Information on EC 2.1.1.86 - tetrahydromethanopterin S-methyltransferase

for references in articles please use BRENDA:EC2.1.1.86
Word Map on EC 2.1.1.86
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Euryarchaeota

top print hide
EC NUMBER
COMMENTARY hide
2.1.1.86
-
top print hide
RECOMMENDED NAME
GeneOntology No.
tetrahydromethanopterin S-methyltransferase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in = 5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methanogenesis from H2 and CO2
-
-
methanogenesis from CO2
-
-
Methane metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
5-methyl-5,6,7,8-tetrahydromethanopterin:coenzyme-M 2-methyltransferase (Na+-transporting)
Involved in the formation of methane from CO2 in methanogenic archaea. The reaction involves the export of one or two sodium ions. The enzyme from the archaeon Methanobacterium thermoautotrophicum is a membrane-associated multienzyme complex composed of eight different subunits, and contains a 5'-hydroxybenzimidazolyl-cobamide prosthetic group, to which the methyl group is attached during the transfer. A soluble enzyme that is induced by the presence of CO has been reported as well [6].
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
103406-60-6
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
top print hide
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
CmtA is a soluble 5-methyl-5,6,7,8-tetrahydrosarcinapterin:coenzyme M methyltransferase postulated to supplement the membrane-bound 5-methyl-5,6,7,8-tetrahydromethanopterin:coenzyme M methyltransferase during CO-dependent growth of Methanosarcina acetivorans
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + H+
show the reaction diagram
-
-
-
-
r
5,6,7,8-tetrahydromethanopterin + methylcob(III)alamin
5-methyl-5,6,7,8-tetrahydromethanopterin + cob(III)alamin
show the reaction diagram
-
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
show the reaction diagram
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M
5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M
show the reaction diagram
-
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + H+
5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M
show the reaction diagram
-
-
-
-
r
5-methyl-5,6,7,8-tetrahydrosarcinapterin + coenzyme M
5,6,7,8-tetrahydrosarcinapterin + methyl-coenzyme M
show the reaction diagram
-
-
-
?
methylcobalamin + 2-mercaptoethanesulfonate
?
show the reaction diagram
N5-methyltetrahydrofolate + 2-mercaptoethanesulfonate
?
show the reaction diagram
top print hide
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + H+
show the reaction diagram
-
-
-
-
r
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
show the reaction diagram
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M
5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M
show the reaction diagram
Q8THX4
-
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + H+
5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M
show the reaction diagram
-
-
-
-
r
5-methyl-5,6,7,8-tetrahydrosarcinapterin + coenzyme M
5,6,7,8-tetrahydrosarcinapterin + methyl-coenzyme M
show the reaction diagram
Q8THX4
-
-
-
?
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
corrinoid
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
-
top print hide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
maximum activity at 1 mM Na+
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.7
(2-methylthio)ethanesulfonate
-
-
0.88
5,6,7,8-tetrahydromethanopterin
-
-
0.135
5-Methyl-5,6,7,8-tetrahydromethanopterin
at 37°C in 50 mM MOPS-KOH (pH 7.0)
0.277
coenzyme M
at 37°C in 50 mM MOPS-KOH (pH 7.0)
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.4
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
37°C, pH 6.9
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
-
top print hide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
-
sharp decrease in activity below pH 6.0 and above pH 7.0
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
assay at
top print hide
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
top print hide
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9000
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
12000
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
13000
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
20000
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
28000
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
34000
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
69000
x * 69000, SDS-PAGE
380000
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
non-denaturing gradient PAGE
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
during purification, the enzyme is stabilized with 0.01 mM hydroxocobalamin
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
top print hide
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen-sensitive
-
639489
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
all of these subunits are shown to be heterologously expressed in minicells of the Escherichia coli mutant DK6. Sequence comparisons with the methyltransferases of thermophilic and hypothermophilic methanogenic archaea
O59640 and P80655 and O59638 and P80653 and P80651 and P80654 and P80656 and P80650
expressed in Escherichia coli Rosetta (DE3) cells
top print hide
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTAmtr
-
mutants lacking H4MPT:coenzyme M methyltransferase-encoding operon (DELTAmtr), the methylene-H4MPT reductase encoding gene (DELTAmer), the methylene-H4MPT dehydrogenase-encoding gene (DELTAmtd), and the formyl-methanofuran: H4MPT formyl-transferase-encoding gene (DELTAftr) fail to grow using either methanol or H2/CO2 as a growth substrate, indicating that there is an absolute requirement for the C1 oxidation/reduction pathway for hydrogenotrophic and methylotrophic methanogenesis. Mutants also fail to grow on acetate. DELTAmtr and DELTAmer mutants are capable of producing methane from methanol. Thus, there is an Mtr/Mer bypass pathway that allows oxidation of methanol to the level of methylene-H4MPT in Methanosarcina barkeri. Formaldehyde may be an intermediate in this bypass. DELTAmer and DELTAmtr mutants are able to grow on a combination of methanol plus acetate
top
Show AA Sequence (1591 entries)
Please use the Sequence Search for a specific query.
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.86)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)