Aldolase and transaldolase activities reported in Archaea.

(1) In the coupled assay, aldolase activity was determined using coupled assay, were the cleavage of F-1,6-P was coupled with glycerol-3-phosphate dehydrogenase (EC 1.1.1.8) and triose-phosphate isomerase (TIM, EC 5.3.1.1) of rabbit muscle. Enzymatic activities were measured by monitoring the increase in absorption of NADH at 366 nm (ε50°C = 3.36 mm−1cm−1).(2) DHQ generated with recombinant proteins was determined by GC-MS.(3) Formation of DHAP was measured by Colorimetric assay (see materials and methods for details).(4) MJ0400 from M. jannaschii is homologous to OE1472F from H. salinarum and MMP0686 from M. maripaludis. Predicted transaldolase catalyzing the first reaction of the AroAA biosynthesis pathway in these organisms.(5) MJ1585 from M. jannaschii is homologous to OE2019F from H. salinarum and MMP0293 from M. maripaludis. It is an aldolase.(6) MJ1249 is homologous to OE1475F from H. salinarum and MMP0006 from M. maripaludis. It is believed to catalyze the second reaction in the AroAA biosynthesis, synthesizing DHQ.(7) Thermoproteus tenax, crenarchaeon.(8) Pyrococcus furiosus, euryarchaeon.(9) GenBank accession number.Aldolase and transaldolase activities reported in Archaea.