Kinetic characteristics of phosphofructokinase from Lactobacillus casei var. Rhamnosus ATCC 7469 and Lactobacillus plantarum ATCC 14917

Doelle H.W. (1972) Kinetic characteristics of phosphofructokinase from Lactobacillus casei var. Rhamnosus ATCC 7469 and Lactobacillus plantarum ATCC 14917. BBA - Enzymology, 258 2: 404-410. doi:10.1016/0005-2744(72)90232-X


Author Doelle H.W.
Title Kinetic characteristics of phosphofructokinase from Lactobacillus casei var. Rhamnosus ATCC 7469 and Lactobacillus plantarum ATCC 14917
Journal name BBA - Enzymology
ISSN 0005-2744
Publication date 1972-02-28
Sub-type Article (original research)
DOI 10.1016/0005-2744(72)90232-X
Volume 258
Issue 2
Start page 404
End page 410
Total pages 7
Subject 2700 Medicine
Abstract The enzyme phosphofructokinase (ATP:d-fructose 6-phosphate 1-phosphotransferase, EC 2.7.1.11) from Lactobacillus casei and Lactobacillus plantarum did not exhibit sigmoidal kinetics. The Km values for ATP were 0.37 mM and 0.67 mM and for Fru-6-P 1.43 mM and 0.15 mM, respectively. The addition of ADP, AMP or adenosine 3′,5′-monophosphate (cyclic AMP) resulted in a general inhibition of the phosphofructokinase from L. plantarum, but not from L. casei. NH4+ stimulated the activity of the enzyme from both sources, but P1 did so only in the case of L. casei. Citrate inhibited the enzyme at physiological concentrations (2-10 mM), but lactate only to a minor extent. The results are discussed in the light of the role of phosphofructokinase as regulatory enzyme in glucose metabolism.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import
 
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