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1 ferase (ACAT) enzymes convert vitamin B12 to coenzyme B12.
2 d CobC) that install DMB in the formation of coenzyme B12.
3 hes that respond to S-adenosylmethionine and coenzyme B12.
6 trate radical pair catalytic intermediate in coenzyme B12 (adenosylcobalamin)-dependent ethanolamine
7 decades of research, the mechanism by which coenzyme B12 (adenosylcobalamin, AdoCbl)-dependent enzym
8 erica degrades 1,2-propanediol (1,2-PD) in a coenzyme B12 (adenosylcobalamin, AdoCbl)-dependent fashi
9 2'-deoxynucleoside 5'-triphosphates and uses coenzyme B12, adenosylcobalamin (AdoCbl), as a cofactor.
10 the assimilation of dietary cobalamins into coenzyme B12 (Ado-B12), the required cofactor for MCM.
11 s essential for B12 biochemistry and renders coenzyme B12 (AdoCbl) so intriguingly suitable for enzym
12 CA) catalyzes the conversion of cobalamin to coenzyme B12, an essential cofactor in animal metabolism
13 lies outside the compartment, using external coenzyme B12 and injecting its product, acetaldehyde, in
14 l for human metabolism, the organocobalamins coenzyme B12 and methylcobalamin, are highly photolabile
15 m Aquincola tertiaricarbonis in complex with coenzyme B12 and the substrates (S)-3-hydroxybutyryl- an
16 lex of dioldehydrase with adenosylcobalamin (coenzyme B12) and potassium ion reacts with molecular ox
17 s motif confirms that the RNA directly binds coenzyme B12, and that it likely serves as a genetic con
18 ic aciduria, but the role of this protein in coenzyme B12 assimilation and/or utilization is not know
19 consists of an approximately 200 nucleotide, coenzyme B12 binding aptamer domain and an approximately
20 e of converting vitamin B12 derivatives into coenzyme B12 by catalyzing the thermodynamically challen
21 ns are fast enough for kinetic competence in coenzyme B12 dependent enzyme-catalyzed reactions of gly
23 studies reporting magnetic field effects on coenzyme B12-dependent ethanolamine ammonia lyase in vit
24 urium propanediol dehydratase was related to coenzyme B12-dependent glycerol dehydratases from Citrob
30 coli and Salmonella typhimurium each carry a coenzyme B12-dependent riboswitch that causes repressed
31 dent of the radical chemistry common to both coenzyme B12 enzymology and its known photochemistry.
33 The catalytic power of enzymes containing coenzyme B12 has been, in some respects, the "last basti
35 iosynthetic branch of the adenosylcobalamin (coenzyme B12) pathway of Salmonella enterica serovar Typ
37 RNase P from Escherichia coli cleaves the coenzyme B12 riboswitch from E. coli and a similar one f
38 eakly and not attached to the cobalt atom of coenzyme B12, rotated and shifted from its position in t
39 have examined the distribution of cobalamin (coenzyme B12) synthetic ability and cobalamin-dependent
41 which Perry Frey described as a "poor man's coenzyme B12," were believed to be relatively rare chemi
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