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1 ons and for the biosynthesis of methanogenic coenzyme B.
2 drogen atom abstraction from the S-H bond in coenzyme B.
3 he essential Co-C bond of adenosylcobalamin (coenzyme B 12) by transferring the adenosyl group from c
6 step in the conversion of vitamin B(12) into coenzyme B(12) (adenosylcobalamin, AdoCbl) is catalyzed
8 To fully understand radical generation in coenzyme B(12) (dAdoCbl)-dependent enzymes, however, maj
12 ine kinase used for the de novo synthesis of coenzyme B(12) and the assimilation of cobyric acid (Cby
13 ine kinase used for the de novo synthesis of coenzyme B(12) and the assimilation of cobyric acid.
14 EAL) enzyme (encoded by the eutBC genes) and coenzyme B(12) are necessary and sufficient to grow on e
18 The catalytic power of enzymes containing coenzyme B(12) cofactor has been, in some respects, the
19 X mutants were impaired for the synthesis of coenzyme B(12) de novo and from Cby, but not from cobina
21 of the reactive cobalt-carbon bond found in coenzyme B(12) or 5'-deoxyadenosylcobalamin (AdoCbl), wh
22 this study, we demonstrate that delivery of coenzyme B(12) or 5'-deoxyadenosylcobalamin by adenosylt
23 The existence of a pathway for salvaging the coenzyme B(12) precursor dicyanocobinamide (Cbi) from th
24 obA(Mm) here) was cloned and used to restore coenzyme B(12) synthesis in a Salmonella enterica strain
26 hin the dead time of the instrument whenever coenzyme B(12) was preincubated with enzyme prior to mix
27 tional enzyme involved in adenosylcobalamin (coenzyme B(12)) biosynthesis in Salmonella typhimurium L
28 The discovery that adenosylcobalamin (or coenzyme B(12)) can act as a light-sensing chromophore h
30 ser photolysis of adenosylcobalamin (AdoCbl; coenzyme B(12)) in AdoCbl-dependent ethanolamine ammonia
33 arge and complex, such as adenosylcobalamin (coenzyme B(12)), simpler, such as S-adenosylmethionine a
34 rs the product, adenosylcobalamin (AdoCbl or coenzyme B(12)), to methylmalonyl-CoA mutase (MCM), resu
35 the adenosylcobalamin (AdoCbl, also known as coenzyme B(12))-dependent diol dehydratase model reactio
36 omutase (OAM), an adenosylcobalamin (AdoCbl; coenzyme B(12))-dependent isomerase, employs a large-sca
40 d in the concentration of 1,2-propanediol or coenzyme B(12), but are consistent with the hypothesis t
42 , Klebsiella cysG mutants fail to synthesize coenzyme B(12), suggesting that the alternative siroheme
43 radical pair catalytic intermediate state in coenzyme B(12)- (adenosylcobalamin-) dependent ethanolam
44 uses a bacterial microcompartment (MCP) for coenzyme B(12)-dependent 1,2-propanediol (1,2-PD) utiliz
45 siological role of this enzyme is to support coenzyme B(12)-dependent 1,2-propanediol degradation, an
46 rmation of polyhedral organelles involved in coenzyme B(12)-dependent 1,2-propanediol degradation.
47 rica forms polyhedral organelles involved in coenzyme B(12)-dependent 1,2-propanediol degradation.
49 yphimurium LT2 contains genes needed for the coenzyme B(12)-dependent catabolism of 1,2-propanediol.
51 subunit (PduD) is required for packaging the coenzyme B(12)-dependent diol dehydratase (PduCDE) into
52 onsist of a proteinaceous shell that encases coenzyme B(12)-dependent diol dehydratase and perhaps ot
54 mon first step in the reactions catalyzed by coenzyme B(12)-dependent enzymes is cleavage of the coba
57 enterica forms polyhedral organelles during coenzyme B(12)-dependent growth on 1,2-propanediol (1,2-
58 onyl-CoA mutase is a member of the family of coenzyme B(12)-dependent isomerases and catalyzes the 1,
68 a-ketosuberate, a precursor to the coenzymes coenzyme B (7-mercapto heptanoylthreonine phosphate) and
69 enzyme M (2-mercaptoethanesulfonic acid) and coenzyme B (7-mercaptoheptanoylthreonine phosphate) play
71 es the final step of methanogenesis in which coenzyme B and methyl-coenzyme M are converted to methan
72 to form 7-oxoheptanoic acid, a precursor to coenzyme B, and an oxidative decarboxylation to form pim
75 CH3-S-CH2CH2-SO3(-), Me-S-CoM) and the thiol coenzyme B (CoB-SH) as substrates and converts them reve
76 f methane by catalyzing the reaction between coenzymes B (CoBS-H) and M (H(3)C-SCoM), hosts in its co
78 uction of methyl-coenzyme M (methyl-SCoM) by coenzyme B (CoBSH) to methane and a heterodisulfide (CoB
80 tudies have revealed two distinct classes of Coenzyme B-Coenzyme M heterodisulfide (CoB-S-S-CoM) redu
84 duction of methyl-coenzyme M (CH3-S-CoM) and coenzyme B (HS-CoB) to methane and heterodisulfide CoM-S
85 adical, which abstracts a hydrogen atom from coenzyme B (HSCoB) to generate methane and the mixed dis
86 ubstrate of MCR in an ionic reaction that is coenzyme B-independent and leads to debromination of BPS
87 thanesulfonate, methyl-SCoM) is reduced with coenzyme B (N-(7-mercaptoheptanoyl)threonine phosphate,
88 HDR catalyzes the two-electron reduction of coenzyme B-S-S-coenzyme M (CoB-S-S-CoM), the heterodisul
89 lized for the biosynthesis of coenzyme M and coenzyme B, the sulfur-containing cofactors required for