PRODUCTION OF CHORISMATE MUTASE-PREPHENATE DEHYDROGENASE BY A STRAIN OF ESCHERICHIA-COLI CARRYING A MULTICOPY, TYRA PLASMID - ISOLATION AND PROPERTIES OF THE ENZYME

被引:13
作者
BHOSALE, SB [1 ]
ROOD, JI [1 ]
SNEDDON, MK [1 ]
MORRISON, JF [1 ]
机构
[1] AUSTRALIAN NATL UNIV, JOHN CURTIN SCH MED RES, DEPT BIOCHEM, CANBERRA, ACT 2601, AUSTRALIA
关键词
D O I
10.1016/0304-4165(82)90372-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A multicopy plasmid that contains the tyrosine operon was used to transform strains of E. coli K-12. The resultant strains yielded levels of chorismate mutase-prephenate dehydrogenase that were up to 5000-fold higher than that given by the parent strain and about 6-fold higher than that given by a tyrR strain. The production of enzyme fell when tetracycline was omitted from the growth medium because of the loss of the plasmid. The bifunctional enzyme was isolated in good yield by a simple purification procedure and shown to possess properties identical to those exhibited by the enzyme from a tyrR strains.
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页码:6 / 11
页数:6
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