Document Detail

Kinetic properties and related changes of molecular weight in a fructokinase from Streptomyces violaceoruber.
MedLine Citation:
PMID:  164228     Owner:  NLM     Status:  MEDLINE    
1. A study of the initial reaction rates at variable substrate concentrations and of the molecular weight of the enzyme in the presence of different effectors, has been carried out using fructokinase (ATP: fructose 6-phosphotransferase, EC from Streptomyces violaceoruber. 2. Saturation curves for MgATP or CoATP are sigmoidal and they change to hyperbolic in the presence of 10 mM Mg2+ or Co2+ in excess over the nucleoside triphosphate. 3. Saturation cuvves for fructose show intermediary plateaux at high (but not at low) concentrations of ATP or Mg2+. 4. The molecular weight of the enzyme in the presence of high concentrations of MgATP is 80 000. In the presence of fructose, and/or Mg2+, the molecular weight is 20 000. 5. The effects of MgADP, uncomplexed ADP or ATP, and low concentrations of detergent on the kinetics have been studied. The results are interpreted as showing the existence of cooperative effects.
B Sabater; G Delafuente
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  377     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1975 Feb 
Date Detail:
Created Date:  1975-07-07     Completed Date:  1975-07-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  258-70     Citation Subset:  IM    
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MeSH Terms
Adenosine Triphosphate / pharmacology
Binding Sites
Cobalt / pharmacology
Coenzyme A / pharmacology
Electrophoresis, Disc
Magnesium / pharmacology
Molecular Weight
Phosphotransferases / metabolism*
Protein Binding
Streptomyces / enzymology*
Reg. No./Substance:
30237-26-4/Fructose; 56-65-5/Adenosine Triphosphate; 7439-95-4/Magnesium; 7440-48-4/Cobalt; 85-61-0/Coenzyme A; EC 2.7.-/Phosphotransferases

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