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 E D T A indicating that the enzyme is a class I aldolase. This enzyme exhibits good stability at high temperatures and extreme stability over a wide p H 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 p H 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.

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The enzymic reaction between ribulose-5-phosphate (1) and spectroscopic methods, especially NOED, the configuration formaldehyde or acetaldehyde catalyzed by hexulose phosof the dephosphorylated products was established as (5R,6S) phate synthase (HPS) from Methylomonas M 15 DSM 580 and (5R,6R). The configuration of two earlier described 7,8yielded ~-arabino-3-hexulose-6-phosphate (2) and two new dideoxy-4-octulose-1 -phosphates (8, 10) synthesized like-7-deoxy-4-heptulose-1-phosphates (4, 6). By various NMR-wise by HPS catalysis must be corrected.