Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1982-12-2
|
pubmed:abstractText |
1. The reactions of the adenosylcobalamin-dependent enzyme, ethanolamine ammonia-lyase, with the 'good' and 'relatively poor' substrates 2-aminoethanol and (S)-2-aminopropanol respectively, under conditions of saturation with substrate were investigated by rapid freezing in conjunction with electron paramagnetic resonance (e.p.r.) spectroscopy and by stopped-flow spectrophotometry. 2. In disagreement with earlier reports [Babior et al. (1972) J. Biol. Chem. 247, 4389-4392], it was found that the reaction of 2-aminoethanol gave an e.p.r. signal observed in rapid freezing experiments characteristic of a coupled Co(II)-free radical system. This signal was similar to, though not identical with, that obtained with (S)-2-aminopropanol. The steady-state level of the signal with 2-aminoethanol as substrate was 0.56 of that attained with (S)-2-aminopropanol. 3. The results of these e.p.r. experiments were shown to be consistent with stopped-flow data obtained under closely similar reaction conditions, the latter indicating a corresponding ratio of 0.64. The results also are consistent with those of a rapid wavelength scanning, stopped-flow spectrophotometric study [Hollaway et al. (1978) Eur. J. Biochem. 82, 143-154].
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ammonia-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Cobalt,
http://linkedlifedata.com/resource/pubmed/chemical/Cobamides,
http://linkedlifedata.com/resource/pubmed/chemical/Ethanolamine Ammonia-Lyase,
http://linkedlifedata.com/resource/pubmed/chemical/cobamamide
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0014-2956
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
125
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
299-303
|
pubmed:dateRevised |
2008-11-21
|
pubmed:meshHeading |
pubmed-meshheading:6288372-Ammonia-Lyases,
pubmed-meshheading:6288372-Catalysis,
pubmed-meshheading:6288372-Chemical Phenomena,
pubmed-meshheading:6288372-Chemistry,
pubmed-meshheading:6288372-Cobalt,
pubmed-meshheading:6288372-Cobamides,
pubmed-meshheading:6288372-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:6288372-Ethanolamine Ammonia-Lyase,
pubmed-meshheading:6288372-Freezing,
pubmed-meshheading:6288372-Spectrophotometry,
pubmed-meshheading:6288372-Substrate Specificity
|
pubmed:year |
1982
|
pubmed:articleTitle |
The extents of formation of cobalt(II)-radical intermediates in the reactions with different substrates catalysed by the adenosylcobalamin-dependent enzyme ethanolamine ammonia-lyase.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|