Analysis of molecular and structural causes of metabolic diversity mediated by prenylating enzymes

WOLFGANG BRANDT
LUDGER A. WESSJOHANN
Leibniz Institute of Plant Biochemistry
Weinberg 3
D-06120 Halle/S.
Wolfgang.Brandt@ipb-halle.de
Ludger.Wessjohann@ipb-halle.de
http://www.ipb-halle.de/de/forschung/natur-und-wirkstoffchemie/

References
Brandt, W. and Stehle, F. 1-O-sinapoyl-b-glucose:L-malate sinapoyltransferase from Arabidopsis thaliana. 2006. Protein Data Bank, entry: 2DRF.

Bräuer, L., W. Brandt, and L. A. Wessjohann. 2004. Modeling the E-coli 4-hydroxybenzoic acid oligoprenyltransferase (ubiA transferase) and characterization of potential active sites. Journal of Molecular Modeling 10:317-327.

Bräuer, L., Wessjohann, L. A., and Brandt, W. Modeling of a Cannabis sativa terpene synthase. 2007. Protein Data Bank, entry 2DK0.

Geissler, R., W. Brandt, and J. Ziegler. 2007. Molecular modeling and site-directed mutagenesis reveal the benzylisoquinoline binding site of the short-chain dehydrogenase/reductase salutaridine reductase. Plant Physiol 143:1493-1503.

Stehle, F., W. Brandt, C. Milkowski, and D. Strack. 2006. Structure determinants and substrate recognition of serine carboxypeptidase-like acyltransferases from plant secondary metabolism. FEBS Lett 580:6366-6374.

Teuber, M., M. E. Azemi, F. Namjoyan, A. C. Meier, A. Wodak, W. Brandt, and B. Drager. 2007. Putrescine N-methyltransferases-a structure-function analysis. Plant Mol Biol 63:787-801.

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