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KMID : 0545120070170091579
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Journal of Microbiology and Biotechnology
2007 Volume.17 No. 9 p.1579 ~ p.1584
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5-Aminolevulinic Acid Biosynthesis in Escherichia coli Coexpressing NADP-dependent Malic Enzyme and 5-Aminolevulinate Synthase
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Shin Jeong-Ah
Kwon Yeong-Deok
Kwon Oh-Hee
Lee Heung-Shick
Kim Pil
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Abstract
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5-Aminolevulinate (ALA) synthase (E.C. 2.3.1.37), which mediates the pyridoxal phosphate-dependent condensation of glycine and succinyl-CoA, encoded by the Rhodobacter sphaeroides hemA gene, enables Escherichia coli strains to produce ALA at a low level. To study the effect of the enhanced C4 metabolism of E. coli on ALA biosynthesis, NADP-dependent malic enzyme (maeB, E.C. 1.1.1.40) was coexpressed with ALA synthase in E. coli. The concentration of ALA was two times greater in cells coexpressing maeB and hemA than in cells expressing hemA alone under anaerobic conditions with medium containing glucose and glycine. Enhanced ALA synthase activity via coupled expression of hemA and maeB may lead to metabolic engineering of E. coli capable of large-scale ALA production
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KEYWORD
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ALA synthase, NADP-dependent malic enzyme, coexpression, 5-aminolevulinic acid
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