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| pubmed-article:1655752 | lifeskim:mentions | umls-concept:C0031456 | lld:lifeskim |
| pubmed-article:1655752 | lifeskim:mentions | umls-concept:C0301713 | lld:lifeskim |
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| pubmed-article:1655752 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
| pubmed-article:1655752 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:1655752 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:1655752 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:1655752 | pubmed:issue | 28 | lld:pubmed |
| pubmed-article:1655752 | pubmed:dateCreated | 1991-11-8 | lld:pubmed |
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| pubmed-article:1655752 | pubmed:abstractText | The complete amino acid sequence (296 amino acids) of Chromobacterium violaceum phenylalanine hydroxylase (PAH) was determined by nucleotide analysis of a DNA clone isolated using both a synthetic oligonucleotide probe based on the NH2-terminal amino acid sequence and an antibody against this enzyme. The ApaL I fragment (approximately 1.9 kilobase pairs) containing the entire PAH gene was subcloned in pBluescript II and induced by isopropyl-beta-D-thiogalactopyranoside. In order to eliminate fusion proteins the XbaI/ClaI fragment which contained the PAH gene from the Bluescript construct was subcloned into pMAC 5-8 containing the TAC promoter. The recombinant protein reacts with antibody raised to authentic C. violaceum PAH and its NH2-terminal 20-amino acid sequence and COOH-terminal amino acid residue were identical with the wild-type protein. Key physical and chemical characteristics of the recombinant protein, i.e. its copper content and Michaelis-Menten parameters, were the same as wild-type. Comparison of amino acid sequences revealed a highly conserved region between C. violaceum PAH and three different mammalian aromatic amino acid hydroxylases. This conserved area may well be a catalytically important domain of these pterin- and metal-requiring aromatic amino acid hydroxylases. The over-expression of C. violaceum PAH in Escherichia coli will facilitate the analysis of the enzyme mechanism by various spectroscopic methods. | lld:pubmed |
| pubmed-article:1655752 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1655752 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1655752 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1655752 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1655752 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1655752 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1655752 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1655752 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1655752 | pubmed:author | pubmed-author:BenkovicS JSJ | lld:pubmed |
| pubmed-article:1655752 | pubmed:author | pubmed-author:OnishiAA | lld:pubmed |
| pubmed-article:1655752 | pubmed:author | pubmed-author:LiottaL JLJ | lld:pubmed |
| pubmed-article:1655752 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1655752 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:1655752 | pubmed:volume | 266 | lld:pubmed |
| pubmed-article:1655752 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1655752 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1655752 | pubmed:pagination | 18454-9 | lld:pubmed |
| pubmed-article:1655752 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1655752 | pubmed:meshHeading | pubmed-meshheading:1655752-... | lld:pubmed |
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| pubmed-article:1655752 | pubmed:meshHeading | pubmed-meshheading:1655752-... | lld:pubmed |
| pubmed-article:1655752 | pubmed:meshHeading | pubmed-meshheading:1655752-... | lld:pubmed |
| pubmed-article:1655752 | pubmed:meshHeading | pubmed-meshheading:1655752-... | lld:pubmed |
| pubmed-article:1655752 | pubmed:meshHeading | pubmed-meshheading:1655752-... | lld:pubmed |
| pubmed-article:1655752 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1655752 | pubmed:articleTitle | Cloning and expression of Chromobacterium violaceum phenylalanine hydroxylase in Escherichia coli and comparison of amino acid sequence with mammalian aromatic amino acid hydroxylases. | lld:pubmed |
| pubmed-article:1655752 | pubmed:affiliation | Department of Chemistry, Pennsylvania State University, University Park 16802. | lld:pubmed |
| pubmed-article:1655752 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1655752 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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