, abstract = {The soln.-state conformations of N,N',N''-triacetyl chitotriose (1) and other potential chitinase inhibitors 2-4 were studied using a combination of NMR spectroscopy (NOESY) and mol. mechanics calcns. Detn. solely of the global energy min. conformation was found to be insufficient for an agreement with the NMR results. An appropriate consistency between the NMR exptl. data and theor. calcns. was only reached by assessing the structures as population-weighted av. conformers based on Boltzmann distributions derived from the calcd. relative energies. Analogies, but also particular differences, between the synthetic compds. 2-4 and the naturally-occurring N,N',N''-triacetyl chitotriose were found. Furthermore, the conformation of compds. 1 and 2 when bound to hevamine was also studied using transferred NOESY expts. and the binding process was found to impart a level of conformational restriction on the ligands. The preferred conformation as detd. for 1 in the bound state to hevamine belonged to one of the conformational families found for the compd. when free in soln., although full characterization of the bound-state conformations was impeded due to severe signal overlap. Satn. transfer difference NMR expts. were also employed to analyze the binding epitopes of the bound compds. We thus detd. that it is mainly the acetyl amido groups of the trisaccharide and the heterocyclic moiety which are in close contact with hevamine.}, language = {en} } @article{EijsinkSynstadGaseidnesetal.2003, author = {Eijsink, Vincent G. H. and Synstad, Bjoenar and Gaseidnes, Sigrid and Komander, David and Houston, Douglas R. and Peter, Martin G. and van Aalten, Daan M. F.}, title = {Structure and function of chitinolytic enzymes}, isbn = {82-471-5901-5}, year = {2003}, abstract = {The recent work on a variety of family 18 chitonolytic enzymes has yielded important data concerning the structure, substrate-binding, catalysis, inhibitor-binding and even dynamics. These data have been useful in helping to better understand the roles of various types of chitinases in chitin hydrolysis, to rationally engineer the properties of these enzymes, thus making them more suitable as biocatalysts, and to study and understand the effectiveness of natural and designed chitinase inhibitors, which may be of medical interest. On the other hand, the recent work on ChiB shows that catalysis in family 18 chitinases is a highly complicated process, involving larger parts of the enzyme and dynamics. Thus, despite recent discoveries, there is still a lot more to discover about how these enzyme work.}, language = {en} } @phdthesis{BahrkeEinarssonGislasonetal.2003, author = {Bahrke, Sven and Einarsson, Jon M. and Gislason, Johannes and Haebel, Sophie and Peter-Katalinic, Jasna and Peter, Martin G.}, title = {Characterization of chitooligosaccharides by mass spectrometry}, isbn = {82-47-15901-5}, year = {2003}, language = {en} } @article{KamlageSefkowZimmermannetal.2002, author = {Kamlage, Stefan and Sefkow, Michael and Zimmermann, Nicole and Peter, Martin G.}, title = {Concise synthesis of (+)-beta-benzyl gamma-butyrolactones from butynediol}, year = {2002}, language = {en} }