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Corynebacterium glutamicum contains 3-deoxy-D-arabino-heptulosonate 7-phosphate synthases that display novel biochemical features

Title data

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. Vol. 74 (2008) Issue 17 . - pp. 5497-5503.
ISSN 1098-5336
DOI: https://doi.org/10.1128/AEM.00262-08

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: BAYCEER62317
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Ecological Microbiology
Research Institutions > Research Centres > Bayreuth Center of Ecology and Environmental Research- BayCEER
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology
Research Institutions
Research Institutions > Research Centres
Result of work at the UBT: Yes
DDC Subjects: 500 Science
Date Deposited: 29 Jul 2015 05:53
Last Modified: 29 Jul 2015 05:53
URI: https://eref.uni-bayreuth.de/id/eprint/17388