Cloning and characterization of a novel glutathione transferase gene from Penicillium chrysogenum / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 618-622, 2007.
Article
in Chinese
| WPRIM
| ID: wpr-327977
ABSTRACT
Glutathione transferases (GSTs) are a family of multifunctional proteins that mainly catalyze the conjugation of intracellular glutathione (GSH) to a wide variety of endogenous and exogenous electrophilic compounds. GSTs play important roles in stress tolerance and in the detoxification metabolism in organisms. A novel GST gene, Pc gstB, was cloned from penicillin producing fungus Penicillium chrysogenum using RT-PCR. The open reading frame (ORF) of Pc gstB was 651 bp and encoded a peptide of 216 residues. The deduced amino acids sequence had conserved GST domain and showed 65% identity to the characterized Aspergillus fumigutus gstB. The entire ORF of Pc gstB was inserted into vector pTrc99A and transformed into Escherichia coli DH5alpha. Recombinant PcGstB was overexpressed and its GST activity toward substrate 1-chloro-2,4-dinitrobenzene (CDNB) was validated.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Penicillium chrysogenum
/
Recombinant Proteins
/
Fungal Proteins
/
Catalysis
/
Open Reading Frames
/
Cloning, Molecular
/
Sequence Analysis, Protein
/
Escherichia coli
/
Genes, Bacterial
/
Genetics
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2007
Type:
Article
Similar
MEDLINE
...
LILACS
LIS