Repressible alkaline phosphatase from Thermus aquaticus: associated phosphodiesterase activity

A repressible alkaline phosphatase has been isolated from the extreme bacterial thermophile. Thermus aquaticus, and has been purified to homogeneity as judged by disc acrylamide electrophoresis and sodium dodecyl sulfate electrophoresis. Upon investigation, the purified enzyme was shown to hydrolyze...

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Bibliographic Details
Published in:The Journal of biological chemistry 1977-05, Vol.252 (10), p.3399-3401
Main Authors: Smile, D H, Donohue, M, Yeh, M F, Kenkel, T, Trela, J M
Format: Article
Language:English
Subjects:
Adenine Nucleotides - pharmacology
Alkaline Phosphatase - antagonists & inhibitors
Alkaline Phosphatase - metabolism
Electrophoresis, Disc
Enzyme Repression
Glucosephosphates - pharmacology
Gram-Negative Aerobic Bacteria - enzymology
Hydrogen-Ion Concentration
Isoelectric Point
Phosphates - metabolism
Phosphates - pharmacology
Phosphodiesterase Inhibitors
Phosphoric Diester Hydrolases - metabolism
Temperature
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Summary:A repressible alkaline phosphatase has been isolated from the extreme bacterial thermophile. Thermus aquaticus, and has been purified to homogeneity as judged by disc acrylamide electrophoresis and sodium dodecyl sulfate electrophoresis. Upon investigation, the purified enzyme was shown to hydrolyze certain phosphodiesters in addition to a wide variety of phosphomonoesters. The diesters included bis-p-nitro-phenyl phosphate and thymidine 3'-monophospho-p-nitro-phenyl ester. The temperature optimum for the diesterase activity was 80--85 degrees at pH 7.2. Orthophosphate competitively inhibited both activities. Nucleotides such as AMP, ADP, and ATP also inhibited both esterase activities as did alpha-D-glucose 1-phosphate and alpha-sodium glycerol phosphate. The isoelectric point of the enzyme was determined to be 8.4.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)40404-2