Abstract
The acid phosphatase of an atypical Citrobacter sp. was purified in two isoforms, designated CPI and CPII, which had different K m values for glycerol 1-phosphate and glycerol 2-phosphate The enzyme was not inhibited by the end-product glycerol. Enzyme activity was increased in the presence of phosphate acceptor molecules having free hydroxyl groups (glycerol, methanol, ethanol). 31P-nuclear magnetic resonance spectroscopy indicated transfer of the liberated phosphate onto the alcohol, with the de novo production of (e.g.) glycerol 1-phosphate by enzyme supplemented with phosphomonoester substrate and glycerol.
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