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Liu, Ya-Jun ; Li, Pan-Pan ; Zhao, Ke-Xin ; Wang, Bao-Jun ; Jiang, Cheng-Ying ; Drake, Harold L. ; Liu, Shuang-Jiang:
Corynebacterium glutamicum contains 3-deoxy-D-arabino-heptulosonate 7-phosphate synthases that display novel biochemical features.
In: Applied and Environmental Microbiology.
Bd. 74
(2008)
Heft 17
.
- S. 5497-5503.
ISSN 1098-5336
DOI: https://doi.org/10.1128/AEM.00262-08
Abstract
3-Deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase (EC 2.5.1.54) catalyzes the first step of the shikimate pathway that finally leads to the biosynthesis of aromatic amino acids phenylalanine (Phe), tryptophan (Trp), and tyrosine (Tyr). In Corynebacterium glutamicum ATCC 13032, two chromosomal genes, NCgl0950 (aroF) and NCgl2098 (aroG), were located that encode two putative DAHP synthases. The deletion of NCgl2098 resulted in the loss of the ability of C. glutamicum RES167 (a restriction-deficient strain derived from C. glutamicum ATCC 13032) to grow in mineral medium; however, the deletion of NCgl0950 did not result in any observable phenotypic alteration. Analysis of DAHP synthase activities in the wild type and mutants of C. glutamicum RES167 indicated that NCgl2098, rather than NCgl0950, was involved in the biosynthesis of aromatic amino acids. Cloning and expression in Escherichia coli showed that both NCgl0950 and NCgl2098 encoded active DAHP synthases. Both the NCgl0950 and NCgl2098 DAHP synthases were purified from recombinant E. coli cells and characterized. The NCgl0950 DAHP synthase was sensitive to feedback inhibition by Tyr and, to a much lesser extent, by Phe and Trp. The NCgl2098 DAHP synthase was slightly sensitive to feedback inhibition by Trp, but not sensitive to Tyr and Phe, findings that were in contrast to the properties of previously known DAHP synthases from C. glutamicum subsp. flavum. Both Co2_ and Mn2_ significantly stimulated the NCgl0950 DAHP synthase’s activity, whereas Mn2_ was much more stimulatory than Co2_ to the NCgl2098 DAHP synthase’s activity.
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| Publikationsform: | Artikel in einer Zeitschrift |
|---|---|
| Begutachteter Beitrag: | Ja |
| Zusätzliche Informationen: | BAYCEER62317 |
| Institutionen der Universität: | Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Biologie > Lehrstuhl Ökologische Mikrobiologie Forschungseinrichtungen > Forschungszentren > Bayreuther Zentrum für Ökologie und Umweltforschung - BayCEER Fakultäten Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Biologie Forschungseinrichtungen Forschungseinrichtungen > Forschungszentren |
| Titel an der UBT entstanden: | Ja |
| Themengebiete aus DDC: | 500 Naturwissenschaften und Mathematik |
| Eingestellt am: | 29 Jul 2015 05:53 |
| Letzte Änderung: | 29 Jul 2015 05:53 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/17388 |