Subcloning and nucleotide sequence of the 3,4‐dihydroxyphenylacetate (homoprotocatechuate) 2,3‐dioxygenase gene from Escherichia coli C

FEBS Letters

Roper, David I.¹  Cooper, Ronald A.¹ 

[1] Department of Biochemistry, University of Leicester, Leicester LE1 7RH, UK

关键词: Homoprotocatechuate 2;    3 dioxygenase;    Protein purification;    N-terminal sequence;    Gene sequence;    Derived primary structure;    Escherichia coli C;   

DOI  :  10.1016/0014-5793(90)81437-S

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A cloned gene encoding the Escherichia coli C homoprotocatechuate (HPC) dioxygenase, an aromatic ring cleavage enzyme, was used to produce large amounts of the protein. Preparations of E. coli C HPC dioxygenase, whether expressed from the cloned gene or produced by the bacterium, lost activity very rapidly. The pure protein showed one type of subunit of M ₁ 33000. The first 21 N-terminal amino acids were sequenced and the data used to confirm that the open reading frame of 831 bp, identified from the nucleotide sequence, encoded HPC dioxygenase. Comparison of the derived amino acid sequence with those of other extradiol and intradiol dioxygenases showed no obvious similarity to any of them.

【 授权许可】

Unknown