Catalytic-site mapping of pyruvate formate lyase. Hypophosphite reaction on the acetyl-enzyme intermediate affords carbon-phosphorus bond synthesis (1-hydroxyethylphosphonate)-Reference-Cited by-同舟云学术

Catalytic-site mapping of pyruvate formate lyase. Hypophosphite reaction on the acetyl-enzyme intermediate affords carbon-phosphorus bond synthesis (1-hydroxyethylphosphonate)

Published:1988-12 Issue:2 Volume:178 Page:445-450
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

PLAGA Wulf,FRANK Rainer,KNAPPE Joachim

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1988.tb14468.x/fullpdf

Reference17 articles.

1. Pyruvate Formate-Lyase of Escherichia coli: the Acetyl-Enzyme Intermediate

2. Post-translational activation introduces a free radical into pyruvate formate-lyase.

3. 3. J. Knappe, and F. C. Neidhardt (1987 ) inEscherichia coli and Salmonella typhimurium: cellular and molecular biology () vol. 1 , pp.151 -155 , American Society for Microbiology, Washington DC.

4. Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate-formate-lyase-activating enzyme deduced from the DNA nucleotide sequences

5. Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: Isolation and structural properties

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