| pubmed-article:9494080 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9494080 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:9494080 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
| pubmed-article:9494080 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
| pubmed-article:9494080 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:9494080 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
| pubmed-article:9494080 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:9494080 | pubmed:dateCreated | 1998-5-21 | lld:pubmed |
| pubmed-article:9494080 | pubmed:abstractText | 13C- and 15N-NMR studies of the reaction of aromatic amine dehydrogenase (AADH) with methylamine demonstrated that the products of the reductive half-reaction are an equivalent of formaldehyde hydrate and a reduced aminoquinol form of the tryptophan tryptophylquinone (TTQ) cofactor which contains covalently bound substrate-derived N. These data are consistent with the Ping Pong kinetic mechanism and aminotransferase-type chemical reaction mechanism which have been previously proposed for AADH. Comparison of the 15N-NMR spectra of the aminoquinol TTQ intermediates of AADH and methylamine dehydrogenase (MADH) revealed that the substrate-derived aminoquinol N of AADH and MADH exhibited distinct 15N chemical shifts which are separated by approx. 7 p.p.m. In each case, the signal for the substrate-derived aminoquinol N appears optimally with short pulse delay and exhibits a relaxation time and chemical shift which are consistent with 15N covalently bound to an aromatic ring (i.e. aminoquinol) which is attached to a rigid protein matrix. The aminoquinol of AADH is less stable against reoxidation than that of MADH. These data suggest that differences in the active-site mediated electrostatic environments of the aminoquinol N in the respective enzymes may influence both the observed 15N chemical shift and the relative reactivities of the TTQ aminoquinols towards oxygen. These data also demonstrate the utility of 13C- and 15N-NMR spectroscopy as a tool for monitoring the intermediates and products of enzyme-catalysed transformations. | lld:pubmed |
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| pubmed-article:9494080 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9494080 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9494080 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9494080 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9494080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9494080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9494080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9494080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9494080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9494080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9494080 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9494080 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9494080 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:9494080 | pubmed:author | pubmed-author:BishopG RGR | lld:pubmed |
| pubmed-article:9494080 | pubmed:author | pubmed-author:ZhuZZ | lld:pubmed |
| pubmed-article:9494080 | pubmed:author | pubmed-author:DavidsonV LVL | lld:pubmed |
| pubmed-article:9494080 | pubmed:author | pubmed-author:HicksR PRP | lld:pubmed |
| pubmed-article:9494080 | pubmed:author | pubmed-author:WhiteheadT... | lld:pubmed |
| pubmed-article:9494080 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9494080 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9494080 | pubmed:volume | 330 ( Pt 3) | lld:pubmed |
| pubmed-article:9494080 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9494080 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9494080 | pubmed:pagination | 1159-63 | lld:pubmed |
| pubmed-article:9494080 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:9494080 | pubmed:meshHeading | pubmed-meshheading:9494080-... | lld:pubmed |
| pubmed-article:9494080 | pubmed:meshHeading | pubmed-meshheading:9494080-... | lld:pubmed |
| pubmed-article:9494080 | pubmed:meshHeading | pubmed-meshheading:9494080-... | lld:pubmed |
| pubmed-article:9494080 | pubmed:meshHeading | pubmed-meshheading:9494080-... | lld:pubmed |
| pubmed-article:9494080 | pubmed:meshHeading | pubmed-meshheading:9494080-... | lld:pubmed |
| pubmed-article:9494080 | pubmed:meshHeading | pubmed-meshheading:9494080-... | lld:pubmed |
| pubmed-article:9494080 | pubmed:meshHeading | pubmed-meshheading:9494080-... | lld:pubmed |
| pubmed-article:9494080 | pubmed:meshHeading | pubmed-meshheading:9494080-... | lld:pubmed |
| pubmed-article:9494080 | pubmed:meshHeading | pubmed-meshheading:9494080-... | lld:pubmed |
| pubmed-article:9494080 | pubmed:meshHeading | pubmed-meshheading:9494080-... | lld:pubmed |
| pubmed-article:9494080 | pubmed:meshHeading | pubmed-meshheading:9494080-... | lld:pubmed |
| pubmed-article:9494080 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9494080 | pubmed:articleTitle | Identification of reaction products and intermediates of aromatic-amine dehydrogenase by 15N and 13C NMR. | lld:pubmed |
| pubmed-article:9494080 | pubmed:affiliation | Department of Biochemistry, University of Mississippi Medical Center, Jackson, MS 39216-4505, USA. | lld:pubmed |
| pubmed-article:9494080 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9494080 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9494080 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:9494080 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
