Phosphorylation enzymes of the propionic acid bacteria and the roles of ATP inorganic pyrophosphate, and polyphosphates.
It is shown that polyphosphates are not generated in significant amounts in the phosphoglycerate kinase reaction; polyphosphate is more effective than ATP in the formation of glucose 6-P by glucokinase, but the rate with ATP may be adequate to meet the requirements of glucose metabolism; PPi is far more effective than ATP as a phosphate donor in the formation of fructose 1,6-P2 by phosphofructokinase; PPi rather than ATP almost certainly is used in this reaction; and, aside from glucokinase and phosphofructokinase, the enzymes of phosphorylation are specific in their requirements of phosphate donors or acceptors and are present in adequate amounts to meet the requirements of glucose metabolism by the propionic acid bacteria.
Wood
H G
HG
Goss
N H
NH
D000255:Adenosine Triphosphate / Q000378:metabolism*; D011756:Diphosphates / Q000378:metabolism*; D005941:Glucokinase / Q000378:metabolism; D007700:Kinetics; D007773:Lactates / Q000378:metabolism; D019344:Lactic Acid; D010732:Phosphofructokinase-1 / Q000378:metabolism; D010735:Phosphoglycerate Kinase / Q000378:metabolism; D010766:Phosphorylation; D011122:Polyphosphates / Q000378:metabolism*; D011424:Propionibacterium / Q000201:enzymology* / Q000254:growth & development; D011770:Pyruvate Kinase / Q000378:metabolism; D011772:Pyruvate, Orthophosphate Dikinase / Q000378:metabolism
D011756:Diphosphates; D007773:Lactates; D011122:Polyphosphates; D019344:Lactic Acid; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1; D005941:Glucokinase; D011770:Pyruvate Kinase; D010735:Phosphoglycerate Kinase; D011772:Pyruvate, Orthophosphate Dikinase