THE CLONING AND EXPRESSION OF THE AROL GENE FROM ESCHERICHIA-COLI-K12 - PURIFICATION AND COMPLETE AMINO-ACID-SEQUENCE OF SHIKIMATE KINASE-II, THE AROL-GENE PRODUCT
THE CLONING AND EXPRESSION OF THE AROL GENE FROM ESCHERICHIA-COLI-K12 - PURIFICATION AND COMPLETE AMINO-ACID-SEQUENCE OF SHIKIMATE KINASE-II, THE AROL-GENE PRODUCT
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DOI：
10.1042/bj2370427
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发表时间：
1986-07-15
影响因子：
4.1
通讯作者：
COGGINS, JR
中科院分区：
文献类型：
--
作者：
MILLAR, G;LEWENDON, A;COGGINS, JR
从大肠杆菌K12中克隆了编码莽草酸激酶II的aroL基因。过表达菌株的构建首次允许将单功能莽草酸激酶纯化至均一。莽草酸激酶II的完整氨基酸序列的核苷酸和直接氨基酸测序相结合的策略确定。E.大肠杆菌莽草酸激酶II是含有173个氨基酸残基的单体酶，计算的Mr为18937。该氨基酸序列包含与其他激酶和ATP需要酶同源的区域。有证据表明aroL基因的转录起始位点位于一个潜在的操作位点内。
The aroL gene encoding the enzyme shikimate kinase II was cloned from Escherichia coli K12. Construction of over-expressing strains permitted for the first time the purification to homogeneity of a monofunctional shikimate kinase. The complete amino acid sequence of shikimate kinase II was determined by a combined nucleotide and direct amino acid sequencing strategy. E. coli shikimate kinase II is a monomeric enzyme containing 173 amino acid residues with a calculated Mr 18937. The amino acid sequence contains a region homologous with other kinases and ATP-requiring enzymes. Evidence is presented suggesting that the transcriptional start site of the aroL gene is located within a potential operator site.