5-aminolevulinic acid biosynthesis in Escherichia coli coexpressing NADP-dependent malic enzyme and 5-aminolevulinate synthase.
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.
Department of Biotechnology, The Catholic University of Korea, Bucheon, Gyunggi 420-743, Korea.
Jeong-Ah
JA
Shin
Yeong Deok
YD
Kwon
Oh-Hee
OH
Kwon
Heung Shick
HS
Lee
Pil
P
Kim
D000624:5-Aminolevulinate Synthetase / Q000235:genetics / Q000378:metabolism*; D000622:Aminolevulinic Acid / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D008291:Malate Dehydrogenase / Q000235:genetics* / Q000378:metabolism
D000622:Aminolevulinic Acid; D008291:Malate Dehydrogenase; C031917:malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+); D000624:5-Aminolevulinate Synthetase