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.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Grotjohann, NorbertUniBi ; Kowallik, W; Thiemann, M; Huang, Y; Mutumba, G; Beermann, L; Broer, D
Abstract / Bemerkung
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.
Stichworte
6-bisphosphate-dependent fructose 6-phosphate kinase; 2; glycolytic enzymes; Suillus bovinus; fructose; class II aldolase; mycorrhiza
Erscheinungsjahr
1998
Zeitschriftentitel
ZEITSCHRIFT FUER NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES
Band
53
Ausgabe
9-10
Seite(n)
818-827
ISSN
0939-5075
Page URI
https://pub.uni-bielefeld.de/record/1624520

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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, Norbert, 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 (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.

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PMID: 17388901
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