2.3.1.101: formylmethanofuran-tetrahydromethanopterin N-formyltransferase
This is an abbreviated version!
For detailed information about formylmethanofuran-tetrahydromethanopterin N-formyltransferase, go to the full flat file.
Word Map on EC 2.3.1.101
-
2.3.1.101
-
glycinamide
-
methionyl-trnafmet
-
kandleri
-
methanopyrus
-
transformylase
-
folate-dependent
-
aminoimidazole
-
aminoimidazolecarboxamide
-
garft
-
monoglutamate
-
2.1.2.3
-
aicarft
-
5,10-dideazatetrahydrofolate
- 2.3.1.101
- glycinamide
- methionyl-trnafmet
- kandleri
-
methanopyrus
-
transformylase
-
folate-dependent
-
aminoimidazole
-
aminoimidazolecarboxamide
- garft
-
monoglutamate
-
2.1.2.3
- aicarft
- 5,10-dideazatetrahydrofolate
Reaction
Synonyms
CBH38579, formylmethanofuran: tetrahydromethanopterin formyltransferase, formylmethanofuran:5,6,7,8-tetrahydromethanopterin N5-formyltransferase, formylmethanofuran:tetrahydromethanopterin formyltransferase, formyltransferase, formyltransferase, formylmethanofuran-tetrahydromethanopterin, formyltransferase/hydrolase complex, FTR, N-formylmethanofuran(CHO-MFR):tetrahydromethanopterin(H4MPT) formyltransferase
ECTree
2.3.1.101 formylmethanofuran-tetrahydromethanopterin N-formyltransferaseAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 2.3.1.101 - formylmethanofuran-tetrahydromethanopterin N-formyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
130
-
up to, in the presence of high lyotropic salt concentrations, mechanism of salt-dependent thermoadaption
70
up to, in presence of 1.5 M K2HPO4, hyperthermophilic enzyme
80
90
additional information
80
50% inactivation after 20 min at 0.005 M K3PO4. No inactivation after 20 min at 0.05 M K3PO4
80
50% inactivation after 20 min at 1.2 M K3PO4. No inactivation after 20 min at 1.5 M K3PO4
80
50% inactivation after 20 min at 0.05 M K3PO4. No inactivation after 20 min at 0.5 M K3PO4
90
-
30 min, wild-type enzyme, loss of 70% activity at 0.8-1.0 M potassium phosphate
90
-
in 0.5 M 2,3-diphosphoglycerate, the cyclohydrolase is completely stable at pH 8.0 and 90°C.
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
