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Phosphotransferase activity of acid phosphatases of a Citrobacter sp. (1997)

Jeong, B.C ; Kim, H.-W ; Macaskie, L.E

Oxford, UK : Blackwell Publishing Ltd

FEMS microbiology letters 147 (1997), S. 0

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ISSN: 1574-6968

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: The acid phosphatase of an atypical Citrobacter sp. was purified in two isoforms, designated CPI and CPII, which had different Km 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1574-6968.1997.tb10227.x

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