| pubmed-article:1901488 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1901488 | lifeskim:mentions | umls-concept:C0995746 | lld:lifeskim |
| pubmed-article:1901488 | lifeskim:mentions | umls-concept:C0001916 | lld:lifeskim |
| pubmed-article:1901488 | lifeskim:mentions | umls-concept:C0041484 | lld:lifeskim |
| pubmed-article:1901488 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:1901488 | pubmed:dateCreated | 1991-5-9 | lld:pubmed |
| pubmed-article:1901488 | pubmed:abstractText | Site-directed mutagenesis was used to determine the functional role of several residues of Streptomyces glaucescens tyrosinase. Replacement of His-37, -53, -193 or -215 by glutamine yields albino phenotypes, as determined by expression on melanin-indicator plates. The purified mutant proteins display no detectable oxy-enzyme and increased Cu lability at the binuclear active site. The carbonyl derivatives of H189Q and H193Q luminesce, with lambda max. displaced more than 25 nm to a longer wavelength compared with native tyrosinase. The remaining histidine mutants display no detectable luminescence. The results are consistent with these histidine residues (together with His-62 and His-189 reported earlier) acting as Cu ligands in the Streptomyces glaucescens enzyme. Conservative substitution of the invariant Asn-190 by glutamine also gives an albino phenotype, no detectable oxy-enzyme and labilization of active-site Cu. The luminescence spectrum of carbonyl-N190Q, however, closely resembles that of the native enzyme under conditions promoting double Cu occupancy of the catalytic site. A critical role for Asn-190 in active-site hydrogen-bonding interactions is proposed. | lld:pubmed |
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| pubmed-article:1901488 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1901488 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1901488 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1901488 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1901488 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:1901488 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:1901488 | pubmed:author | pubmed-author:LerchKK | lld:pubmed |
| pubmed-article:1901488 | pubmed:author | pubmed-author:JackmanM PMP | lld:pubmed |
| pubmed-article:1901488 | pubmed:author | pubmed-author:HajnalAA | lld:pubmed |
| pubmed-article:1901488 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1901488 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1901488 | pubmed:volume | 274 ( Pt 3) | lld:pubmed |
| pubmed-article:1901488 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1901488 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1901488 | pubmed:pagination | 707-13 | lld:pubmed |
| pubmed-article:1901488 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1901488 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1901488 | pubmed:articleTitle | Albino mutants of Streptomyces glaucescens tyrosinase. | lld:pubmed |
| pubmed-article:1901488 | pubmed:affiliation | Biochemisches Institut, Universität Zürich, Switzerland. | lld:pubmed |
| pubmed-article:1901488 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1901488 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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