Probing nitrogen-sensitive steps in the free-radical-mediated deamination of amino alcohols by ethanolamine ammonia-lyase. Publishing Authors By Initials
Probing nitrogen-sensitive steps in the free-radical-mediated deamination of amino alcohols by ethanolamine ammonia-lyase. Journal Published:
PUBLICATION TYPE: Research Support, N.I.H., Extr
Journal: Journal of the American Chemical Society
VOLUME: 128
Page Numbers: 7120-1
Journal Abbreviation: J. Am. Chem. Soc.
ISSN: 0002-7863
DAY: 7
MONTH: Jun
YEAR: 2006
Probing nitrogen-sensitive steps in the free-radical-mediated deamination of amino alcohols by ethanolamine ammonia-lyase. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 7503056
Probing nitrogen-sensitive steps in the free-radical-mediated deamination of amino alcohols by ethanolamine ammonia-lyase. Keywords Mesh Terms:
KEYWORDS: Substrate Specificity
MESH TERMS: genetics
Chemical & Substance for Abstract: Probing nitrogen-sensitive steps in the free-radical-mediated deamination of amino alcohols by ethanolamine ammonia-lyase. Information
Substance Name: Ethanolamine Ammonia-Lyase
Registry Number: EC 4.3.1.7
Grant and Affiliation Information for Probing nitrogen-sensitive steps in the free-radical-mediated deamination of amino alcohols by ethanolamine ammonia-lyase.
AFFILIATION: Department of Biochemistry, Enzyme Institute, University of Wisconsin, 1710 University Avenue, Madison, Wisconsin 53726, USA.
Country: United States
AGENCY: United States NIGMS
GRANT: GM35752
ACRONYM: GM
MEDLINETA: J Am Chem Soc
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