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
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2.3.1.101
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glycinamide
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methionyl-trnafmet
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kandleri
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methanopyrus
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transformylase
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folate-dependent
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aminoimidazole
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aminoimidazolecarboxamide
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garft
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monoglutamate
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2.1.2.3
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aicarft
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5,10-dideazatetrahydrofolate
- 2.3.1.101
- glycinamide
- methionyl-trnafmet
- kandleri
-
methanopyrus
-
transformylase
-
folate-dependent
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aminoimidazole
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aminoimidazolecarboxamide
- garft
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monoglutamate
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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 (Subunits
Subunits on EC 2.3.1.101 - formylmethanofuran-tetrahydromethanopterin N-formyltransferase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
homotetramer
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composed of two dimers, each subunit is subdivided into two tightly associated lobes both consisting of a predominantly antiparallel beta sheet flanked by alpha helices forming an alpha/beta sandwich structure, amino acid composition
monomer
tetramer
additional information
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structure analysis, at low salt conditions the enzyme is in an equilibrium of dimer, trimer and tetramer, the latter being the active and most thermostable enzyme form, the dimer is also active, but the monomer is inactive
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Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
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enzyme is the 32000 Da subunit of enzyme complex
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dimer
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2 * 32000, crystal structure analysis, high potassium phosphate concentration of 1.0 M
dimer
dimer and tetramer are about 20% and about 80%, respectively, in 20100 mM potassium phosphate at pH 7.2. The ratio is independent of the buffer concentration. Oligomers larger than a tetramer can not be detected
dimer
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dimer and tetramer are about 20% and about 80%, respectively, in 20100 mM potassium phosphate at pH 7.2. The ratio is independent of the buffer concentration. Oligomers larger than a tetramer can not be detected
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monomer
monomer/dimer/tetramer equilibrium. Mostly in a monomeric state at a phosphate concentration of 100 mM and which tetramerizes only potassium phosphate concentrations above 400 mM
monomer
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monomer/dimer/tetramer equilibrium. Mostly in a monomeric state at a phosphate concentration of 100 mM and which tetramerizes only potassium phosphate concentrations above 400 mM
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tetramer
the enzyme already reveals a tetrameric state at salt concentrations below 0.1 M
tetramer
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4 * 32000, crystal structure analysis, high potassium phosphate concentration of 1.5 M
tetramer
dimer and tetramer are about 20% and about 80%, respectively, in 20100 mM potassium phosphate at pH 7.2. The ratio is independent of the buffer concentration. Oligomers larger than a tetramer can not be detected
tetramer
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dimer and tetramer are about 20% and about 80%, respectively, in 20100 mM potassium phosphate at pH 7.2. The ratio is independent of the buffer concentration. Oligomers larger than a tetramer can not be detected
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tetramer
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4 * 41000, SDS-PAGE before and after treatment with dimethylsuberimidate
