| pubmed-article:20687613 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20687613 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
| pubmed-article:20687613 | lifeskim:mentions | umls-concept:C0020364 | lld:lifeskim |
| pubmed-article:20687613 | lifeskim:mentions | umls-concept:C0041252 | lld:lifeskim |
| pubmed-article:20687613 | lifeskim:mentions | umls-concept:C0301713 | lld:lifeskim |
| pubmed-article:20687613 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:20687613 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:20687613 | lifeskim:mentions | umls-concept:C0243127 | lld:lifeskim |
| pubmed-article:20687613 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:20687613 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:20687613 | lifeskim:mentions | umls-concept:C0443331 | lld:lifeskim |
| pubmed-article:20687613 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:20687613 | pubmed:dateCreated | 2010-8-31 | lld:pubmed |
| pubmed-article:20687613 | pubmed:abstractText | Tryptophan hydroxylase (TrpH) uses a non-heme mononuclear iron center to catalyze the tetrahydropterin-dependent hydroxylation of tryptophan to 5-hydroxytryptophan. The reactions of the TrpH.Fe(II), TrpH.Fe(II).tryptophan, TrpH.Fe(II).6MePH(4).tryptophan, and TrpH.Fe(II).6MePH(4).phenylalanine complexes with O(2) were monitored by stopped-flow absorbance spectroscopy and rapid quench methods. The second-order rate constant for the oxidation of TrpH.Fe(II) has a value of 104 M(-1) s(-1) irrespective of the presence of tryptophan. Stopped-flow absorbance analyses of the reaction of the TrpH.Fe(II).6MePH(4).tryptophan complex with oxygen are consistent with the initial step being reversible binding of oxygen, followed by the formation with a rate constant of 65 s(-1) of an intermediate I that has maximal absorbance at 420 nm. The rate constant for decay of I, 4.4 s(-1), matches that for formation of the 4a-hydroxypterin product monitored at 248 nm. Chemical-quench analyses show that 5-hydroxytryptophan forms with a rate constant of 1.3 s(-1) and that overall turnover is limited by a subsequent slow step, presumably product release, with a rate constant of 0.2 s(-1). All of the data with tryptophan as substrate can be described by a five-step mechanism. In contrast, with phenylalanine as substrate, the reaction can be described by three steps: a second-order reaction with oxygen to form I, decay of I as tyrosine forms, and slow product release. | lld:pubmed |
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| pubmed-article:20687613 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20687613 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20687613 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:20687613 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20687613 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:20687613 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:20687613 | pubmed:author | pubmed-author:FitzpatrickPa... | lld:pubmed |
| pubmed-article:20687613 | pubmed:author | pubmed-author:PavonJorge... | lld:pubmed |
| pubmed-article:20687613 | pubmed:author | pubmed-author:EserBekirB | lld:pubmed |
| pubmed-article:20687613 | pubmed:author | pubmed-author:HuynhMichaela... | lld:pubmed |
| pubmed-article:20687613 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20687613 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:20687613 | pubmed:volume | 49 | lld:pubmed |
| pubmed-article:20687613 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20687613 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20687613 | pubmed:pagination | 7563-71 | lld:pubmed |
| pubmed-article:20687613 | pubmed:dateRevised | 2011-9-13 | lld:pubmed |
| pubmed-article:20687613 | pubmed:meshHeading | pubmed-meshheading:20687613... | lld:pubmed |
| pubmed-article:20687613 | pubmed:meshHeading | pubmed-meshheading:20687613... | lld:pubmed |
| pubmed-article:20687613 | pubmed:meshHeading | pubmed-meshheading:20687613... | lld:pubmed |
| pubmed-article:20687613 | pubmed:meshHeading | pubmed-meshheading:20687613... | lld:pubmed |
| pubmed-article:20687613 | pubmed:meshHeading | pubmed-meshheading:20687613... | lld:pubmed |
| pubmed-article:20687613 | pubmed:meshHeading | pubmed-meshheading:20687613... | lld:pubmed |
| pubmed-article:20687613 | pubmed:meshHeading | pubmed-meshheading:20687613... | lld:pubmed |
| pubmed-article:20687613 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20687613 | pubmed:articleTitle | Single turnover kinetics of tryptophan hydroxylase: evidence for a new intermediate in the reaction of the aromatic amino acid hydroxylases. | lld:pubmed |
| pubmed-article:20687613 | pubmed:affiliation | Department of Biochemistry and Biophysics, Texas A&M University, College Station,Texas 77843-2128, USA. | lld:pubmed |
| pubmed-article:20687613 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20687613 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20687613 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
