Literature summary extracted from
Van der Meijden, P.; te Brömmelstroet, B.W.; Poirot, C.M.; van der Drift, C.; Vogels, G.D.
Purification and properties of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri (1984), J. Bacteriol., 160, 629-635.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
2.1.1.90 |
ATP |
half-maximal activation at 0.16 mM ATP |
Methanosarcina barkeri |
|
2.1.1.90 |
additional information |
reductive activation by a mixture of H2, ferredoxin needed in the reductive activation process |
Methanosarcina barkeri |
|
2.1.1.90 |
additional information |
reductive activation by a mixture of H2, ferredoxin and hydrogenase but also by CO, ATP, GTP or CTP needed in the reductive activation process |
Methanosarcina barkeri |
|
General Stability
EC Number |
General Stability |
Organism |
---|
2.1.1.90 |
presence of divalent cations e.g. Mg2+, Mn2+, Sr2+, Ca2+ or Ba2+ are required for stability |
Methanosarcina barkeri |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.1.1.90 |
HgCl2 |
1 mM, 90% inhibition |
Methanosarcina barkeri |
|
2.1.1.90 |
Na2SO3 |
1 mM, 50% inhibition |
Methanosarcina barkeri |
|
2.1.1.90 |
NaNO2 |
0.1 mM, 90% inhibition |
Methanosarcina barkeri |
|
2.1.1.90 |
NH4Cl |
400 mM, 93% inhibition |
Methanosarcina barkeri |
|
2.1.1.90 |
O2 |
inactivation by O2 and other oxidizing agents |
Methanosarcina barkeri |
|
2.1.1.90 |
pyridoxal 5'-phosphate |
1 mM, 74% inhibition |
Methanosarcina barkeri |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.1.1.90 |
Ba2+ |
metal-free enzyme preparation has no activity, addition of Ba2+ restores 27% of the original activity |
Methanosarcina barkeri |
|
2.1.1.90 |
Ca2+ |
metal-free enzyme preparation has no activity, addition of Ca2+ restores 35% of the original activity |
Methanosarcina barkeri |
|
2.1.1.90 |
Co2+ |
metal-free enzyme preparation has no activity, addition of Co+ restores 46% of the original activity |
Methanosarcina barkeri |
|
2.1.1.90 |
Mg2+ |
metal-free enzyme preparation has no activity, addition of Mg2+ restores 66% of the original activity |
Methanosarcina barkeri |
|
2.1.1.90 |
Mn2+ |
metal-free enzyme preparation has no activity, addition of Mn2+ restores 27% of the original activity |
Methanosarcina barkeri |
|
2.1.1.90 |
Ni2+ |
metal-free enzyme preparation has no activity, addition of Ni2+ restores 21% of the original activity |
Methanosarcina barkeri |
|
2.1.1.90 |
Sr2+ |
metal-free enzyme preparation has no activity, addition of Sr2+ restores 20% of the original activity |
Methanosarcina barkeri |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
2.1.1.90 |
34000 |
- |
alpha2,beta, 2 * 34000 + 1 * 53000, SDS-PAGE in presence of 2-mercaptoethanol |
Methanosarcina barkeri |
2.1.1.90 |
53000 |
- |
alpha2,beta, 2 * 34000 + 1 * 53000, SDS-PAGE in presence of 2-mercaptoethanol |
Methanosarcina barkeri |
2.1.1.90 |
122000 |
- |
PAGE with different gel concentrations |
Methanosarcina barkeri |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.1.1.90 |
methanol + 5-hydroxybenzimidazolylcobamide |
Methanosarcina barkeri |
one of the enzymes responsible for the transmethylation from methanol to coenzyme M |
Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.1.1.90 |
Methanosarcina barkeri |
Q46EH3 |
- |
- |
Oxidation Stability
EC Number |
Oxidation Stability |
Organism |
---|
2.1.1.90 |
oxygen-sensitive |
Methanosarcina barkeri |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.1.1.90 |
- |
Methanosarcina barkeri |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.1.1.90 |
methanol + 5-hydroxybenzimidazolylcobamide |
- |
Methanosarcina barkeri |
Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O |
- |
? |
|
2.1.1.90 |
methanol + 5-hydroxybenzimidazolylcobamide |
one of the enzymes responsible for the transmethylation from methanol to coenzyme M |
Methanosarcina barkeri |
Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.1.1.90 |
trimer |
alpha2,beta, 2 * 34000 + 1 * 53000, SDS-PAGE in presence of 2-mercaptoethanol |
Methanosarcina barkeri |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
2.1.1.90 |
37 |
- |
assay at |
Methanosarcina barkeri |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
2.1.1.90 |
7.2 |
- |
assay at |
Methanosarcina barkeri |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
2.1.1.90 |
5-hydroxybenzimidazolylcobamide |
3-4 molecules bound, acting as methyl acceptor |
Methanosarcina barkeri |
|