Fructose-1,6-bisphosphatase from Corynebacterium glutamicum : expression and deletion of the fbp gene and biochemical characterization of the enzyme

2003 ◽  
Vol 180 (4) ◽  
pp. 285-292 ◽  
Author(s):  
Doris Rittmann ◽  
Steffen Schaffer ◽  
Volker F. Wendisch ◽  
Hermann Sahm
Keyword(s):  
Corynebacterium Glutamicum ◽  
Biochemical Characterization ◽  
Fructose 1,6 Bisphosphatase

scholarly journals Structural and Biochemical Characterization of the Type II Fructose-1,6-bisphosphatase GlpX fromEscherichia coli

2008 ◽  
Vol 284 (6) ◽  
pp. 3784-3792 ◽  
Author(s):  
Greg Brown ◽  
Alexander Singer ◽  
Vladimir V. Lunin ◽  
Michael Proudfoot ◽  
Tatiana Skarina ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Type Ii ◽  
Fromescherichia Coli ◽  
Fructose 1,6 Bisphosphatase

Genetic and biochemical characterization of a 4-hydroxybenzoate hydroxylase from Corynebacterium glutamicum

2008 ◽  
Vol 78 (1) ◽  
pp. 75-83 ◽  
Author(s):  
Yan Huang ◽  
Ke-xin Zhao ◽  
Xi-Hui Shen ◽  
Chen-Ying Jiang ◽  
Shuang-Jiang Liu
Keyword(s):  
Corynebacterium Glutamicum ◽  
Biochemical Characterization ◽  
Hydroxybenzoate Hydroxylase

Biochemical characterization of two thymidylate synthases in Corynebacterium glutamicum NCHU 87078

2010 ◽  
Vol 1804 (9) ◽  
pp. 1751-1759 ◽  
Author(s):  
Shu-Chen Kan ◽  
Jai-Shin Liu ◽  
Hui-Yu Hu ◽  
Chia-Ming Chang ◽  
Wei-De Lin ◽  
...  
Keyword(s):  
Corynebacterium Glutamicum ◽  
Biochemical Characterization ◽  
Thymidylate Synthases

scholarly journals Molecular and Biochemical Characterization of a Distinct Type of Fructose-1,6-Bisphosphatase from Pyrococcus furiosus

2002 ◽  
Vol 184 (12) ◽  
pp. 3401-3405 ◽  
Author(s):  
Corné H. Verhees ◽  
Jasper Akerboom ◽  
Emile Schiltz ◽  
Willem M. de Vos ◽  
John van der Oost
Keyword(s):  
Biochemical Characterization ◽  
Pyrococcus Furiosus ◽  
Distinct Type ◽  
Sequence Motifs ◽  
Conserved Sequence ◽  
New Family ◽  
Fructose 1,6 Bisphosphatase ◽  
Conserved Sequence Motifs ◽  
Fructose 1,6 Bisphosphate

ABSTRACT The Pyrococcus furiosus fbpA gene was cloned and expressed in Escherichia coli, and the fructose-1,6-bisphosphatase produced was subsequently purified and characterized. The dimeric enzyme showed a preference for fructose-1,6-bisphosphate, with a Km of 0.32 mM and a V max of 12.2 U/mg. The P. furiosus fructose-1,6-bisphosphatase was strongly inhibited by Li+ (50% inhibitory concentration, 1 mM). Based on the presence of conserved sequence motifs and the substrate specificity of the P. furiosus fructose-1,6-bisphosphatase, we propose that this enzyme belongs to a new family, class IV fructose-1,6-bisphosphatase.

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