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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
4 lyzed formation of the cobalt-carbon bond of coenzyme B 12.
5 nd position of cobalamin in the synthesis of coenzyme B 12.
6 step in the conversion of vitamin B(12) into coenzyme B(12) (adenosylcobalamin, AdoCbl) is catalyzed
7                                              Coenzyme B(12) (AdoCbl; 5'-deoxy-5'-adenosylcobalamin),
8    To fully understand radical generation in coenzyme B(12) (dAdoCbl)-dependent enzymes, however, maj
9 e biosynthesis of adenosylcobalamin (AdoCbl; coenzyme B(12) ).
10                           With 5'-deuterated coenzyme B(12) and deuterated substrate, the isotope eff
11 A ligase reaction and in the biosynthesis of coenzyme B(12) and phospholipids.
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
15 nt was impaired for the de novo synthesis of coenzyme B(12) as expected.
16 localized with genes for nickel-dependent or coenzyme B(12) biosynthesis enzymes.
17 cid, a bona fide intermediate of the de novo coenzyme B(12) biosynthetic route.
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
20                                              Coenzyme B(12) is used by two highly similar radical enz
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
25 irst L-threonine kinase shown to function in coenzyme B(12) synthesis.
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
29  the formation of adenosylcobalamin (AdoCbl, coenzyme B(12)) from cobalamin and ATP.
30 ser photolysis of adenosylcobalamin (AdoCbl; coenzyme B(12)) in AdoCbl-dependent ethanolamine ammonia
31 required for de novo synthesis of cobalamin (coenzyme B(12)) in S. enterica.
32           The cleavage of adenosylcobalamin (coenzyme B(12)) to form cob(II)alamin (B(12r)) with etha
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
37 ), a precursor of adenosylcobalamin (AdoCbl, coenzyme B(12)).
38 is required for de novo synthesis of AdoCbl (coenzyme B(12)).
39 ide (Cbi), a precursor of adenosylcobalamin (coenzyme B(12)).
40 d in the concentration of 1,2-propanediol or coenzyme B(12), but are consistent with the hypothesis t
41 thylbenzimidazole (DMB), the lower ligand of coenzyme B(12), has remained elusive.
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.
48                                              Coenzyme B(12)-dependent acyl-CoA mutases are radical en
49 yphimurium LT2 contains genes needed for the coenzyme B(12)-dependent catabolism of 1,2-propanediol.
50  barrel, combined with a Rossmann domain for coenzyme B(12)-dependent chemistry.
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
53 bacterium (BchE, EC 1.14.13.81), a predicted coenzyme B(12)-dependent enzyme.
54 mon first step in the reactions catalyzed by coenzyme B(12)-dependent enzymes is cleavage of the coba
55 ordinate for long-range radical migration in coenzyme B(12)-dependent enzymes.
56 erica grows on 1,2-propanediol (1,2-PD) in a coenzyme B(12)-dependent fashion.
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,
59 erica degrades 1,2-propanediol (1,2-PD) in a coenzyme B(12)-dependent manner.
60                                    CarH is a coenzyme B(12)-dependent photoreceptor involved in regul
61 tanding of the enzymology of the assembly of coenzyme B(12).
62 l step in the conversion of vitamin B(12) to coenzyme B(12).
63 t with the hydrogens in the C5' methylene of coenzyme B(12).
64 sizing 5'-deoxyadenosylcobalamin (AdoCbl) or coenzyme B(12).
65 s establishing an unprecedented mechanism of coenzyme B(6) dependent catalysis.
66 nversion beyond the common scope entailed by coenzyme B(6) dependent catalysts.
67                               This enzyme is coenzyme B(6)-dependent and its catalysis is initiated b
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
70 oheptanoic acid, a moiety of methanoarchaeal coenzyme B (7-mercaptoheptanylthreonine phosphate).
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
73 th of precursors in leucine, isoleucine, and coenzyme B biosyntheses.
74 r the 2-oxosuberate pathway for methanogenic coenzyme B biosynthesis.
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
77                                        Using coenzyme B (CoBSH) as the two-electron donor, MCR reduce
78 uction of methyl-coenzyme M (methyl-SCoM) by coenzyme B (CoBSH) to methane and a heterodisulfide (CoB
79 methane from methyl-coenzyme M (Me-SCoM) and coenzyme B (CoBSH).
80 tudies have revealed two distinct classes of Coenzyme B-Coenzyme M heterodisulfide (CoB-S-S-CoM) redu
81 hane and a heterodisulfide of coenzyme M and coenzyme B (CoM-S-S-CoB).
82                       Methane is produced by coenzyme B-dependent two-electron reduction of methyl-co
83 s, namely methyl-coenzyme M (CH3-S-CoM) plus coenzyme B (HS-CoB) to methane and CoM-S-S-CoB.
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