3.5.4.27: methenyltetrahydromethanopterin cyclohydrolase
This is an abbreviated version!
For detailed information about methenyltetrahydromethanopterin cyclohydrolase, go to the full flat file.
Word Map on EC 3.5.4.27
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3.5.4.27
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methanobacterium
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thermoautotrophicum
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archaea
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methane
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formyltransferase
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methanogenic
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formylmethanofuran
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methanogenesis
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methylenetetrahydromethanopterin
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formylmethanofuran:tetrahydromethanopterin
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dioxide
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kandleri
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methanosarcina
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methanopyrus
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methanotrophic
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donnelly
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marburg
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wolfe
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lyotropic
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monoxide
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hyperthermophilic
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barkeri
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archaeoglobus
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consortia
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tetrahydrofolate
- 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
Reaction
Synonyms
5,10-methenyltetrahydromethanopterin cyclohydrolase, CBH37751, cyclohydrolase, hydrolase, methenyltetrahydromethanopterin cyclo-, Mch, methenyl-H4MPT cyclohydrolase, methenyl-H4MPT+ cyclohydrolase, methenyltetrahydromethanopterin cyclohydrolase, N5,N10-methenyltetrahydromethanopterin cyclohydrolase
ECTree
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Temperature Stability
Temperature Stability on EC 3.5.4.27 - methenyltetrahydromethanopterin cyclohydrolase
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60
90
additional information
60
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10 min, 50% loss of activity in absence of salts. Stable for 25 min in presence of salt, 1 M K2HPO4
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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
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in 0.75 M 2,3-diphosphoglycerate, the cyclohydrolase is completely stable at pH 8.0 and 90°C
90
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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
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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
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salts increase heat stability of the enzyme