Propionate kinase (, PduW, TdcD, propionate/acetate kinase) is an enzyme with systematic name ATP:propanoate phosphotransferase. It catalyses the following reversible chemical reaction
The enzyme characterised from Escherichia coli requires magnesium ion (Mg2+) and converts propionic acid to propanoyl phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The reaction is part of a sequence which degrades the amino acid L-threonine to propionic acid. The enzyme is also found in Salmonella enterica, which allows that bacterium to grow on propylene glycol. It can also act on acetic acid.
Structural studies X-ray crystallography has been used to determine the structure of the enzyme from Salmonella typhimurium.
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