Complete sequence of glycolytic enzymes in the mycorrhizal basidiomycete, Suillus bovinus

Grotjohann N, Kowallik W, Thiemann M, Huang Y, Mutumba G, Beermann L, Broer D (1998)
ZEITSCHRIFT FUER NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES 53(9-10): 818-827.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ; ;
Abstract
Axenic cultures of Suillus bovinus were cultivated in inorganic liquid medium with glucose as a carbon source at 25 degrees C and continuous supply of oxygen by aeration with compressed air in the dark. Exogenous fructose as sole carbon source yielded about 50% less increase in dry weight than glucose. This resulted from different uptake velocities. Sucrose as sole exogenous carbon source yielded no measurable increase in dry weight. In glucose cultures, activities of all glycolytic enzymes were found. Maximum specific activities varied largely (from about 60 [fructose 6-phosphate kinase] to about 20 000 [triosephosphate isomerase] nmoles.mg protein(-1).min(-1)). Apparent K-m-values also varied over more than two orders of magnitude (0.035 mM [pyruvate kinase] to 6.16 mM [triosephosphate isomerase]). Fructose 6-phosphate kinase proved to be the fructose 2,6-bisphosphate-regulated type, aldolase the divalent cation-dependent (class II) type and glyceratephosphate mutase the glycerate 2,3-phosphate-independent type of the respective enzymes. Eight of the 10 enzymes exhibited pH-optima between 7.5-8.0. Triosephosphate isomerase and pyruvate kinase showed highest activities at pH 6.5. Regulatory sites within the glycolytic pathway of Suillus bovinus are discussed, fructose 6-phosphate kinase appears to be its main bottle neck.
Publishing Year
ISSN
PUB-ID

Cite this

Grotjohann N, Kowallik W, Thiemann M, et al. Complete sequence of glycolytic enzymes in the mycorrhizal basidiomycete, Suillus bovinus. ZEITSCHRIFT FUER NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES. 1998;53(9-10):818-827.
Grotjohann, N., Kowallik, W., Thiemann, M., Huang, Y., Mutumba, G., Beermann, L., & Broer, D. (1998). Complete sequence of glycolytic enzymes in the mycorrhizal basidiomycete, Suillus bovinus. ZEITSCHRIFT FUER NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES, 53(9-10), 818-827.
Grotjohann, N., Kowallik, W., Thiemann, M., Huang, Y., Mutumba, G., Beermann, L., and Broer, D. (1998). Complete sequence of glycolytic enzymes in the mycorrhizal basidiomycete, Suillus bovinus. ZEITSCHRIFT FUER NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES 53, 818-827.
Grotjohann, N., et al., 1998. Complete sequence of glycolytic enzymes in the mycorrhizal basidiomycete, Suillus bovinus. ZEITSCHRIFT FUER NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES, 53(9-10), p 818-827.
N. Grotjohann, et al., “Complete sequence of glycolytic enzymes in the mycorrhizal basidiomycete, Suillus bovinus”, ZEITSCHRIFT FUER NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES, vol. 53, 1998, pp. 818-827.
Grotjohann, N., Kowallik, W., Thiemann, M., Huang, Y., Mutumba, G., Beermann, L., Broer, D.: Complete sequence of glycolytic enzymes in the mycorrhizal basidiomycete, Suillus bovinus. ZEITSCHRIFT FUER NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES. 53, 818-827 (1998).
Grotjohann, Norbert, Kowallik, W, Thiemann, M, Huang, Y, Mutumba, G, Beermann, L, and Broer, D. “Complete sequence of glycolytic enzymes in the mycorrhizal basidiomycete, Suillus bovinus”. ZEITSCHRIFT FUER NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES 53.9-10 (1998): 818-827.
This data publication is cited in the following publications:
This publication cites the following data publications:

1 Citation in Europe PMC

Data provided by Europe PubMed Central.

Increased trehalose biosynthesis in Hartig net hyphae of ectomycorrhizas.
Lopez MF, Manner P, Willmann A, Hampp R, Nehls U., New Phytol. 174(2), 2007
PMID: 17388901

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 9825541
PubMed | Europe PMC

Search this title in

Google Scholar