2.3.1.101: formylmethanofuran-tetrahydromethanopterin N-formyltransferase

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For detailed information about formylmethanofuran-tetrahydromethanopterin N-formyltransferase, go to the full flat file.

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 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.101 formylmethanofuran-tetrahydromethanopterin N-formyltransferase

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Results	in table
2	Activating Compound
2300	AA Sequence
1	CAS Registry Number
8	Cloned(Commentary)
5	Crystallization (Commentary)
5	General Information
4	General Stability
24	KM Value [mM]
17	Metals/Ions
15	Molecular Weight [Da]
12	Natural Substrates/ Products (Substrates)
4	Organic Solvent Stability
61	Organism
5	Oxidation Stability
9	Pathway
28	PDB ID
9	pH Optimum
1	pI Value
11	Purification (Commentary)
11	Reaction
1	Reaction Type
38	Reference
4	Source Tissue
12	Specific Activity [micromol/min/mg]
1	Storage Stability
38	Substrates and Products (Substrate)
28	Subunits
14	Synonyms
1	Systematic Name
13	Temperature Optimum [°C]
1	Temperature Range [°C]
15	Temperature Stability [°C]
2	Turnover Number [1/s]

Activating Compound

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Activating Compound on EC 2.3.1.101 - formylmethanofuran-tetrahydromethanopterin N-formyltransferase

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2,3-diphosphoglycerate

Methanopyrus kandleri

-

the 1 M 2,3-diphosphoglycerate the enzyme is highly active

726828

potassium cyclic 2,3-diphosphoglycerate

Methanopyrus kandleri

-

required for activity at 1 M, can be substituted by other salts with strongly hydrated anions, especially by K+, the enzyme is inactive and thermolabile, and changes the oligomerization state at low salt concentrations

661043