Production of sepiapterin in Escherichia coli by coexpression of cyanobacterial GTP cyclohydrolase I and human 6-pyruvoyltetrahydropterin synthase.
Synechocystis sp. strain PCC 6803 GTP cyclohydrolase I and human 6-pyruvoyltetrahydropterin synthase were coexpressed in Escherichia coli. The E. coli transformant produced sepiapterin, which was identified by high-performance liquid chromatography and enzymatically converted to dihydrobiopterin by sepiapterin reductase. Aldose reductase, another indispensable enzyme for sepiapterin production, may be endogenous in E. coli.
Woo
Hyun Joo
HJ
Department of Microbiology, Inje University, Kimhae 621-749, Korea.
Kang
Jee Yun
JY
Choi
Yong Kee
YK
Park
Young Shik
YS
D000449:Aldehyde Reductase / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D000458:Cyanobacteria / Q000201:enzymology*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D006136:GTP Cyclohydrolase / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D019761:Phosphorus-Oxygen Lyases / Q000378:metabolism*; D011621:Pteridines / Q000378:metabolism*; D011622:Pterins; D011994:Recombinant Proteins / Q000378:metabolism
D011621:Pteridines; D011622:Pterins; D011994:Recombinant Proteins; C016727:sepiapterin; D000449:Aldehyde Reductase; D006136:GTP Cyclohydrolase; D019761:Phosphorus-Oxygen Lyases; C043497:6-pyruvoyltetrahydropterin synthase