Requires Mg2+ for activity. While purified enzyme from Escherichia coli is specific for acetate , others have found that the enzyme can also use propanoate as a substrate, but more slowly . Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8, phosphate acetyltransferase. Both this enzyme and EC 2.7.2.15, propionate kinase, play important roles in the production of propanoate .
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
(S)-lactate fermentation to propanoate, acetate and hydrogen, (S)-propane-1,2-diol degradation, acetate and ATP formation from acetyl-CoA I, acetylene degradation (anaerobic), Bifidobacterium shunt, ethanolamine utilization, gallate degradation III (anaerobic), glycine degradation (reductive Stickland reaction), L-lysine fermentation to acetate and butanoate, L-threonine degradation I, lactate fermentation to acetate, CO2 and hydrogen (Desulfovibrionales), methanogenesis from acetate, mixed acid fermentation, purine nucleobases degradation I (anaerobic), purine nucleobases degradation II (anaerobic), pyruvate fermentation to acetate II, pyruvate fermentation to acetate IV, reductive glycine pathway of autotrophic CO2 fixation, superpathway of fermentation (Chlamydomonas reinhardtii)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ATP:acetate phosphotransferase
Requires Mg2+ for activity. While purified enzyme from Escherichia coli is specific for acetate [4], others have found that the enzyme can also use propanoate as a substrate, but more slowly [7]. Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8, phosphate acetyltransferase. Both this enzyme and EC 2.7.2.15, propionate kinase, play important roles in the production of propanoate [9].