Inactivation of Escherichia coli pyruvate formate-lyase by hypophosphite: evidence for a rate-limiting phosphorus-hydrogen bond cleavage

Biochemistry ◽  
1988 ◽  
Vol 27 (6) ◽  
pp. 2217-2222 ◽  
Author(s):  
Edward J. Brush ◽  
Koren A. Lipsett ◽  
John W. Kozarich
Keyword(s):  
Escherichia Coli ◽  
Hydrogen Bond ◽  
Bond Cleavage ◽  
Pyruvate Formate Lyase ◽  
Rate Limiting

scholarly journals Assembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin. Kinetics and molecular basis of rate-limiting steps in vitro.

1996 ◽  
Vol 271 (43) ◽  
pp. 27188
Author(s):  
Lloyd W. Ruddock ◽  
Jeremy J.F. Coen ◽  
Caroline Cheesman ◽  
Robert B. Freedman ◽  
Timothy R. Hirst
Keyword(s):  
Escherichia Coli ◽  
Molecular Basis ◽  
B Subunit ◽  
Heat Labile ◽  
Rate Limiting

scholarly journals Carbon-Hydrogen Bond Activation of Phenyldi(2- Thienyl)Phosphine at A Triruthenium Cluster Center

2012 ◽  
Vol 25 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Shahed Rana ◽  
Shishir Ghosh ◽  
Shariff E Kabir
Keyword(s):  
Hydrogen Bond ◽  
Elemental Analysis ◽  
Bond Activation ◽  
Bond Cleavage ◽  
Chemical Society ◽  
Cluster Center ◽  
Carbon Hydrogen Bond Activation

Ketyl-initiated reaction between Ru3(CO)12 and phenyldi(2-thienyl)phosphine (PhPTh2) furnished simple phosphine-substituted triruthenium clusters [Ru3(CO)10(PhPTh2)21 and [Ru3(CO)9(PhPTh2)3] 2. Heating 1 in boiling benzene afforded [Ru3(CO)8{?3- PhThP(C4H2S)}(PhPTh2)] 3 by carbon-hydrogen bond cleavage of a coordinated thienylphosphine ligand. All three new clusters have been characterized by elemental analysis, IR and NMR spectroscopic data.DOI: http://dx.doi.org/10.3329/jbcs.v25i1.11764 Journal of Bangladesh Chemical Society, Vol. 25(1), 1-6, 2012

Fatty acid uptake in Escherichia coli: regulation by recruitment of fatty acyl-CoA synthetase to the plasma membrane

1993 ◽  
Vol 71 (1-2) ◽  
pp. 51-56 ◽  
Author(s):  
Dev Mangroo ◽  
Gerhard E. Gerber
Keyword(s):  
Escherichia Coli ◽  
Plasma Membrane ◽  
Fatty Acid ◽  
Fatty Acid Uptake ◽  
Fatty Acyl ◽  
Acid Uptake ◽  
Bacterial Membranes ◽  
Rate Limiting Step ◽  
Triton X ◽  
Rate Limiting

Fatty acid uptake in Escherichia coli has been shown to be inhibited by starvation and to be reversed by a short preincubation of the starved cells with D- or L-lactate, succinate, and acetate; these effects on oleate uptake were due to regulation of the rate-limiting step which involves fatty acyl-CoA synthetase. Investigation into the mechanism of regulation of fatty acyl-CoA synthetase showed that D-lactate did not affect the activity of the enzyme directly. Fatty acyl-CoA synthetase was found to be activated by about 20-fold by Triton X-100 and by another 4-fold by the addition of bacterial membranes. D-Lactate treatment was shown to result in coisolation of fatty acyl-CoA synthetase with the plasma membrane; these results are consistent with the interpretation that recruitment of the enzyme to the plasma membrane by D-lactate results in its activation and consequently in the increased level of fatty acid uptake.Key words: fatty acid, uptake, regulation, recruitment, fatty acyl-CoA synthetase, Escherichia coli, plasma membrane.

Enzyme-dependent Activation of Pyruvate Formate-lyase of Escherichia coli

1972 ◽  
pp. 319-329 ◽  
Author(s):  
Joachim Knappe ◽  
Hans-Peter Blaschkowski ◽  
Rudolf Edenharder
Keyword(s):  
Escherichia Coli ◽  
Pyruvate Formate Lyase

scholarly journals Production of Glucaric Acid from a Synthetic Pathway in Recombinant Escherichia coli

2008 ◽  
Vol 75 (3) ◽  
pp. 589-595 ◽  
Author(s):  
Tae Seok Moon ◽  
Sang-Hwal Yoon ◽  
Amanda M. Lanza ◽  
Joseph D. Roy-Mayhew ◽  
Kristala L. Jones Prather
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Syringae ◽  
Glucuronic Acid ◽  
Value Added ◽  
Culture Broth ◽  
Glucaric Acid ◽  
Synthetic Pathway ◽  
Genes Encoding ◽  
Microbial System ◽  
Rate Limiting

ABSTRACT A synthetic pathway has been constructed for the production of glucuronic and glucaric acids from glucose in Escherichia coli. Coexpression of the genes encoding myo-inositol-1-phosphate synthase (Ino1) from Saccharomyces cerevisiae and myo-inositol oxygenase (MIOX) from mice led to production of glucuronic acid through the intermediate myo-inositol. Glucuronic acid concentrations up to 0.3 g/liter were measured in the culture broth. The activity of MIOX was rate limiting, resulting in the accumulation of both myo-inositol and glucuronic acid as final products, in approximately equal concentrations. Inclusion of a third enzyme, uronate dehydrogenase (Udh) from Pseudomonas syringae, facilitated the conversion of glucuronic acid to glucaric acid. The activity of this recombinant enzyme was more than 2 orders of magnitude higher than that of Ino1 and MIOX and increased overall flux through the pathway such that glucaric acid concentrations in excess of 1 g/liter were observed. This represents a novel microbial system for the biological production of glucaric acid, a “top value-added chemical” from biomass.

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