MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity |
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Authors: | Anne K Samland Mei Wang & Georg A Sprenger |
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Institution: | Institute of Microbiology, Universität Stuttgart, Stuttgart, Germany |
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Abstract: | The central carbon metabolism is well investigated in bacteria, but this is not the case for archaea. MJ0400-His6 from Methanocaldococcus jannaschii catalyzes the cleavage of fructose-1,6-bisphosphate (FBP) to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate with a V max of 33 mU mg?1 and a K m of 430 μM at 50 °C. MJ0400-His6 is inhibited competitively by erythrose-4-phosphate with a K i of 380 μM and displays heat stability with a half-life of c . 1 h at 100 °C. Hence, MJ0400 is the second gene encoding for an FBP aldolase in M. jannaschii . Previously, MJ0400 was shown to act as an 2-amino-3,7-dideoxy- d - threo -hept-6-ulosonic acid synthase. This indicates that MJ0400 is involved in both the carbon metabolism and the shikimate pathway in M. jannaschii . |
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Keywords: | archaeal FBP aldolase aromatic amino acid biosynthesis carbon metabolism heat stability MJ0400 substrate specificity |
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