scholarly journals Pyrophosphate-dependent phosphofructo-1-kinase complements fructose 1,6-bisphosphatase but not phosphofructokinase deficiency in Escherichia coli.

1993 ◽  
Vol 175 (17) ◽  
pp. 5723-5724 ◽  
Author(s):  
R G Kemp ◽  
R L Tripathi
Keyword(s):  
Escherichia Coli ◽  
Fructose 1,6 Bisphosphatase ◽  
Phosphofructokinase Deficiency

Purification, kinetic studies, and homology model of Escherichia coli fructose-1,6-bisphosphatase

2002 ◽  
Vol 1594 (1) ◽  
pp. 6-16 ◽  
Author(s):  
Nancy Kelley-Loughnane ◽  
Susan A Biolsi ◽  
Kate M Gibson ◽  
Guqiang Lu ◽  
Michael J Hehir ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Kinetic Studies ◽  
Homology Model ◽  
Fructose 1,6 Bisphosphatase

scholarly journals Purification and Characterization ofglpX-Encoded Fructose 1,6-Bisphosphatase, a New Enzyme of the Glycerol 3-Phosphate Regulon of Escherichia coli

2000 ◽  
Vol 182 (19) ◽  
pp. 5624-5627 ◽  
Author(s):  
Janet L. Donahue ◽  
Jennifer L. Bownas ◽  
Walter G. Niehaus ◽  
Timothy J. Larson
Keyword(s):  
Escherichia Coli ◽  
Glycerol Kinase ◽  
Gene Products ◽  
Purification And Characterization ◽  
Fructose 1,6 Bisphosphatase ◽  
Fructose 1,6 Bisphosphate ◽  
Phosphate Regulon

ABSTRACT In Escherichia coli, gene products of theglp regulon mediate utilization of glycerol andsn-glycerol 3-phosphate. The glpFKX operon encodes glycerol diffusion facilitator, glycerol kinase, and as shown here, a fructose 1,6-bisphosphatase that is distinct from the previously described fbp-encoded enzyme. The purified enzyme was dimeric, dependent on Mn2+ for activity, and exhibited an apparent Km of 35 μM for fructose 1,6-bisphosphate. The enzyme was inhibited by ADP and phosphate and activated by phosphoenolpyruvate.

Overexpression in Escherichia coli and Characterization of the Chloroplast Fructose-1,6-bisphosphatase from Wheat

2000 ◽  
Vol 19 (3) ◽  
pp. 411-418 ◽  
Author(s):  
Gong-Li Tang ◽  
Yan-Fang Wang ◽  
Jian-Shao Bao ◽  
Hai-Bao Chen
Keyword(s):  
Escherichia Coli ◽  
Fructose 1,6 Bisphosphatase

scholarly journals Methanol-dependent Escherichia coli strains with a complete ribulose monophosphate cycle

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Philipp Keller ◽  
Elad Noor ◽  
Fabian Meyer ◽  
Michael A. Reiter ◽  
Stanislav Anastassov ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Triosephosphate Isomerase ◽  
Methanol Conversion ◽  
Adaptive Laboratory Evolution ◽  
Fructose 1,6 Bisphosphatase ◽  
Food And Feed ◽  
Balance Analysis ◽  
Ribulose Monophosphate Cycle ◽  
High Degree ◽  
Rump Cycle

Abstract Methanol is a biotechnologically promising substitute for food and feed substrates since it can be produced renewably from electricity, water and CO2. Although progress has been made towards establishing Escherichia coli as a platform organism for methanol conversion via the energy efficient ribulose monophosphate (RuMP) cycle, engineering strains that rely solely on methanol as a carbon source remains challenging. Here, we apply flux balance analysis to comprehensively identify methanol-dependent strains with high potential for adaptive laboratory evolution. We further investigate two out of 1200 candidate strains, one with a deletion of fructose-1,6-bisphosphatase (fbp) and another with triosephosphate isomerase (tpiA) deleted. In contrast to previous reported methanol-dependent strains, both feature a complete RuMP cycle and incorporate methanol to a high degree, with up to 31 and 99% fractional incorporation into RuMP cycle metabolites. These strains represent ideal starting points for evolution towards a fully methylotrophic lifestyle.

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