Increasing glutathione formation by functional expression of the gamma-glutamylcysteine synthetase gene in Saccharomyces cerevisiae.
A recombinant plasmid, pGMF, containing a gamma-glutamylcysteine synthetase gene (GSH-I) from Saccharomyces cerevisiae, was constructed with a copper-resistance gene as the selection marker and was introduced into S. cerevisiae YSF-31. The glutathione content of the recombinant strain was 1.5-fold (13.1 mg g dry cells(-1)) of that in the host strain.
Fan
Xiuying
X
The Center of Biotechnology, Institute of Microbiology, Academia Sinica, Beijing 100080, PR China.
He
Xiuping
X
Guo
Xuena
X
Qu
Na
N
Wang
Changlu
C
Zhang
Borun
B
D002455:Cell Division / Q000502:physiology; D003001:Cloning, Molecular / Q000379:methods*; D004926:Escherichia coli / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D005721:Glutamate-Cysteine Ligase / Q000235:genetics / Q000378:metabolism*; D005978:Glutathione / Q000096:biosynthesis* / Q000235:genetics; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000096:biosynthesis; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics
D011994:Recombinant Proteins; D005721:Glutamate-Cysteine Ligase; D005978:Glutathione