@article{Pollegioni1992Studi-8219,
  year={1992},
  doi={10.1042/bj2860389},
  title={Studies on the active centre of Rhodotorula gracilis D-amino acid oxidase and comparison with pig kidney enzyme},
  number={2},
  volume={286},
  issn={0264-6021},
  journal={Biochemical Journal},
  pages={389--394},
  author={Pollegioni, Loredano and Ghisla, Sandro and Pilone, Mirella S.}
}

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    <dc:creator>Pilone, Mirella S.</dc:creator>
    <dc:contributor>Pilone, Mirella S.</dc:contributor>
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    <dcterms:issued>1992</dcterms:issued>
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    <dcterms:bibliographicCitation>First publ. in: Biochemical Journal ; 286 (1992). - S. 389-394</dcterms:bibliographicCitation>
    <dc:creator>Ghisla, Sandro</dc:creator>
    <dc:contributor>Ghisla, Sandro</dc:contributor>
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    <dc:creator>Pollegioni, Loredano</dc:creator>
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    <dc:contributor>Pollegioni, Loredano</dc:contributor>
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    <dcterms:title>Studies on the active centre of Rhodotorula gracilis D-amino acid oxidase and comparison with pig kidney enzyme</dcterms:title>
    <dcterms:abstract xml:lang="eng">D-Amino acid oxidase (EC 1.4.3.3) from Rhodotorula gracilis has been reconstituted with 8-chloro-, 8-mercapto-, 6-hydroxy-, 2-thio-, 5-deaza- and 1-deaza-FAD, and the properties of the resulting complexes have been studied and compared with those of the correspondingly modified pig kidney D-amino acid oxidases. Binding appears to be tight for most analogues, at least as tight as for native FAD (~10(-8) M). 8-Mercapto- and 6-hydroxy-FAD bind in their para- and ortho-quinoid forms respectively to yeast D-amino acid oxidase, inferring the presence of a positive charge near the flavin N(1) position, as in the case of the mammalian enzyme. On the other hand, important differences in active-site microenvironment emerge: solvent accessibility to flavin position 8 is drastically restricted in yeast D-amino acid oxidase as indicated by the unreactivity of 8-chloro- and 8-mercapto-FAD enzyme with thiolates and alkylating agents. Significantly different microenvironments are also likely to occur around the flavin positions N(1)-C(2) = 0, N(3)-H and N(5). This is deduced from the differences in interaction of the two proteins with 1-deaza-FAD, 5-deaza-FAD and 2-thio-FAD and from the properties of the respective complexes. The same re-side flavin stereospecificity as shown by the mammalian enzyme was determined for the yeast enzyme using 8-hydroxy-5-deaza-FAD. Thus we can deduce the presence of a similar pattern of functional groups at the active centres of the two enzymes, while the fine tuning of specificity and regulation correlate with environmental differences at specific flavin loci.</dcterms:abstract>
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