L-LYXOSE METABOLISM EMPLOYS THE L-RHAMNOSE PATHWAY IN MUTANT-CELLS OF ESCHERICHIA-COLI ADAPTED TO GROW ON L-LYXOSE

被引:47
作者
BADIA, J
GIMENEZ, R
BALDOMA, L
BARNES, E
FESSNER, WD
AGUILAR, J
机构
[1] UNIV BARCELONA PEDRALBES,SCH PHARM,DEPT BIOCHEM,E-08028 BARCELONA,SPAIN
[2] UNIV FREIBURG,DEPT ORGAN CHEM & BIOCHEM,W-7800 FREIBURG,GERMANY
关键词
D O I
10.1128/jb.173.16.5144-5150.1991
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Escherichia coli cannot grow on L-lyxose, a pentose analog of the 6-deoxyhexose L-rhamnose, which supports the growth of this and other enteric bacteria. L-Rhamnose is metabolized in E. coli by a system that consists of a rhamnose permease, rhamnose isomerase, rhamnulose kinase, and rhamnulose-1-phosphate aldolase, which yields the degradation products dihydroxyacetone phosphate and L-lactaldehyde. This aldehyde is oxidized to L-lactate by lactaldehyde dehydrogenase. All enzymes of the rhamnose system were found to be inducible not only by L-rhamnose but also by L-lyxose. L-Lyxose competed with L-rhamnose for the rhamnose transport system, and purified rhamnose isomerase catalyzed the conversion of L-lyxose into L-xylulose. However, rhamnulose kinase did not phosphorylate L-xylulose sufficiently to support the growth of wild-type E. coli on L-lyxose. Mutants able to grow on L-lyxose were analyzed and found to have a mutated rhamnulose kinase which phosphorylated L-xylulose as efficiently as the wild-type enzyme phosphorylated L-rhamnulose. Thus, the mutated kinase, mapped in the rha locus, enabled the growth of the mutant cells on L-lyxose. The glycolaldehyde generated in the cleavage of L-xylulose 1-phosphate by the rhamnulose-1-phosphate aldolase was oxidized by lactaldehyde dehydrogenase to glycolate, a compound normally utilized by E. coli.
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页码:5144 / 5150
页数:7
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