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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1998-5-21
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494080-1409575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494080-1850627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494080-2028257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494080-2111581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494080-2126329,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494080-2885317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494080-3651442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494080-7827040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494080-8188594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494080-8448129,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494080-8688089
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
330 ( Pt 3)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1159-63
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9494080-Alcaligenes,
pubmed-meshheading:9494080-Carbon Isotopes,
pubmed-meshheading:9494080-Catalysis,
pubmed-meshheading:9494080-Enzyme Stability,
pubmed-meshheading:9494080-Fourier Analysis,
pubmed-meshheading:9494080-Kinetics,
pubmed-meshheading:9494080-Methylamines,
pubmed-meshheading:9494080-Nitrogen Isotopes,
pubmed-meshheading:9494080-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:9494080-Oxidation-Reduction,
pubmed-meshheading:9494080-Oxidoreductases Acting on CH-NH Group Donors
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pubmed:year |
1998
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pubmed:articleTitle |
Identification of reaction products and intermediates of aromatic-amine dehydrogenase by 15N and 13C NMR.
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pubmed:affiliation |
Department of Biochemistry, University of Mississippi Medical Center, Jackson, MS 39216-4505, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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