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1 ons and for the biosynthesis of methanogenic coenzyme B.
2 he essential Co-C bond of adenosylcobalamin (coenzyme B 12) by transferring the adenosyl group from c
5 step in the conversion of vitamin B(12) into coenzyme B(12) (adenosylcobalamin, AdoCbl) is catalyzed
6 To fully understand radical generation in coenzyme B(12) (dAdoCbl)-dependent enzymes, however, maj
10 ine kinase used for the de novo synthesis of coenzyme B(12) and the assimilation of cobyric acid (Cby
11 ine kinase used for the de novo synthesis of coenzyme B(12) and the assimilation of cobyric acid.
12 EAL) enzyme (encoded by the eutBC genes) and coenzyme B(12) are necessary and sufficient to grow on e
16 The catalytic power of enzymes containing coenzyme B(12) cofactor has been, in some respects, the
17 X mutants were impaired for the synthesis of coenzyme B(12) de novo and from Cby, but not from cobina
19 of the reactive cobalt-carbon bond found in coenzyme B(12) or 5'-deoxyadenosylcobalamin (AdoCbl), wh
20 this study, we demonstrate that delivery of coenzyme B(12) or 5'-deoxyadenosylcobalamin by adenosylt
21 The existence of a pathway for salvaging the coenzyme B(12) precursor dicyanocobinamide (Cbi) from th
22 obA(Mm) here) was cloned and used to restore coenzyme B(12) synthesis in a Salmonella enterica strain
24 hin the dead time of the instrument whenever coenzyme B(12) was preincubated with enzyme prior to mix
25 tional enzyme involved in adenosylcobalamin (coenzyme B(12)) biosynthesis in Salmonella typhimurium L
27 ser photolysis of adenosylcobalamin (AdoCbl; coenzyme B(12)) in AdoCbl-dependent ethanolamine ammonia
30 arge and complex, such as adenosylcobalamin (coenzyme B(12)), simpler, such as S-adenosylmethionine a
31 rs the product, adenosylcobalamin (AdoCbl or coenzyme B(12)), to methylmalonyl-CoA mutase (MCM), resu
32 the adenosylcobalamin (AdoCbl, also known as coenzyme B(12))-dependent diol dehydratase model reactio
33 omutase (OAM), an adenosylcobalamin (AdoCbl; coenzyme B(12))-dependent isomerase, employs a large-sca
37 d in the concentration of 1,2-propanediol or coenzyme B(12), but are consistent with the hypothesis t
39 , Klebsiella cysG mutants fail to synthesize coenzyme B(12), suggesting that the alternative siroheme
40 radical pair catalytic intermediate state in coenzyme B(12)- (adenosylcobalamin-) dependent ethanolam
41 uses a bacterial microcompartment (MCP) for coenzyme B(12)-dependent 1,2-propanediol (1,2-PD) utiliz
42 siological role of this enzyme is to support coenzyme B(12)-dependent 1,2-propanediol degradation, an
43 rmation of polyhedral organelles involved in coenzyme B(12)-dependent 1,2-propanediol degradation.
44 rica forms polyhedral organelles involved in coenzyme B(12)-dependent 1,2-propanediol degradation.
46 yphimurium LT2 contains genes needed for the coenzyme B(12)-dependent catabolism of 1,2-propanediol.
48 subunit (PduD) is required for packaging the coenzyme B(12)-dependent diol dehydratase (PduCDE) into
49 onsist of a proteinaceous shell that encases coenzyme B(12)-dependent diol dehydratase and perhaps ot
51 mon first step in the reactions catalyzed by coenzyme B(12)-dependent enzymes is cleavage of the coba
54 enterica forms polyhedral organelles during coenzyme B(12)-dependent growth on 1,2-propanediol (1,2-
55 onyl-CoA mutase is a member of the family of coenzyme B(12)-dependent isomerases and catalyzes the 1,
63 a-ketosuberate, a precursor to the coenzymes coenzyme B (7-mercapto heptanoylthreonine phosphate) and
64 enzyme M (2-mercaptoethanesulfonic acid) and coenzyme B (7-mercaptoheptanoylthreonine phosphate) play
66 es the final step of methanogenesis in which coenzyme B and methyl-coenzyme M are converted to methan
67 to form 7-oxoheptanoic acid, a precursor to coenzyme B, and an oxidative decarboxylation to form pim
70 CH3-S-CH2CH2-SO3(-), Me-S-CoM) and the thiol coenzyme B (CoB-SH) as substrates and converts them reve
72 uction of methyl-coenzyme M (methyl-SCoM) by coenzyme B (CoBSH) to methane and a heterodisulfide (CoB
74 tudies have revealed two distinct classes of Coenzyme B-Coenzyme M heterodisulfide (CoB-S-S-CoM) redu
78 duction of methyl-coenzyme M (CH3-S-CoM) and coenzyme B (HS-CoB) to methane and heterodisulfide CoM-S
79 ubstrate of MCR in an ionic reaction that is coenzyme B-independent and leads to debromination of BPS
80 thanesulfonate, methyl-SCoM) is reduced with coenzyme B (N-(7-mercaptoheptanoyl)threonine phosphate,
81 HDR catalyzes the two-electron reduction of coenzyme B-S-S-coenzyme M (CoB-S-S-CoM), the heterodisul
82 lized for the biosynthesis of coenzyme M and coenzyme B, the sulfur-containing cofactors required for
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