Richard John P
Department of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, USA.
ACS Chem Biol. 2008 Oct 17;3(10):605-7. doi: 10.1021/cb800238s.
Gluconeogenesis is blocked in a strain of Escherichia coli that is deficient in triosephosphate isomerase, but it was restored by the insertion of a plasmid coding for an L-glyceraldehyde 3-phosphate reductase (YghZ). This reductase provides a "bypass" that produces dihydroxyacetone phosphate (DHAP) by the consecutive enzyme-catalyzed reduction of L-glyceraldehyde 3-phosphate ( L-GAP) by NADPH to give L-glycerol 3-phosphate and reoxidation by NAD(+) catalyzed by endogenous L-glycerol 3-phosphate dehydrogenase to give DHAP. The origin of cellular L-GAP remains to be determined.
在一株缺乏磷酸丙糖异构酶的大肠杆菌中,糖异生作用受阻,但通过插入编码L-甘油醛3-磷酸还原酶(YghZ)的质粒得以恢复。这种还原酶提供了一条“旁路”,通过NADPH连续酶促还原L-甘油醛3-磷酸(L-GAP)生成L-甘油3-磷酸,再由内源性L-甘油3-磷酸脱氢酶催化被NAD(+)重新氧化生成磷酸二羟丙酮(DHAP)。细胞内L-GAP的来源仍有待确定。