ライフサイエンスコーパス: coenzyme M

1 ect to methylcobalamin, but competitive with coenzyme M.

2 beta-ketothioether to form acetoacetate and coenzyme M.

3 B-dependent two-electron reduction of methyl-coenzyme M.

4 yielding the products acetoacetate and free coenzyme M.

5 ide requires the intermediate methylation of 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 yzed S-methylation of 2-thioethanesulfonate (coenzyme M) and exhibited similar apparent Km values for

19 bond cleavage of the substrate, 2-ketopropyl-coenzyme M, and carboxylation of what is thought to be a

20 ical products of the reaction, acetoacetate, coenzyme M, and NADP, and reduction of the crystals with

21 age of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the keto

22 ethanogenesis in which coenzyme B and methyl-coenzyme M are converted to methane and the heterodisulf

23 e findings evince a newfound versatility for coenzyme M as a carrier and activator of alkyl groups lo

24 ase/carboxylase, highlighting the utility of coenzyme M as a carrier molecule in the pathway.

25 ase (ComA), that catalyzes the first step in coenzyme M biosynthesis.

26 mA-catalyzed reaction, the first step in the coenzyme M biosynthetic pathway, likely proceeds via a M

27 The analysis of this structure and that of a coenzyme-M-bound form provides insights into the stabili

28 tase (MCR) catalyzes the formation of methyl-coenzyme M (CH(3)S-CH(2)CH(2)SO(3)) from methane.

29 MCR uses the methyl thioether methyl-coenzyme M (CH3-S-CH2CH2-SO3(-), Me-S-CoM) and the thiol

30 catalyzes the reversible reduction of methyl-coenzyme M (CH3-S-CoM) and coenzyme B (HS-CoB) to methan

31 s the key step in the process, namely methyl-coenzyme M (CH3-S-CoM) plus coenzyme B (HS-CoB) to metha

32 Ethyl-coenzyme M (CH3CH2-S-CH2CH2-SO3(-), Et-S-CoM) serves as

33 the two-electron reduction of coenzyme B-S-S-coenzyme M (CoB-S-S-CoM), the heterodisulfide product of

34 Coenzyme M (CoM) (2-mercaptoethanesulfonic acid) biosynt

35 with short-chain aliphatic alkenes requires coenzyme M (CoM) (2-mercaptoethanesulfonic acid), which

36 nesulfonate; 2-KPC] to form acetoacetate and coenzyme M (CoM) in the bacterial pathway of propylene m

37 Coenzyme M (CoM) is methylated during methanogenesis fro

38 rown cells possessed DMS- and MMPA-dependent coenzyme M (CoM) methylation activities.

39 Reconstitution of trimethylamine-dependent coenzyme M (CoM) methylation was achieved with three pur

40 5-methyl-tetrahydrosarcinapterin (CH3-H4SPT):coenzyme M (CoM) methyltransferase, encoded by the mtr o

41 g the methyl-tetrahydromethanopterin (H4MPT):coenzyme M (CoM) methyltransferase-encoding operon (delt

42 at the homologs are strictly dimethylsulfide:coenzyme M (CoM) methyltransferases not involved in the

43 of these pathways is the reduction of methyl-coenzyme M (CoM) to methane catalyzed by methyl-CoM redu

44 n Mycobacterium strain JS60 and discovered a coenzyme M (CoM)-dependent enzyme activity in extracts f

45 opylene oxidation uses the atypical cofactor coenzyme M (CoM, 2-mercaptoethanesulfonate) as the nucle

46 olism, catalyzing the nucleophilic attack of coenzyme M (CoM, 2-mercaptoethanesulfonic acid) on epoxy

47 CoMT) catalyzes the nucleophilic addition of coenzyme M (CoM, 2-mercaptoethanesulfonic acid) to epoxy

48 at requires four enzymes, NADPH, NAD(+), and coenzyme M (CoM; 2-mercaptoethanesulfonate) and occurs w

49 This pathway uses the atypical cofactor coenzyme M (CoM; 2-mercaptoethanesulfonic acid) as the n

50 Coenzyme M (CoM; 2-mercaptoethanesulfonic acid) is the t

51 ng these reactions, termed (R)-hydroxypropyl-coenzyme M dehydrogenase (R-HPCDH) and (S)-hydroxypropyl

52 ehydrogenase (R-HPCDH) and (S)-hydroxypropyl-coenzyme M dehydrogenase (S-HPCDH), are NAD(+)-dependent

53 e (R-HPC) dehydrogenase, that is part of the coenzyme M-dependent pathway of alkene and epoxide metab

54 bsequently demethylated by MtbA to methylate coenzyme M during methanogenesis from dimethylamine.

55 lyze methylation of mercaptoethanesulfonate (coenzyme M) during methanogenesis have also been shown t

56 allized in the presence of (S)-hydroxypropyl-coenzyme M has been determined using X-ray diffraction m

57 revealed two distinct classes of Coenzyme B-Coenzyme M heterodisulfide (CoB-S-S-CoM) reductase (Hdr)

58 in chain-length than methane, a function for coenzyme M in a catabolic pathway of hydrocarbon oxidati

59 f hydrocarbon oxidation, and the presence of coenzyme M in the bacterial domain of the phylogenetic t

60 es the binding of the substrate 2-ketopropyl-coenzyme M induces a conformational change resulting in

61 s suggested an active site geometry in which coenzyme M is bound both by S-coordination to zinc, and

62 formation of biological methane from methyl-coenzyme M (Me-SCoM) and coenzyme B (CoBSH).

63 se reactions is involved in the formation of coenzyme M, methanopterin, coenzyme F(420), and methanof

64 kDa polypeptide and stimulated dimethylamine:coenzyme M methyl transfer 3.4-fold in a cell extract.

65 ecificity of MtbB1 and MtbC in dimethylamine:coenzyme M methyl transfer activity.

66 tsA and cob(I)alamin mediate dimethylsulfide:coenzyme M methyl transfer in the complete absence of Mt

67 replaced proteins involved in dimethylamine:coenzyme M methyl transfer indicated high specificity of

68 ent proteins of the resolved monomethylamine:coenzyme M methyl transfer reaction replaced proteins in

69 tein requirements for in vitro dimethylamine:coenzyme M methyl transfer.

70 MCR) catalyzes methane formation from methyl-coenzyme M (methyl-SCoM) and N-7-mercaptoheptanoylthreon

71 sis, catalyzes methane formation from methyl-coenzyme M (methyl-SCoM) and N-7-mercaptoheptanoylthreon

72 methane biogenesis: the reduction of methyl-coenzyme M (methyl-SCoM) by coenzyme B (CoBSH) to methan

73 s the two-electron donor, MCR reduces methyl-coenzyme M (methyl-SCoM) to methane and the mixed disulf

74 of the genes encoding a recently discovered coenzyme M methylase in Methanosarcina barkeri were anal

75 member of the methyltransferase II family of coenzyme M methylases.

76 sibility of zinc involvement in catalysis of coenzyme M methylation is considered.

77 An MtbB1:MtbC ratio of 1 was optimal for coenzyme M methylation with dimethylamine.

78 MtbA, a MtsA homolog participating in coenzyme M methylation with methylamines, was not inhibi

79 gels revealed an additional methylcobalamin:coenzyme M (methylcobalamin:CoM) methyltransferase prese

80 eristics of two isozymes of methylcobamide:- coenzyme M methyltransferase (MT2).

81 nal activities of isozymes of methylcobamide:coenzyme M methyltransferase (MT2-M and MT2-A) in the me

82 This reaction is catalyzed by a methylthiol:coenzyme M methyltransferase composed of two polypeptide

83 tent with a model for the native methylthiol:coenzyme M methyltransferase in which MtsA mediates the

84 ch copurified with MtbA, the methylcorrinoid:Coenzyme M methyltransferase specific for methanogenesis

85 of two polypeptides, MtsA (a methylcobalamin:coenzyme M methyltransferase) and MtsB (homologous to a

86 MtsA is an active methylcobalamin:coenzyme M methyltransferase, but also methylates cob(I)

87 o the "A" and "M" isozymes of methylcobamide:coenzyme M methyltransferases (methyltransferase II), in

88 and exhibited similar apparent Km values for coenzyme M of 35 microM (MT2-A) and 20 microM (MT2-M).

89 The NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC) is the te

90 NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC), an atypi

91 Ketopropyl-coenzyme M oxidoreductase/carboxylase belongs to a famil

92 s of the DSOR family, the NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase catalyzes the redu

93 ofactor disulfide intermediate of ketopropyl-coenzyme M oxidoreductase/carboxylase has been determine

94 The mixed disulfide of 2-ketopropyl-coenzyme M oxidoreductase/carboxylase was captured throu

95 Ketopropyl-coenzyme M oxidoreductase/carboxylase, a unique member o

96 ently demethylates MtsB-bound corrinoid with coenzyme M, possibly employing elements of the same meth

97 Methyl-coenzyme M reductase (MCR) catalyzes methane formation f

98 Methyl-coenzyme M reductase (MCR) catalyzes the final and rate-

99 Methyl-coenzyme M reductase (MCR) catalyzes the final step in m

100 Methyl-coenzyme M reductase (MCR) catalyzes the final step of m

101 Methyl-coenzyme M reductase (MCR) catalyzes the formation of me

102 Methyl-coenzyme M reductase (MCR) catalyzes the key step in the

103 Methyl-coenzyme M reductase (MCR) catalyzes the reversible redu

104 Methyl-coenzyme M reductase (MCR) catalyzes the terminal step i

105 Methyl-coenzyme M reductase (MCR) catalyzes the terminal step i

106 The nickel enzyme methyl-coenzyme M reductase (MCR) catalyzes two important trans

107 lism, including those that encode the methyl-coenzyme M reductase (MCR) complex.

108 using methane monooxygenase (MMO) and methyl coenzyme M reductase (MCR) enzymes.

109 Methyl-coenzyme M reductase (MCR) from methanogenic archaea cat

110 Methyl-coenzyme M reductase (MCR) from methanogenic archaea cat

111 Methyl-coenzyme M reductase (MCR) from Methanothermobacter marb

112 Methyl-coenzyme M reductase (MCR) is a nickel tetrahydrocorphin

113 Methyl-coenzyme M reductase (MCR) is the key enzyme of methanog

114 A competition assay showed that the methyl coenzyme M reductase (mcr) promoter region DNA and the n

115 a homologous substrate for the enzyme methyl-coenzyme M reductase (MCR) resulting in the product etha

116 Methyl-coenzyme M reductase (MCR), found in strictly anaerobic

117 Methyl-coenzyme M reductase (MCR), the key enzyme in methanogen

118 ments that 3-NOP specifically targets methyl-coenzyme M reductase (MCR).

119 engineered archaeal strain to produce methyl-coenzyme M reductase from unculturable anaerobic methano

120 10-methenyl-H4MPT reductase (MTD) and methyl coenzyme M reductase I (MRI), respectively, were transcr

121 (methenyl-H4MPT) reductase (MTH) and methyl coenzyme M reductase II (MRII), respectively.

122 Fsr protein is comparable to that of methyl-coenzyme M reductase, an enzyme essential for methanogen

123 genesis in methanogens is mediated by methyl-coenzyme M reductase, an enzyme that is also responsible

124 Methyl-coenzyme M reductase, the rate-limiting enzyme in methan

125 and the function of heme proteins and methyl-coenzyme M reductase.

126 by a second methyltransferase to form methyl-coenzyme M, the direct methane precursor.

127 metabolism from the nucleophilic addition of coenzyme M to (R)- and (S)-epoxypropane, respectively.

128 ise the first enzyme for the biosynthesis of coenzyme M to be described.

129 Component I catalyzed the addition of coenzyme M to epoxypropane to form a beta-hydroxythioeth

130 is initiated by the nucleophilic addition of coenzyme M to the (R)- and (S)-enantiomers of epoxypropa

131 Epoxyalkane:coenzyme M transferase (EaCoMT) catalyzes the nucleophil

132 2-A, trimethylamine-dependent methylation of coenzyme M was observed at approximately 20% of the rate

133 Methyl transfer from dimethylamine to coenzyme M was reconstituted in vitro for the first time