Abstract
A 2.9 kb DNA fragment encoding s-(2-aminoethyl)-l-cysteine (AEC) resistant aspartokinase of Corynebacteriumglutamicum was cloned on the C.glutamicum/E.coli shuttle vector pECCG117. A recombinant plasmid, designated pAK12, conferred the AEC resistance, the ability to excrete lysine and threonine, and the 3-5 fold increased specific activity of aspartokinase to host strain.
| Original language | English |
|---|---|
| Pages (from-to) | 721-726 |
| Number of pages | 6 |
| Journal | Biotechnology Letters |
| Volume | 13 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - 1991 Oct 1 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology
Cite this
}
Molecular cloning and expression of s-(2-aminoethyl)-L-cysteine resistant aspartokinase gene of Corynebacteriumglutamicum. / Han, Jong Kwon; Oh, Jong-Won; Lee, Hyune Hwan; Chung, Stephen; Hyun, Hyung Hwan; Lee, Jae Heung.
In: Biotechnology Letters, Vol. 13, No. 10, 01.10.1991, p. 721-726.Research output: Contribution to journal › Article
TY - JOUR
T1 - Molecular cloning and expression of s-(2-aminoethyl)-L-cysteine resistant aspartokinase gene of Corynebacteriumglutamicum
AU - Han, Jong Kwon
AU - Oh, Jong-Won
AU - Lee, Hyune Hwan
AU - Chung, Stephen
AU - Hyun, Hyung Hwan
AU - Lee, Jae Heung
PY - 1991/10/1
Y1 - 1991/10/1
N2 - A 2.9 kb DNA fragment encoding s-(2-aminoethyl)-l-cysteine (AEC) resistant aspartokinase of Corynebacteriumglutamicum was cloned on the C.glutamicum/E.coli shuttle vector pECCG117. A recombinant plasmid, designated pAK12, conferred the AEC resistance, the ability to excrete lysine and threonine, and the 3-5 fold increased specific activity of aspartokinase to host strain.
AB - A 2.9 kb DNA fragment encoding s-(2-aminoethyl)-l-cysteine (AEC) resistant aspartokinase of Corynebacteriumglutamicum was cloned on the C.glutamicum/E.coli shuttle vector pECCG117. A recombinant plasmid, designated pAK12, conferred the AEC resistance, the ability to excrete lysine and threonine, and the 3-5 fold increased specific activity of aspartokinase to host strain.
UR - http://www.scopus.com/inward/record.url?scp=0026015163&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026015163&partnerID=8YFLogxK
U2 - 10.1007/BF01088176
DO - 10.1007/BF01088176
M3 - Article
AN - SCOPUS:0026015163
VL - 13
SP - 721
EP - 726
JO - Biotechnology Letters
JF - Biotechnology Letters
SN - 0141-5492
IS - 10
ER -