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Information on EC 3.5.4.27 - methenyltetrahydromethanopterin cyclohydrolase
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EC Tree
3.5.4.27 methenyltetrahydromethanopterin cyclohydrolaseIUBMB Comments
Methanopterin is a pterin analogue. The enzyme is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum.
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Word Map
- 3.5.4.27
-
methanobacterium
- thermoautotrophicum
- archaea
- methane
-
formyltransferase
-
methanogenic
- formylmethanofuran
-
methanogenesis
- methylenetetrahydromethanopterin
-
formylmethanofuran:tetrahydromethanopterin
- dioxide
- kandleri
-
methanosarcina
-
methanopyrus
-
methanotrophic
-
donnelly
- marburg
-
wolfe
-
lyotropic
-
monoxide
-
hyperthermophilic
- barkeri
- archaeoglobus
-
consortia
- tetrahydrofolate
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
n5,n10-methenyltetrahydromethanopterin cyclohydrolase, methenyltetrahydromethanopterin cyclohydrolase, 5,10-methenyltetrahydromethanopterin cyclohydrolase, methenyl-h4mpt cyclohydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5,10-methenyltetrahydromethanopterin cyclohydrolase
-
-
-
-
hydrolase, methenyltetrahydromethanopterin cyclo-
-
-
-
-
Mch
methenyl-H4MPT cyclohydrolase
N5,N10-methenyltetrahydromethanopterin cyclohydrolase
methenyl-H4MPT cyclohydrolase
-
-
-
-
N5,N10-methenyltetrahydromethanopterin cyclohydrolase
-
-
-
-
N5,N10-methenyltetrahydromethanopterin cyclohydrolase
-
-
N5,N10-methenyltetrahydromethanopterin cyclohydrolase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = 5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of cyclic amidines
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
5,10-methenyltetrahydromethanopterin 10-hydrolase (decyclizing)
Methanopterin is a pterin analogue. The enzyme is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum.
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CAS REGISTRY NUMBER
COMMENTARY
99533-50-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
the active site is primarily built up by the segment 93:95, Arg183 and Glu186 that either interact with the catalytic water attacking 5,10-methenyl-5,6,7,8-tetrahydromethanopterin or with the formyl oxygen of 5-formyl-5,6,7,8-tetrahydromethanopterin. The catalytic function of the strictly conserved Arg183 and Glu186 is substantiated by the low enzymatic activities of the E186A, E186D, E186N, E186Q, R183A, R183Q, R183E, R183K, and R183E-E186Q variants. Glu186 most likely acts as a general base. Arg183 decisively influences the pKa value of Glu186 and the proposed catalytic water mainly by its positive charge. In addition, Glu186 appears to be also responsible for product specificity by donating a proton to the directly neighbored N10 tertiary amine of H4MPT. Thus, N10 becomes a better leaving group than N5 which implies the generation of 5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
enzyme residue Lys77 binds to the phosphate moiety of substrate moiety H4MPT
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
enzyme residue Lys77 binds to the phosphate moiety of substrate moiety H4MPT
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
r
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
?
-
in acetate-grown cells the cyclohydrolase level is lowered 2 to 3fold, in cultures growing on acetate supplemented with methanol or H2CO cyclohydrolase activity level increases 3 to 4fold
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
?
Methanosarcina barkeri Fusaro / DSM 804
-
in acetate-grown cells the cyclohydrolase level is lowered 2 to 3fold, in cultures growing on acetate supplemented with methanol or H2CO cyclohydrolase activity level increases 3 to 4fold
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
?
-
enzyme is involved in methanogenesis from CO2 and H2, which represents the energy metabolism
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
?
-
enzyme is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
?
-
the enzyme might have a catabolic function in the C1-unit metabolism
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
?
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
the enzyme might have a catabolic function in the C1-unit metabolism
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
r
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
r
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
Methanosarcina barkeri Fusaro / DSM 804
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
N10-formyl-5,6,7,8-tetrahydromethanopterin is the nonenzymatic reaction product
r
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
the methenyl derivative is favored over 5-formyltetrahydromethanopterin
-
r
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
-
-
-
r
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
-
-
-
r
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
substrate isolated and purified from Methanobacterium thermoautotrophicum, overview
-
-
r
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
-
-
-
r
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
-
-
-
r
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
-
-
-
r
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
-
-
-
r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
r
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
?
-
in acetate-grown cells the cyclohydrolase level is lowered 2 to 3fold, in cultures growing on acetate supplemented with methanol or H2CO cyclohydrolase activity level increases 3 to 4fold
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
?
Methanosarcina barkeri Fusaro / DSM 804
-
in acetate-grown cells the cyclohydrolase level is lowered 2 to 3fold, in cultures growing on acetate supplemented with methanol or H2CO cyclohydrolase activity level increases 3 to 4fold
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
?
-
enzyme is involved in methanogenesis from CO2 and H2, which represents the energy metabolism
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
?
-
enzyme is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
?
-
the enzyme might have a catabolic function in the C1-unit metabolism
-
-
?
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O
?
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
the enzyme might have a catabolic function in the C1-unit metabolism
-
-
?
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
-
-
-
r
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
-
-
-
r
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
-
-
-
r
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
-
-
-
r
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
-
-
-
r
formyl-tetrahydromethanopterin
methenyl-tetrahydromethanopterin + H2O
-
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
activity in cell extract is dependent on the presence of high concentrations of potassium phosphate. The activity in 1.0 M potassium phosphate buffer pH 7.6 is eightfold higher than that in 0.12 M potassium phosphate buffer pH 7.6
K2HPO4
K2SO4
KCl
Mg2+
Na2HPO4
-
maximal activation by 1.5 M K2HPO4, 1 M Na2HPO4 or 1 M Na2SO4
Na2SO4
NaCl
additional information
K2HPO4
-
maximal activation by 1.5 M K2HPO4, 1 M Na2HPO4, or 1 M Na2SO4
NaCl
-
presence of salts required, activity in absence of salts is only 15% of that in the presence of salts
additional information
-
lyotrophic salts at high concentrations above 1 M are required for enzyme activity, but not for stability, 200fold activation
additional information
-
lyotrophic salts at high concentrations above 1 M are required for enzyme activity, but not for stability, 4fold activation
additional information
-
lyotrophic salts at high concentrations above 1 M are required for enzyme activity, but not for stability, 65fold activation
additional information
-
lyotrophic salts at high concentrations above 1 M are required for enzyme activity, but not for stability, 2fold activation
additional information
-
lyotrophic salts at high concentrations above 1 M are required for enzyme activity, but not for stability, 7fold activation
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-diphosphoglycerate
-
the activity increases with increasing 2,3-diphosphoglycerate concentrations from 30 U/mg up to a specific activity of 7,500 U/mg. The maximal activity is reached at a 2,3-diphosphoglycerate concentration of 0.75 M. At higher concentrations, the activity decreases
cyclic 2,3-bisphosphoglycerate
-
optimally active at 0.75 M, about 7500 U/mg
-
2,3-bisphosphoglycerate
-
the potassium salts of 2,3-bisphosphoglycerate stimulates cyclohydrolase activity
phosphate
-
the potassium salts of phosphateglycerate stimulates cyclohydrolase activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
effect of salts on Km
-
0.025
5,10-methenyl-5,6,7,8-tetrahydromethanopterin
pH 7.6, 65°C, mutant enzyme R183E
0.026
5,10-methenyl-5,6,7,8-tetrahydromethanopterin
pH 7.6, 65°C, mutant enzyme E186A
0.043
5,10-methenyl-5,6,7,8-tetrahydromethanopterin
pH 7.6, 65°C, mutant enzyme R183A
0.043
5,10-methenyl-5,6,7,8-tetrahydromethanopterin
pH 7.6, 65°C, mutant enzyme R183K
0.043
5,10-methenyl-5,6,7,8-tetrahydromethanopterin
pH 7.6, 65°C, mutant enzyme R183Q
0.047
5,10-methenyl-5,6,7,8-tetrahydromethanopterin
pH 7.6, 65°C, mutant enzyme K94V
0.05
5,10-methenyl-5,6,7,8-tetrahydromethanopterin
pH 7.6, 65°C, mutant enzyme E186N
0.055
5,10-methenyl-5,6,7,8-tetrahydromethanopterin
pH 7.6, 65°C, wild-type enzyme
0.062
5,10-methenyl-5,6,7,8-tetrahydromethanopterin
pH 7.6, 65°C, mutant enzyme E186D
0.077
5,10-methenyl-5,6,7,8-tetrahydromethanopterin
pH 7.6, 65°C, mutant enzyme K94E
0.03
N5,N10-methenyl-5,6,7,8-tetrahydromethanopterin
-
recombinant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.6
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
65
85
additional information
additional information
-
optimal growth temperature of the organism is 85°C
additional information
-
optimal growth temperature of the organism is 98°C
additional information
-
optimal growth temperature of the organism is 37°C
additional information
-
optimal growth temperature of the organism is 65°C
additional information
-
optimal growth temperature of the organism is 83°C
additional information
-
optimal growth temperature of the organism is 30°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
30°C: about 75% of maximal activity, 70°C: about 55% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DSM7471, originally isolated from the solar saltern of Figueria da Foz, Portugal
UniProt
brenda
DSM7471, originally isolated from the solar saltern of Figueria da Foz, Portugal
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
optimal growth temperature is 85°C
brenda
additional information
-
optimal growth temperature is 65°C
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
several of the differentially expressed genes during long-term hyper- or hypo-salt stress are related to the unique energy-acquiring methanogenesis pathway in this organism, including the transmembrane protein MttP, cobalamin biosynthesis protein, methenyl-H4MPT cyclohydrolase and monomethylamine methyltransferase. The methenyl-H4MPT cyclohydrolase participates in the pathway of methyl-group oxidation for transferring methanogenesis substrates into biosynthesis substrates
metabolism
-
several of the differentially expressed genes during long-term hyper- or hypo-salt stress are related to the unique energy-acquiring methanogenesis pathway in this organism, including the transmembrane protein MttP, cobalamin biosynthesis protein, methenyl-H4MPT cyclohydrolase and monomethylamine methyltransferase. The methenyl-H4MPT cyclohydrolase participates in the pathway of methyl-group oxidation for transferring methanogenesis substrates into biosynthesis substrates
-
physiological function
the enzyme catalyzes a reaction in the one-carbon energy metabolism of methanogenic, methanotrophic, and sulfate-reducing archaea and of methylotrophic bacteria
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
physiological function
the enzyme is involved in the methanogenesis pathway of archaea as a C1 unit carrier
physiological function
-
in hyperthermophilic methanogens of the orders Methanobacteriales and Methanopyrales, the cyclic 2,3-bisphosphoglycerate (cDPG) concentration appears to correlate with the growth temperature optimum, the concentration being 1 M in Methanopyrus kandleri (98°C)
physiological function
-
the enzyme is involved in the methanogenesis pathway of archaea as a C1 unit carrier
-
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
-
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
-
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
-
Show AA Sequence and Transmembrane Helices (2899 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
34246
-
2 * 34246, sequence calculation, 2 * 41000, SDS-PAGE
39000
41000
41500
82000
41000
-
2 * 34246, sequence calculation, 2 * 41000, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
trimer
dimer
-
2 * 34246, sequence calculation, 2 * 41000, SDS-PAGE
dimer
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
2 * 33000, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method in an anaerobic tent with an atmosphere of 95% N2/5% H2 under low-intensity red light. X-ray structures of the substrate-free E186Q mutant enzyme, the enzyme:5,10-methenyl-5,6,7,8-tetrahydromethanopterin complex, and the E186Q mutant enzyme:5-formyl-5,6,7,8-tetrahydromethanopterin complex
crystal structure of apoenzyme is solved at 1.37 A resolution
purified recombinant enzyme, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E186A
Vmax is 0.035% of wild-type activity, Km for 5,10-methenyl-5,6,7,8-tetrahydromethanopterin is 2.1fold lower compared to wild-type value
E186D
Vmax is 0.56% of wild-type activity, Km for 5,10-methenyl-5,6,7,8-tetrahydromethanopterin is 1.1fold higher compared to wild-type value
E186N
Vmax is 0.1% of wild-type activity, Km for 5,10-methenyl-5,6,7,8-tetrahydromethanopterin is 1.1fold lower compared to wild-type value
K94E
Vmax is 86% of wild-type activity, Km for 5,10-methenyl-5,6,7,8-tetrahydromethanopterin is 1.4fold lower compared to wild-type value
K94V
Vmax is 41% of wild-type activity, Km for 5,10-methenyl-5,6,7,8-tetrahydromethanopterin is 1.2fold lower compared to wild-type value
R183a
Vmax is 0.07% of wild-type activity, Km for 5,10-methenyl-5,6,7,8-tetrahydromethanopterin is 1.3fold lower compared to wild-type value
R183E
Vmax is 0.01% of wild-type activity, Km for 5,10-methenyl-5,6,7,8-tetrahydromethanopterin is 2.2fold lower compared to wild-type value
R183K
Vmax is 15% of wild-type activity, Km for 5,10-methenyl-5,6,7,8-tetrahydromethanopterin is 1.3fold lower compared to wild-type value
R183Q
Vmax is 0.05% of wild-type activity, Km for 5,10-methenyl-5,6,7,8-tetrahydromethanopterin is 1.3fold lower compared to wild-type value
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
in 0.75 M 2,3-diphosphoglycerate, the cyclohydrolase is completely stable at pH 8.0 and 90°C
726828
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
90
additional information
60
-
10 min, 50% loss of activity in absence of salts. Stable for 25 min in presence of salt, 1 M K2HPO4
90
-
more than 80% loss of activity after 10 min without stabilizer, completely stable for more than 50 min with addition of 1.0 M K2HPO4
90
-
in 0.75 M 2,3-diphosphoglycerate, the cyclohydrolase is completely stable at pH 8.0 and 90°C
90
-
enzyme in 40 mM potassium phosphate, pH 8.0, 1 h, 8% activity remaining, with addition of 0.5 M cyclic 2,3-bisphosphoglycerate or 0.7 M bisphosphoglycerate or 1.5 M phosphate, 100% activity are remaining
additional information
-
at cyclic 2,3-diphosphoglycerate concentrations prevailing in the cells of Methanopyrus kandleri the enzyme is completely thermostable. At molar concentrations also the potassium salts of phosphate and of 2,3-bisphosphoglycerate, the biosynthetic precursor of cyclic 2,3-diphosphoglycerate confer thermostability to the enzymes
additional information
-
salts increase heat stability of the enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of K2HPO4 or other salts prevents inactivation, relatively low concentrations of the salt, below 0.1 mM, are required for the stabilization, potassium salts being more effective than ammonium and sodium salts, at concentrations above 0.5 M, which are required for maximal activity the thermostability decreases again
-
at cyclic 2,3-diphosphoglycerate concentrations prevailing in the cells of Methanopyrus kandleri the enzyme is completely thermostable. At molar concentrations also the potassium salts of phosphate and of 2,3-bisphosphoglycerate, the biosynthetic precursor of cyclic 2,3-diphosphoglycerate confer thermostability to the enzymes
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the purified enzyme is more resistant to inactivation by O2 than the enzyme in cell extract
the purified enzyme is more resistant to inactivation by O2 than the enzyme in cell extract
-
246739
the purified enzyme is more resistant to inactivation by O2 than the enzyme in cell extract
-
246741
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified native enzyme, 1.32 M KCl, 50 mM Tris-HCl, pH 7.0, under N2 atmosphere, several months without significaant loss of activity
-
-20°C, under N2, 50 mM Tris/HCl buffer, pH 7, containing 1.3 M KCl, no loss of activity for several months
-
-20°C, under N2, in 50 mM Tris/HCl, pH 7, containing 1.3 M KCl, stable for several months
-
0°C, both under anaeobic and aerobic conditions, the enzyme also loses very little activity within 24 h
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation and ion exchange chromatography, native enzyme over 600fold from cell supernatant by ammonium sulfate fractionation and two steps of ion exchange chromatography, purification requires anaerobic conditions, the enzyme is completely soluble at 80% saturated ammonium sulfate
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons to other enzymes of the methanogenesis pathway
expression in Escherichia coli
gene mch, DNA and amino acid sequence determination, overexpression in Escherichia coli strain BL21(DE3)
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
NaCl downregulates methenyl-H4MPT cyclohydrolase expression
NaCl downregulates methenyl-H4MPT cyclohydrolase expression
NaCl downregulates methenyl-H4MPT cyclohydrolase expression
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pomper, B.K.; Vorholt, J.A.; Chistoserdova, L.; Lidstrom, M.E.; Thauer, R.K.
A methenyl tetrahydromethanopterin cyclohydrolase and a methenyl tetrahydrofolate cyclohydrolase in Methylobacterium extorquens AM1
Eur. J. Biochem.
261
475-480
1999
Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
brenda
Donnelly, M.I.; Escalante-Semerena, J.C.; Rinehart, K.L.; Wolfe, R.S.
Methenyl-tetrahydromethanopterin cyclohydrolase in cell extracts of Methanobacterium
Arch. Biochem. Biophys.
242
430-439
1985
Methanothermobacter thermautotrophicus
brenda
Dimarco, A.A.; Donnelly, M.I.; Wolfe, R.S.
Purification and properties of the 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanobacterium thermoautotrophicum
J. Bacteriol.
168
1372-1377
1986
Methanothermobacter thermautotrophicus
brenda
te Boemmelstroet, B.W.; Hensgens, C.M.H.; Geerts, W.J.; Keltjens, J.T.; van der Drift, C.; Vogels, G.D.
Purification and properties of 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri
J. Bacteriol.
172
564-571
1990
Methanosarcina barkeri
brenda
Klein, A.R.; Breitung, J.; Linder, D.; Stetter, K.O.; Thauer, R.K.
N5,N10-Methenyltetrahydromethanopterin cyclohydrolase from the extremely thermophilic sulfate reducing Archaeoglobus fulgidus: comparison of its properties with those of the cyclohydrolase from the extremely thermophilic Methanopyrus kandleri
Arch. Microbiol.
159
213-219
1993
Archaeoglobus fulgidus, Methanopyrus kandleri
brenda
Breitung, J.; Schmitz, R.A.; Stetter, K.O.; Thauer, R.K.
N5,N10-Methenyltetrahydromethanopterin cyclohydrolase from the extreme thermophile Methanopyrus kandleri: increase of the catalytic efficiency (kcat/KM) and thermostability in the presence of salts
Arch. Microbiol.
156
517-524
1991
Methanopyrus kandleri
-
brenda
Grabarse, W.; Vaupel, M.; Vorholt, J.A.; Shima, S.; Thauer, R.K.; Wittershagen, A.; Bourenkov, G.; Bartunik, H.D.; Ermler, U.
The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri
Structure Fold. Des.
7
1257-1268
1999
Methanopyrus kandleri
brenda
Vaupel, M.; Vorholt, J.A.; Thauer, R.K.
Overproduction and one-step purification of the N5,N10-methenyltetrahydromethanopterin cyclohydrolase (Mch) from the hyperthermophilic Methanopyrus kandleri
Extremophiles
2
15-22
1998
Methanosarcina barkeri, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Methanopyrus kandleri
brenda
Vorholt, J.A.; Christoserdova, L.; Stolyar, S.M.; Thauer, R.K.; Lidstrom, M.E.
Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolase
J. Bacteriol.
181
5750-5757
1999
Xanthobacter autotrophicus, Hyphomicrobium methylovorum, Methylobacillus flagellatus, Methylorubrum extorquens, Methylobacterium organophilum, Methylococcus thermophilus, Methylomicrobium album, Methylophilus methylotrophus, Methylosinus trichosporium, Xanthobacter flavus, Methylomonas rubra (Q9RPW2), Methylococcus capsulatus (Q9RPW8), Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1, Methylococcus capsulatus Bath (Q9RPW8), Methylophilus methylotrophus AS1, Methylomicrobium album BG8, Methylomonas rubra 15sh (Q9RPW2), Methylococcus thermophilus IIIp, Xanthobacter flavus H4-14
brenda
Mukhopadhyay, B.; Purwantini, E.; Daniels, L.
Effect of methanogenic substrates on coenzyme f420-dependent N5,N10-methylene-H4MPT dehydrogenase, N5,N10-methenyl-H4MPT cyclohydrolase and F420-reducing hydrogenase activities in Methanosarcina barkeri
Arch. Microbiol.
159
141-146
1993
Methanosarcina barkeri
-
brenda
Shima, S.; Thauer, R.K.
Tetrahydromethanopterin-specific enzymes from Methanopyrus kandleri
Methods Enzymol.
331
317-353
2001
Methanosarcina barkeri, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Methanopyrus kandleri, Methanothermus fervidus, Methylorubrum extorquens
brenda
Shih, C.J.; Lai, M.C.
Differentially expressed genes after hyper- and hypo-salt stress in the halophilic archaeon Methanohalophilus portucalensis
Can. J. Microbiol.
56
295-307
2010
Methanohalophilus portucalensis (A5JHE4), Methanohalophilus portucalensis, Methanohalophilus portucalensis FDF1 (A5JHE4)
brenda
Vornolt, J.; Kunow, J.; Stetter, K.; Thauer, R.
Enzymes and coenzymes of the carbon monoxide dehydrogenase pathway for autotrophic CO2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus
Arch. Microbiol.
163
112-118
1995
Archaeoglobus profundus, Archaeoglobus lithotrophicus, Archaeoglobus lithotrophicus TF-2, Archaeoglobus profundus DSM 5631
-
brenda
Vorholt, J.A.; Hafenbradl, D.; Stetter, K.O.; Thauer, R.K.
Pathways of autotrophic CO2 fixation and of dissimilatory nitrate reduction to N2O in Ferroglobus placidus
Arch. Microbiol.
167
19-23
1997
Ferroglobus placidus, Ferroglobus placidus DSM 10642
brenda
Upadhyay, V.; Demmer, U.; Warkentin, E.; Moll, J.; Shima, S.; Ermler, U.
Structure and catalytic mechanism of N5,N10-methenyl-tetrahydromethanopterin cyclohydrolase
Biochemistry
51
8435-8443
2012
Archaeoglobus fulgidus (O28344)
brenda
Shima, S.; Herault, D.A.; Berkessel, A.; Thauer, R.K.
Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri
Arch. Microbiol.
170
469-472
1998
Methanopyrus kandleri
brenda
Kojima, H.; Moll, J.; Kahnt, J.; Fukui, M.; Shima, S.
A reversed genetic approach reveals the coenzyme specificity and other catalytic properties of three enzymes putatively involved in anaerobic oxidation of methane with sulfate
Environ. Microbiol.
16
3431-3442
2014
uncultured archaeon (D1JGU3)
brenda
Carbone, V.; Schofield, L.R.; Beattie, A.K.; Sutherland-Smith, A.J.; Ronimus, R.S.
The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from Methanobrevibacter ruminantium
Proteins
81
2064-2070
2013
Methanobrevibacter ruminantium (D3E4S5), Methanobrevibacter ruminantium, Methanobrevibacter ruminantium DSM 1093 (D3E4S5)
brenda
Shima, S.; Herault, D.; Berkessel, A.; Thauer, R.
Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri
Arch. Microbiol.
170
469-472
1998
Methanopyrus kandleri
brenda
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