| pubmed-article:20089849 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20089849 | lifeskim:mentions | umls-concept:C0016213 | lld:lifeskim |
| pubmed-article:20089849 | lifeskim:mentions | umls-concept:C0040005 | lld:lifeskim |
| pubmed-article:20089849 | lifeskim:mentions | umls-concept:C0242209 | lld:lifeskim |
| pubmed-article:20089849 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
| pubmed-article:20089849 | lifeskim:mentions | umls-concept:C0598898 | lld:lifeskim |
| pubmed-article:20089849 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:20089849 | pubmed:dateCreated | 2010-3-22 | lld:pubmed |
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| pubmed-article:20089849 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20089849 | pubmed:abstractText | Pyranose 2-oxidase (P2O) catalyzes the oxidation by O(2) of d-glucose and several aldopyranoses to yield the 2-ketoaldoses and H(2)O(2). Based on crystal structures, in one rotamer conformation, the threonine hydroxyl of Thr(169) forms H-bonds to the flavin-N5/O4 locus, whereas, in a different rotamer, it may interact with either sugar or other parts of the P2O.sugar complex. Transient kinetics of wild-type (WT) and Thr(169) --> S/N/G/A replacement variants show that D-Glc binds to T169S, T169N, and WT with the same K(d) (45-47 mm), and the hydride transfer rate constants (k(red)) are similar (15.3-9.7 s(-1) at 4 degrees C). k(red) of T169G with D-glucose (0.7 s(-1), 4 degrees C) is significantly less than that of WT but not as severely affected as in T169A (k(red) of 0.03 s(-1) at 25 degrees C). Transient kinetics of WT and mutants using d-galactose show that P2O binds d-galactose with a one-step binding process, different from binding of d-glucose. In T169S, T169N, and T169G, the overall turnover with d-Gal is faster than that of WT due to an increase of k(red). In the crystal structure of T169S, Ser(169) O gamma assumes a position identical to that of O gamma 1 in Thr(169); in T169G, solvent molecules may be able to rescue H-bonding. Our data suggest that a competent reductive half-reaction requires a side chain at position 169 that is able to form an H-bond within the ES complex. During the oxidative half-reaction, all mutants failed to stabilize a C4a-hydroperoxyflavin intermediate, thus suggesting that the precise position and geometry of the Thr(169) side chain are required for intermediate stabilization. | lld:pubmed |
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| pubmed-article:20089849 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:20089849 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:20089849 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20089849 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:20089849 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:20089849 | pubmed:author | pubmed-author:DivneChristin... | lld:pubmed |
| pubmed-article:20089849 | pubmed:author | pubmed-author:HaltrichDietm... | lld:pubmed |
| pubmed-article:20089849 | pubmed:author | pubmed-author:TanTien-ChyeT... | lld:pubmed |
| pubmed-article:20089849 | pubmed:author | pubmed-author:ChaiyenPimcha... | lld:pubmed |
| pubmed-article:20089849 | pubmed:author | pubmed-author:SucharitakulJ... | lld:pubmed |
| pubmed-article:20089849 | pubmed:author | pubmed-author:ProngjitMethi... | lld:pubmed |
| pubmed-article:20089849 | pubmed:author | pubmed-author:SpadiutOliver... | lld:pubmed |
| pubmed-article:20089849 | pubmed:author | pubmed-author:PitsawongWari... | lld:pubmed |
| pubmed-article:20089849 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20089849 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:20089849 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:20089849 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20089849 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20089849 | pubmed:pagination | 9697-705 | lld:pubmed |
| pubmed-article:20089849 | pubmed:dateRevised | 2011-7-27 | lld:pubmed |
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| pubmed-article:20089849 | pubmed:meshHeading | pubmed-meshheading:20089849... | lld:pubmed |
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| pubmed-article:20089849 | pubmed:meshHeading | pubmed-meshheading:20089849... | lld:pubmed |
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| pubmed-article:20089849 | pubmed:meshHeading | pubmed-meshheading:20089849... | lld:pubmed |
| pubmed-article:20089849 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20089849 | pubmed:articleTitle | A conserved active-site threonine is important for both sugar and flavin oxidations of pyranose 2-oxidase. | lld:pubmed |
| pubmed-article:20089849 | pubmed:affiliation | Department of Biochemistry and Center of Excellence in Protein Structure and Function, Faculty of Science, Mahidol University, Bangkok 10400, Thailand. | lld:pubmed |
| pubmed-article:20089849 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20089849 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20089849 | lld:pubmed |
