Phosphotransferase activity of acid phosphatases of a Citrobacter sp. |
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| Authors: | BC Jeong H-W Kim LE Macaskie |
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| Institution: | Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Yusong, Taejon, South Korea;Fermentation/Bioconversion Process Research Unit, Korea Research Institute of Bioscience and Biotechnology, Yusong, Taejon, South Korea |
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| Abstract: | 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. |
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| Keywords: | Acetyl-CoA synthetase acs Acetate utilization IclR RpoS Escherichia coli |
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