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Preparations of <jats:italic>E. coli<\/jats:italic> 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 <jats:italic>M<\/jats:italic>\n<jats:sub>1<\/jats:sub> 33000. The first 21 N\u2010terminal 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.<\/jats:p>","DOI":"10.1016\/0014-5793(90)81437-s","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T07:44:17Z","timestamp":1027583057000},"page":"53-57","source":"Crossref","is-referenced-by-count":45,"title":["Subcloning and nucleotide sequence of the 3,4\u2010dihydroxyphenylacetate (homoprotocatechuate) 2,3\u2010dioxygenase gene from <i>Escherichia coli<\/i> C"],"prefix":"10.1002","volume":"275","author":[{"given":"David I.","family":"Roper","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ronald A.","family":"Cooper","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2001,12,7]]},"reference":[{"key":"e_1_2_1_2_1","unstructured":"1975 Academic Press London S. 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