Open AccessMJ0400 from Methanocaldococcus jannaschii exhibits fructose‐1,6‐bisphosphate aldolase activity
Author(s) -
Samland Anne K.,
Wang Mei,
Sprenger Georg A.
Publication year - 2008
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2008.01079.x
Subject(s) - aldolase a , dihydroxyacetone phosphate , aldolase b , biochemistry , archaea , methanococcus , glyceraldehyde , fructose , fructose bisphosphate aldolase , chemistry , shikimate pathway , stereochemistry , biology , phosphate , biosynthesis , enzyme , dehydrogenase , gene
Abstract The central carbon metabolism is well investigated in bacteria, but this is not the case for archaea. MJ0400‐His 6 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‐His 6 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 .