Purification and characterization of a class I fructose 1,6-bisphosphate aldolase from Staphylococcus carnosus |
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Authors: | H. P. Brockamp M. R. Kula |
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Affiliation: | (1) Institut für Enzymtechnologie der Heinrich-Heine Universität Düsseldorf im Forschungszentrum Jülich, Postfach 20 50, D-5170 Jülich, Federal Republic of Germany |
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Abstract: | Summary A fructose 1,6-bisphosphate aldolase (E.C.4.1.2.13) from Staphylococcus carnosus DSM 20501 was purified for the first time. The enzymatic activity was insensitive to high levels of EDTA indicating that the enzyme is a class I aldolase. This enzyme exhibits good stability at high temperatures and extreme stability over a wide pH range. The Km for fructose 1,6-bisphosphate as substrate was 0.022 mm. The S. carnosus aldolase is a monomeric enzyme with a molecular mass of about 33 kDa. It exhibits a relatively broad pH optimum between pH 6.5 and 9.0. Furthermore, the aldolase accepts other aldehydes in place of its natural substrate, glyceraldehyde 3-phosphate, allowing the synthesis of various sugar phosphates.Offprint requests to: M. R. Kula |
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