Enzymatic phosphorylation of butyrate.

Conservation of thiol ester bond energy through a reaction sequence involving phosphorolysis of acetyl coenzyme A by phosphotransacetylase (1, 2) and the subsequent formation of adenosine triphosphate from adenosine diphosphate and acetyl phosphate by acetokinase (3, 4) is well established in fermentative bacteria. A similar reaction sequence involving butyryl coenzyme A, phosphotransbutyrylase, and a butyrate-phosphorylating enzyme, butyrokinase, has been predicted to play an important role in energy conservation by the saccharolytic clostridia (5-7). The present report is concerned with the purification and properties of a butyrokinase from Clostridium butyricum. A brief report of some of these properties has appeared (8).

• Publication year

  1962

• Venue

  Journal of Biological Chemistry

• Publication date

  1962-08-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/s0021-9258(19)73776-4PMID 13923331
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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