Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.1.101 - formylmethanofuran-tetrahydromethanopterin N-formyltransferase and Organism(s) Methanopyrus kandleri and UniProt Accession Q49610

for references in articles please use BRENDA:EC2.3.1.101
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Methanofuran is a complex 4-substituted furfurylamine and is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Methanopyrus kandleri
UNIPROT: Q49610
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Methanopyrus kandleri
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
formyltransferase, formylmethanofuran:tetrahydromethanopterin formyltransferase, formylmethanofuran tetrahydromethanopterin formyltransferase, formyltransferase/hydrolase complex, n-formylmethanofuran(cho-mfr):tetrahydromethanopterin(h4mpt) formyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
show the reaction diagram
ternary complex type mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
formylmethanofuran:5,6,7,8-tetrahydromethanopterin 5-formyltransferase
Methanofuran is a complex 4-substituted furfurylamine and is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum.
CAS REGISTRY NUMBER
COMMENTARY hide
105669-83-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
methanofuran + N5-formyl-5,6,7,8-tetrahydromethanopterin
show the reaction diagram
-
-
r
methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
show the reaction diagram
-
-
-
r
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
show the reaction diagram
-
-
-
-
?
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
methanofuran + N5-formyl-5,6,7,8-tetrahydromethanopterin
show the reaction diagram
N-furfurylformamide + 5,6,7,8-tetrahydromethanopterin
2-(aminomethyl)furane + N5-formyl-5,6,7,8-tetrahydromethanopterin
show the reaction diagram
-
pseudo-substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
methanofuran + N5-formyl-5,6,7,8-tetrahydromethanopterin
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K3PO4
1.0 M salt concentration is required for 50% activity at 89°C. 1.5 M salt concentration is required for 100% activity at 89°C
salts
optimal salt concentration for activity: 1.5-2.0 M
K+
-
potassium cyclic 2,3-diphosphoglycerate 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
K2HPO4
-
no activity in absence, assay mixture contains 2 M
potassium phosphate
-
required for activity at 1 M, can be substituted by other salts with strongly hydrated anions, especially by potassium cyclic 2,3-diphosphoglycerate, the enzyme is inactive and thermolabile, and changes the oligomerization state at low salt concentrations
salts
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-diphosphoglycerate
-
the 1 M 2,3-diphosphoglycerate the enzyme is highly active
potassium cyclic 2,3-diphosphoglycerate
-
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.107
5,6,7,8-tetrahydromethanopterin
0.04 - 0.05
formylmethanofuran
0.1
5,6,7,8-tetrahydromethanopterin
-
-
0.05
formylmethanofuran
-
-
20
N-Furfurylformamide
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
recombinant and wild-type enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
the hyperthermophilic methanogenic archaeon grows on H2 and CO2 as sole energy source best at 98°C
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
1 * 35000, SDS-PAGE
32000
35000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
dimer
-
2 * 32000, crystal structure analysis, high potassium phosphate concentration of 1.0 M
homotetramer
-
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
-
1 * 35000, SDS-PAGE
tetramer
additional information
-
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal form P is grown at a salt concentration of 0.3 M (NH4)2SO4, pH 7.0
-
hanging-drop vapor-diffusion method. Crystal structure at 2.0 A resolution of formyltransferase from in ternary complex with its substrates formylmethanofuran and tetrahydromethanopterin and products methanofuran and formyl-tetrahydromethanopterin. Methanofuran is embedded in an elongated cleft at the homodimer interface and fixed by multiple hydrophobic interactions. Tetrahydromethanopterin is weakly bound in a shallow and wide cleft that provides two binding sites
X-ray diffraction studies of forms M, P and S
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
50% inactivation after 20 min at 1.2 M K3PO4. No inactivation after 20 min at 1.5 M K3PO4
90
stable up to, in presence of salts
130
-
up to, in the presence of high lyotropic salt concentrations, mechanism of salt-dependent thermoadaption
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
potassium cyclic 2,3-diphosphoglycerate and potassium phosphate stabilize the enzyme
-
presence of salts, 1.5 M, required for optimal stabilization, order of efficiency in protecting the enzyme from heat inactivation at 90°C: K2HPO4, (NH4)2SO4, KCl, NH4Cl, NaCl, Na2SO4, Na2HPO4
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivated slowly under oxic conditions, purification in anaerobic chamber
-
486097
stable under oxic conditions
-
726828
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
in a anaerobic chamber
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Breitung, J.; Brner, G.; Scholz, S.; Linder, D.; Stetter, K.O.; Thauer, R.K.
Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri
Eur. J. Biochem.
210
971-981
1992
Methanopyrus kandleri
Manually annotated by BRENDA team
Shima, S.; Weiss, D.S.; Thauer, R.K.
Formylmethanofuran:tetrahydromethanopterin formyltransferase (Ftr) from the hyperthermophilic Methanopyrus kandleri. Cloning, sequencing and functional expression of the ftr gene and one-step purification of the enzyme overproduced in Escherichia coli
Eur. J. Biochem.
230
906-913
1995
Methanopyrus kandleri (Q49610), Methanopyrus kandleri
Manually annotated by BRENDA team
Shima, S.; Thauer, R.K.; Michel, H.; Ermler, U.
Crystallization and preliminary x-ray diffraction studies of formylmethanofuran:tetrahydromethanopterin formyltransferase from Methanopyrus kandleri
Proteins Struct. Funct. Genet.
26
118-120
1996
Methanopyrus kandleri
Manually annotated by BRENDA team
Ermler, U.; Merckel, M.C.; Thauer, R.K.; Shima, S.
Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability
Structure
5
635-646
1997
Methanopyrus kandleri
Manually annotated by BRENDA team
Shima, S.; Thauer, R.K.
Tetrahydromethanopterin-specific enzymes from Methanopyrus kandleri
Methods Enzymol.
331
317-353
2001
Methanopyrus kandleri
Manually annotated by BRENDA team
Shima, S.; Thauer, R.K.; Ermler, U.
Hyperthermophilic and salt-dependent formyltransferase from Methanopyrus kandleri
Biochem. Soc. Trans.
32
269-272
2004
Methanopyrus kandleri
Manually annotated by BRENDA team
Acharya, P.; Warkentin, E.; Ermler, U.; Thauer, R.K.; Shima, S.
The structure of formylmethanofuran: tetrahydromethanopterin formyltransferase in complex with its coenzymes
J. Mol. Biol.
357
870-879
2006
Methanopyrus kandleri (Q8TX60)
Manually annotated by BRENDA team
Mamat, B.; Roth, A.; Grimm, C.; Ermler, U.; Tziatzios, C.; Schubert, D.; Thauer, R.K., Shima, S.
Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship
Protein Sci.
11
:2168-2178
2002
Archaeoglobus fulgidus (O28076), Archaeoglobus fulgidus, Methanopyrus kandleri (Q49610), Methanopyrus kandleri, Methanopyrus kandleri DSM 6324 (Q49610), Methanosarcina barkeri (P55301), Methanosarcina barkeri, Methanosarcina barkeri DSM 804 (P55301)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team