(Q43146135)

English

Inhibition kinetics of catabolic dehydrogenases by elevated moieties of ATP and ADP--implication for a new regulation mechanism in Lactococcus lactis

scientific article published on 24 February 2010

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

14 November 2017

Inhibition kinetics of catabolic dehydrogenases by elevated moieties of ATP and ADP--implication for a new regulation mechanism in Lactococcus lactis (English)

1 reference

Europe PubMed Central

PubMed publication ID

14 November 2017

Lactococcus lactis

object named as

Lactococcus lactis

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based on heuristic

inferred from title

author name string

Rong Cao

1

1 reference

Europe PubMed Central

PubMed publication ID

14 November 2017

Ahmad A Zeidan

2

1 reference

Europe PubMed Central

PubMed publication ID

14 November 2017

Peter Rådström

3

1 reference

Europe PubMed Central

PubMed publication ID

14 November 2017

Ed W J van Niel

4

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Europe PubMed Central

PubMed publication ID

14 November 2017

language of work or name

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publication date

24 February 2010

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Europe PubMed Central

PubMed publication ID

14 November 2017

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Europe PubMed Central

PubMed publication ID

14 November 2017

277

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Europe PubMed Central

PubMed publication ID

14 November 2017

8

1 reference

Europe PubMed Central

PubMed publication ID

14 November 2017

1843-1852

1 reference

Europe PubMed Central

PubMed publication ID

14 November 2017

The pool of ADP and ATP regulates anaerobic product formation in resting cells of Lactococcus lactis

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Physiological role of beta-phosphoglucomutase in Lactococcus lactis

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Analysis of the combined effect of two linear inhibitors on a single enzyme

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Physiology of pyruvate metabolism in Lactococcus lactis

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Is the glycolytic flux in Lactococcus lactis primarily controlled by the redox charge? Kinetics of NAD(+) and NADH pools determined in vivo by 13C NMR.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Control of the shift from homolactic acid to mixed-acid fermentation in Lactococcus lactis: predominant role of the NADH/NAD+ ratio

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Changes in glycolytic activity of Lactococcus lactis induced by low temperature

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Inhibition of glucose 6-phosphate dehydrogenase by adenosine 5'-triphosphate

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

IS981-mediated adaptive evolution recovers lactate production by ldhB transcription activation in a lactate dehydrogenase-deficient strain of Lactococcus lactis

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Proteome analysis of a Lactococcus lactis strain overexpressing gapA suggests that the gene product is an auxiliary glyceraldehyde 3-phosphate dehydrogenase

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Horse liver alcohol dehydrogenase SS: Purification and characterization of the homogeneous isoenzyme

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Experimental evidence for allosteric modifier saturation as predicted by the bi-substrate Hill equation.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

The small world of metabolism.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Cellular concentrations of enzymes and their substrates

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Cytosolic redox metabolism in aerobic chemostat cultures of Saccharomyces cerevisiae.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Glycolysis and the regulation of glucose transport in Lactococcus lactis spp. lactis in batch and fed-batch culture

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Transfer of Streptococcus lactis and Related Streptococci to the Genus Lactococcus gen. nov.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Control of glycolysis by glyceraldehyde-3-phosphate dehydrogenase in Streptococcus cremoris and Streptococcus lactis

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Can yeast glycolysis be understood in terms of in vitro kinetics of the constituent enzymes? Testing biochemistry

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2010.07601.X

21 January 2018

Identifiers

10.1111/J.1742-4658.2010.07601.X

1 reference

Europe PubMed Central

PubMed publication ID

14 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

14 November 2017

ResearchGate publication ID

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