Samland Anne K, Wang Mei, Sprenger Georg A
Institute of Microbiology, Universität Stuttgart, Stuttgart, Germany.
FEMS Microbiol Lett. 2008 Apr;281(1):36-41. doi: 10.1111/j.1574-6968.2008.01079.x.
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 microM at 50 degrees C. MJ0400-His(6) is inhibited competitively by erythrose-4-phosphate with a K(i) of 380 microM and displays heat stability with a half-life of c. 1 h at 100 degrees 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.
细菌中的中心碳代谢已得到充分研究，但古菌的情况并非如此。来自詹氏甲烷球菌的MJ0400-His(6)在50℃下催化1,6-二磷酸果糖（FBP）裂解为3-磷酸甘油醛和磷酸二羟丙酮，V(max)为33 mU mg(-1)，K(m)为430 microM。MJ0400-His(6)受到4-磷酸赤藓糖的竞争性抑制，K(i)为380 microM，并且具有热稳定性，在100℃下的半衰期约为1小时。因此，MJ0400是詹氏甲烷球菌中第二个编码FBP醛缩酶的基因。此前，MJ0400被证明可作为2-氨基-3,7-二脱氧-D-苏式-庚-6-酮糖酸合酶。这表明MJ0400参与了詹氏甲烷球菌的碳代谢和莽草酸途径。
