Crystal structure of ethanolamine ammonia-lyase complexed with coenzyme B12 analog Adeninylpentylcobalamin and substrate

Content Provider	Semantic Scholar
Author	Shibata, Naoki
Copyright Year	2010
Abstract	Introduction Ethanolamine ammonia-lyase (EAL) catalyses the formation of acetaldehyde and ammonia from ethanolamine (EA) or of ammonia and propionaldehyde from 2-amino-1-propanol. The reaction is initiated by cleavage of the cobalt-carbon bond of adenosylcobalamin (AdoCbl) to form cob(II)alamin-5'-deoxyadenosyl radical pair. The 5'-deoxyadenosyl radical abstracts a hydrogen atom from the C1 carbon atom of the substrate to form a substrate radical, followed by the migration of an amino group from C2 to C1 of the substrate. AdoCbl-dependent enzymes accelerate the cleavage rate of the cobalt-carbon bond by >10 compared with AdoCbl in solution. EAL is composed of six pairs of α subunit (EutB protein, Mr = 49k) and β-subunit (EutC protein, Mr = 31k), and the total molecular weight reaches to ~480,000. The aim of the structural work of EAL is to investigate how the enzyme activates the cobalt-carbon bond of AdoCbl and catalyses the reaction by a radical mechanism.
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Language	English
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Resource Type	Article