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2. A 7-dimethylallyltryptophan synthase from Aspergillus fumigatus: overproduction, purification and biochemical characterization

Author

Kremer, Anika, Westrich, Lucia, and Li, Shu-Ming

Subjects
Aspergillus -- Chemical properties, Aspergillus -- Sexual behavior, Aspergillus -- Genetic aspects, Bacterial genetics -- Research, Transferases -- Properties, Transferases -- Genetic aspects, Biochemistry -- Research, Biological sciences
Abstract

A putative prenyltransferase gene, Afu3g12930, was identified in the genome sequence of Aspergillus fumigatus. EAL92290, encoded by Afu3g12930, consists of 472 aa, with a molecular mass of about 53 kDa. The coding sequence of Afu3g12930 was cloned in pQE60, and overexpressed in Escherichia coil The soluble [His.sub.6]-fusion protein was purified to apparent homogeneity, and characterized biochemically. The enzyme was found to catalyse the prenylation of Trp at the C-7 position of the indole moiety, in the presence of dimethylallyl diphosphate (DMAPP); therefore, it functions as a 7-dimethylallyltryptophan synthase (7-DMATS). The structure of the enzymic product was elucidated by NMR and MS analysis. [K.sub.m] values were 67 [micro]M for DMAPP, and 137 [micro]M for L-Trp. Geranyl diphosphate was not accepted as prenyl donor, while Trp-containing dipeptides were found to be aromatic substrates of 7-DMATS. 7-DMATS did not need divalent metal ions for its enzymic reaction, although [Ca.sup.2+] enhanced the reaction velocity slightly. The enzyme is the second dimethylallyltryptophan synthase identified in A. fumigatus. Interestingly, it shares a sequence identity of only 31% at the amino acid level with another known dimethylallyltryptophan synthase, FgaPT2, from the same fungus; FgaPT2 prenylates L-Trp at the C-4 position of the indole ring. Afu3g12930 belongs to a putative biosynthetic gene cluster consisting of eight genes. Orthologous clusters were also identified in the genome sequences of Neosartorya fischeri and Aspergillus terreus. The putative roles of the genes in the cluster are discussed.

Published
2007

3. Methyltransferase genes in Streptomyces rishiriensis: new coumermycin derivatives from gene-inactivation experiments

Author

Shu-Ming Li, Westrich, Lucia, Schmidt, Jurgen, Kuhnt, Christine, and Heide, Lutz

Subjects
Microbiological research -- Analysis, Methyltransferases -- Genetic aspects, Streptomyces -- Genetic aspects, Coumarins -- Physiological aspects, Biosynthesis -- Usage, Biological sciences
Abstract

Research has been conducted on Streptomyces rishiriensis methyltransferase genes from the coumermycin A (sub)1 cluster. The identification of these genes carried out via gene inactivation and secondary metabolite inactivation is described.

Published
2002

13. Inactivation of the urdGT2 Gene, Which Encodes a Glycosyltransferase Responsible for the C-Glycosyltransfer of Activated d-Olivose, Leads to Formation of the Novel Urdamycins I, J, and K

Author

Künzel, Eva, primary, Faust, Bettina, additional, Oelkers, Carsten, additional, Weissbach, Ulrike, additional, Bearden, Daniel W., additional, Weitnauer, Gabriele, additional, Westrich, Lucia, additional, Bechthold, Andreas, additional, and Rohr, Jürgen, additional

Published
1999
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18. Cloning and characterization of a gene cluster from Streptomyces cyanogenusS136 probably involved in landomycin biosynthesis

Author

Westrich, Lucia, Domann, Silvie, Faust, Bettina, Bedford, David, Hopwood, David A, and Bechthold, Andreas

Abstract

From a cosmid library of Streptomyces cyanogenusS136, DNA fragments encompassing approximately 35 kb of the presumed landomycin biosynthetic gene cluster were identified and sequenced, revealing 32 open reading frames most of which could be assigned through data base comparison.

Published
1999
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