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1 ide requires the intermediate methylation of coenzyme M.
2 ect to methylcobalamin, but competitive with coenzyme M.
3  beta-ketothioether to form acetoacetate and coenzyme M.
4 B-dependent two-electron reduction of methyl-coenzyme M.
5  yielding the products acetoacetate and free coenzyme M.
6              Short-chain alkylsulfonates and coenzyme M (2-mercaptoethanesulfonate) were found to mod
7                                              Coenzyme M (2-mercaptoethanesulfonic acid) (CoM) plays a
8                        Among archaebacteria, coenzyme M (2-mercaptoethanesulfonic acid) and coenzyme
9 c euryarchaeon Methanococcus jannaschii uses coenzyme M (2-mercaptoethanesulfonic acid) as the termin
10                         In the present work, coenzyme M (2-mercaptoethanesulfonic acid), a compound p
11 l step of methane formation, in which methyl-coenzyme M (2-methylthioethanesulfonate, methyl-SCoM) is
12 e cleavage and carboxylation of 2-ketopropyl-coenzyme M [2-(2-ketopropylthio)ethanesulfonate; 2-KPC]
13 on is the fourth step in the biosynthesis of coenzyme M, a crucial cofactor in methanogenesis and ali
14                                 A variety of coenzyme M analogs were tested for activity and/or inhib
15 s generates methane and a heterodisulfide of coenzyme M and coenzyme B (CoM-S-S-CoB).
16 athways are utilized for the biosynthesis of coenzyme M and coenzyme B, the sulfur-containing cofacto
17 y to be involved in the biosynthesis of both coenzyme M and methanopterin.
18                                     Putative coenzyme M and Na(+) were identified inside or in a side
19 yzed S-methylation of 2-thioethanesulfonate (coenzyme M) and exhibited similar apparent Km values for
20 bond cleavage of the substrate, 2-ketopropyl-coenzyme M, and carboxylation of what is thought to be a
21 ical products of the reaction, acetoacetate, coenzyme M, and NADP, and reduction of the crystals with
22 age of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the keto
23 ethanogenesis in which coenzyme B and methyl-coenzyme M are converted to methane and the heterodisulf
24 e findings evince a newfound versatility for coenzyme M as a carrier and activator of alkyl groups lo
25 ase/carboxylase, highlighting the utility of coenzyme M as a carrier molecule in the pathway.
26 s methanofuran, tetrahydromethanopterin, and coenzyme M at different oxidation states.
27 ase (ComA), that catalyzes the first step in coenzyme M biosynthesis.
28 mA-catalyzed reaction, the first step in the coenzyme M biosynthetic pathway, likely proceeds via a M
29 The analysis of this structure and that of a coenzyme-M-bound form provides insights into the stabili
30 tase (MCR) catalyzes the formation of methyl-coenzyme M (CH(3)S-CH(2)CH(2)SO(3)) from methane.
31         MCR uses the methyl thioether methyl-coenzyme M (CH3-S-CH2CH2-SO3(-), Me-S-CoM) and the thiol
32 catalyzes the reversible reduction of methyl-coenzyme M (CH3-S-CoM) and coenzyme B (HS-CoB) to methan
33 s the key step in the process, namely methyl-coenzyme M (CH3-S-CoM) plus coenzyme B (HS-CoB) to metha
34                                        Ethyl-coenzyme M (CH3CH2-S-CH2CH2-SO3(-), Et-S-CoM) serves as
35 the two-electron reduction of coenzyme B-S-S-coenzyme M (CoB-S-S-CoM), the heterodisulfide product of
36                                              Coenzyme M (CoM) (2-mercaptoethanesulfonic acid) biosynt
37  with short-chain aliphatic alkenes requires coenzyme M (CoM) (2-mercaptoethanesulfonic acid), which
38 nesulfonate; 2-KPC] to form acetoacetate and coenzyme M (CoM) in the bacterial pathway of propylene m
39                                              Coenzyme M (CoM) is methylated during methanogenesis fro
40                  Mercaptoethane sulfonate or coenzyme M (CoM) is the smallest known organic cofactor
41 rown cells possessed DMS- and MMPA-dependent coenzyme M (CoM) methylation activities.
42   Reconstitution of trimethylamine-dependent coenzyme M (CoM) methylation was achieved with three pur
43 5-methyl-tetrahydrosarcinapterin (CH3-H4SPT):coenzyme M (CoM) methyltransferase, encoded by the mtr o
44 g the methyl-tetrahydromethanopterin (H4MPT):coenzyme M (CoM) methyltransferase-encoding operon (delt
45 at the homologs are strictly dimethylsulfide:coenzyme M (CoM) methyltransferases not involved in the
46 of these pathways is the reduction of methyl-coenzyme M (CoM) to methane catalyzed by methyl-CoM redu
47 n Mycobacterium strain JS60 and discovered a coenzyme M (CoM)-dependent enzyme activity in extracts f
48 opylene oxidation uses the atypical cofactor coenzyme M (CoM, 2-mercaptoethanesulfonate) as the nucle
49 olism, catalyzing the nucleophilic attack of coenzyme M (CoM, 2-mercaptoethanesulfonic acid) on epoxy
50 CoMT) catalyzes the nucleophilic addition of coenzyme M (CoM, 2-mercaptoethanesulfonic acid) to epoxy
51 at requires four enzymes, NADPH, NAD(+), and coenzyme M (CoM; 2-mercaptoethanesulfonate) and occurs w
52      This pathway uses the atypical cofactor coenzyme M (CoM; 2-mercaptoethanesulfonic acid) as the n
53                                              Coenzyme M (CoM; 2-mercaptoethanesulfonic acid) is the t
54 ng these reactions, termed (R)-hydroxypropyl-coenzyme M dehydrogenase (R-HPCDH) and (S)-hydroxypropyl
55 ehydrogenase (R-HPCDH) and (S)-hydroxypropyl-coenzyme M dehydrogenase (S-HPCDH), are NAD(+)-dependent
56 e (R-HPC) dehydrogenase, that is part of the coenzyme M-dependent pathway of alkene and epoxide metab
57 bsequently demethylated by MtbA to methylate coenzyme M during methanogenesis from dimethylamine.
58 lyze methylation of mercaptoethanesulfonate (coenzyme M) during methanogenesis have also been shown t
59                           Accordingly, ethyl-coenzyme M (ethyl-CoM) was identified as an intermediate
60 allized in the presence of (S)-hydroxypropyl-coenzyme M has been determined using X-ray diffraction m
61  revealed two distinct classes of Coenzyme B-Coenzyme M heterodisulfide (CoB-S-S-CoM) reductase (Hdr)
62 in chain-length than methane, a function for coenzyme M in a catabolic pathway of hydrocarbon oxidati
63 f hydrocarbon oxidation, and the presence of coenzyme M in the bacterial domain of the phylogenetic t
64 es the binding of the substrate 2-ketopropyl-coenzyme M induces a conformational change resulting in
65 s suggested an active site geometry in which coenzyme M is bound both by S-coordination to zinc, and
66  formation of biological methane from methyl-coenzyme M (Me-SCoM) and coenzyme B (CoBSH).
67 se reactions is involved in the formation of coenzyme M, methanopterin, coenzyme F(420), and methanof
68 kDa polypeptide and stimulated dimethylamine:coenzyme M methyl transfer 3.4-fold in a cell extract.
69 ecificity of MtbB1 and MtbC in dimethylamine:coenzyme M methyl transfer activity.
70 tsA and cob(I)alamin mediate dimethylsulfide:coenzyme M methyl transfer in the complete absence of Mt
71  replaced proteins involved in dimethylamine:coenzyme M methyl transfer indicated high specificity of
72 ent proteins of the resolved monomethylamine:coenzyme M methyl transfer reaction replaced proteins in
73 tein requirements for in vitro dimethylamine:coenzyme M methyl transfer.
74 MCR) catalyzes methane formation from methyl-coenzyme M (methyl-SCoM) and N-7-mercaptoheptanoylthreon
75 sis, catalyzes methane formation from methyl-coenzyme M (methyl-SCoM) and N-7-mercaptoheptanoylthreon
76  methane biogenesis: the reduction of methyl-coenzyme M (methyl-SCoM) by coenzyme B (CoBSH) to methan
77 ading to homolysis of the C-S bond of methyl-coenzyme M (methyl-SCoM) to generate a methyl radical, w
78 s the two-electron donor, MCR reduces methyl-coenzyme M (methyl-SCoM) to methane and the mixed disulf
79  of the genes encoding a recently discovered coenzyme M methylase in Methanosarcina barkeri were anal
80 member of the methyltransferase II family of coenzyme M methylases.
81 yl-tetrahydromethanopterin demethylation and coenzyme M methylation half-reactions structurally descr
82 sibility of zinc involvement in catalysis of coenzyme M methylation is considered.
83 into the membrane protein center and finally coenzyme M methylation while the generated loosely attac
84     An MtbB1:MtbC ratio of 1 was optimal for coenzyme M methylation with dimethylamine.
85        MtbA, a MtsA homolog participating in coenzyme M methylation with methylamines, was not inhibi
86  gels revealed an additional methylcobalamin:coenzyme M (methylcobalamin:CoM) methyltransferase prese
87 eristics of two isozymes of methylcobamide:- coenzyme M methyltransferase (MT2).
88 nal activities of isozymes of methylcobamide:coenzyme M methyltransferase (MT2-M and MT2-A) in the me
89 zed by N (5)-methyl-tetrahydromethanopterin: coenzyme M methyltransferase (MtrABCDEFGH), which couple
90  This reaction is catalyzed by a methylthiol:coenzyme M methyltransferase composed of two polypeptide
91 tent with a model for the native methylthiol:coenzyme M methyltransferase in which MtsA mediates the
92 ch copurified with MtbA, the methylcorrinoid:Coenzyme M methyltransferase specific for methanogenesis
93 of two polypeptides, MtsA (a methylcobalamin:coenzyme M methyltransferase) and MtsB (homologous to a
94            MtsA is an active methylcobalamin:coenzyme M methyltransferase, but also methylates cob(I)
95 o the "A" and "M" isozymes of methylcobamide:coenzyme M methyltransferases (methyltransferase II), in
96 and exhibited similar apparent Km values for coenzyme M of 35 microM (MT2-A) and 20 microM (MT2-M).
97                             The 2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC) enzyme is
98                                 2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC) is a bact
99                                 2-Ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC) is a memb
100                       The NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC) is the te
101                           NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC), an atypi
102                                   Ketopropyl-coenzyme M oxidoreductase/carboxylase belongs to a famil
103 s of the DSOR family, the NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase catalyzes the redu
104 ofactor disulfide intermediate of ketopropyl-coenzyme M oxidoreductase/carboxylase has been determine
105          The mixed disulfide of 2-ketopropyl-coenzyme M oxidoreductase/carboxylase was captured throu
106                                   Ketopropyl-coenzyme M oxidoreductase/carboxylase, a unique member o
107 ently demethylates MtsB-bound corrinoid with coenzyme M, possibly employing elements of the same meth
108 A) use enzymes homologous to MCR named alkyl-coenzyme M reductase (ACR).
109                  These enzymes, called alkyl-coenzyme M reductase (Acrs), are widespread in the envir
110                                       Methyl-coenzyme M reductase (MCR) catalyzes both the synthesis
111                                       Methyl-coenzyme M reductase (MCR) catalyzes methane formation f
112                                       Methyl-coenzyme M reductase (MCR) catalyzes the final and rate-
113                                       Methyl-coenzyme M reductase (MCR) catalyzes the final step in m
114                                       Methyl-coenzyme M reductase (MCR) catalyzes the final step of m
115                                       Methyl-coenzyme M reductase (MCR) catalyzes the formation of me
116                                       Methyl-coenzyme M reductase (MCR) catalyzes the formation of me
117                                       Methyl-coenzyme M reductase (MCR) catalyzes the key step in the
118                                       Methyl coenzyme M reductase (MCR) catalyzes the last step in th
119                                       Methyl-coenzyme M reductase (MCR) catalyzes the reversible redu
120                                       Methyl-coenzyme M reductase (MCR) catalyzes the terminal step i
121                                       Methyl-coenzyme M reductase (MCR) catalyzes the terminal step i
122                     The nickel enzyme methyl-coenzyme M reductase (MCR) catalyzes two important trans
123 lism, including those that encode the methyl-coenzyme M reductase (MCR) complex.
124 using methane monooxygenase (MMO) and methyl coenzyme M reductase (MCR) enzymes.
125                                       Methyl-coenzyme M reductase (MCR) from methanogenic archaea cat
126                                       Methyl-coenzyme M reductase (MCR) from methanogenic archaea cat
127                                       Methyl-coenzyme M reductase (MCR) from Methanothermobacter marb
128                                       Methyl-coenzyme M reductase (MCR) has been originally identifie
129 ry of the methanogenesis gene cluster methyl-coenzyme M reductase (Mcr) in the Bathyarchaeota, and th
130 rding to the well-accepted mechanism, methyl-coenzyme M reductase (MCR) involves Ni-mediated thiolate
131                                       Methyl-coenzyme M reductase (MCR) is a nickel tetrahydrocorphin
132                                       Methyl-coenzyme M reductase (MCR) is the key enzyme of methanog
133                            The enzyme methyl-coenzyme M reductase (MCR) plays an important role in me
134   A competition assay showed that the methyl coenzyme M reductase (mcr) promoter region DNA and the n
135 a homologous substrate for the enzyme methyl-coenzyme M reductase (MCR) resulting in the product etha
136                                       Methyl-coenzyme M reductase (MCR), found in strictly anaerobic
137 h archaeal methane/alkane metabolism, methyl-coenzyme M reductase (Mcr), in metagenome-assembled geno
138 the central enzyme in methanogenesis, methyl-coenzyme M reductase (MCR), in Methanosarcina acetivoran
139                                       Methyl-coenzyme M reductase (MCR), the key enzyme in methanogen
140 ple mcrA gene sequences, encoding for methyl-coenzyme M reductase (Mcr), the key methanogenic enzyme,
141 ectively, using the reversible enzyme methyl-coenzyme M reductase (Mcr).
142 acetyl coenzyme A synthase (ACS), and methyl coenzyme M reductase (MCR).
143 ments that 3-NOP specifically targets methyl-coenzyme M reductase (MCR).
144 ailable metagenomes for homologues of methyl-coenzyme M reductase complex (MCR), we have obtained ten
145 sis to produce energy and rely on the methyl-coenzyme M reductase complex (Mcr).
146 engineered archaeal strain to produce methyl-coenzyme M reductase from unculturable anaerobic methano
147 10-methenyl-H4MPT reductase (MTD) and methyl coenzyme M reductase I (MRI), respectively, were transcr
148  (methenyl-H4MPT) reductase (MTH) and methyl coenzyme M reductase II (MRII), respectively.
149 acterize the TfuA protein involved in methyl-coenzyme M reductase thioamidation and demonstrate that
150 clusters of multihaem cytochromes and methyl coenzyme M reductase).
151  Fsr protein is comparable to that of methyl-coenzyme M reductase, an enzyme essential for methanogen
152 genesis in methanogens is mediated by methyl-coenzyme M reductase, an enzyme that is also responsible
153 s that are necessary for a functional methyl-coenzyme M reductase, and all subunits were detected in
154 s that are necessary for a functional methyl-coenzyme M reductase, and all subunits were detected in
155 ated in the methylation of Arg-285 in methyl coenzyme M reductase, binds a methylcobalamin cofactor r
156 coding methanogenesis enzymes such as methyl-coenzyme M reductase, heterodisulfide reductases and hyd
157                                       Methyl-coenzyme M reductase, responsible for the biological pro
158                                       Methyl-coenzyme M reductase, the rate-limiting enzyme in methan
159                 Recent discoveries of methyl-coenzyme M reductase-encoding genes (mcr) in uncultured
160 and the function of heme proteins and methyl-coenzyme M reductase.
161 ic focus on archaea that use specific methyl coenzyme M reductases to activate their substrates.
162 by a second methyltransferase to form methyl-coenzyme M, the direct methane precursor.
163 metabolism from the nucleophilic addition of coenzyme M to (R)- and (S)-epoxypropane, respectively.
164 PCC catalyzes the conversion of 2-ketopropyl-coenzyme M to acetoacetate, which is used as a carbon so
165 ise the first enzyme for the biosynthesis of coenzyme M to be described.
166        Component I catalyzed the addition of coenzyme M to epoxypropane to form a beta-hydroxythioeth
167 is initiated by the nucleophilic addition of coenzyme M to the (R)- and (S)-enantiomers of epoxypropa
168                                  Epoxyalkane:coenzyme M transferase (EaCoMT) catalyzes the nucleophil
169 -carbon carriers tetrahydromethanopterin and coenzyme M via a vitamin B(12) derivative (cobamide) as
170 2-A, trimethylamine-dependent methylation of coenzyme M was observed at approximately 20% of the rate
171        Methyl transfer from dimethylamine to coenzyme M was reconstituted in vitro for the first time
172 ed reductive cleavage of the H(3)C-S bond in coenzyme M, yielding the transient CH(3) radical capable

 
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