Information on EC 2.3.1.101 - formylmethanofuran-tetrahydromethanopterin N-formyltransferase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
2.3.1.101
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RECOMMENDED NAME
GeneOntology No.
formylmethanofuran-tetrahydromethanopterin N-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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Methane metabolism
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methanogenesis from H2 and CO2
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Microbial metabolism in diverse environments
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reductive acetyl coenzyme A pathway II (autotrophic methanogens)
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methanogenesis from CO2
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain VC-19, DSM 4304
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Manually annotated by BRENDA team
chemolithoautotrophic
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-
Manually annotated by BRENDA team
chemolithoautotrophic
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-
Manually annotated by BRENDA team
strain AM 1
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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 + 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
methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
formylmethanofuran + 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
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + 5-formyl-5,6,7,8-tetrahydromethanopterin
show the reaction diagram
D1J8Z9
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-
-
?
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
(NH4)2SO4
K+
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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
NaCl
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1 M increases the activity 20fold
potassium phosphate
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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
additional information
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not: Fe, Mo, V, Wo
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-diphosphoglycerate
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the 1 M 2,3-diphosphoglycerate the enzyme is highly active
potassium cyclic 2,3-diphosphoglycerate
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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
0.017 - 0.107
5,6,7,8-tetrahydromethanopterin
0.01 - 0.06
formylmethanofuran
20 - 70
N-Furfurylformamide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1970 - 2770
5,6,7,8-tetrahydromethanopterin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
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pH 7.5, 65°C, cell extract
0.05
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pH 7.5, 65°C, cell extract
0.6
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pH 7.5, 65°C
14.4
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pH 7.5, 65°C, cell extract
additional information
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
20°C: about 60% of maximal activity, 50°C: about 60% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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the hyperthermophilic methanogenic archaeon grows on H2 and CO2 as sole energy source best at 98°C
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Methanosarcina barkeri (strain Fusaro / DSM 804)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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4 * 30000 SDS-PAGE
31836
x * 31836, calculated from sequence
31864
x * 31864, calculated from sequence
310000
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enzyme complex with three other polypeptides that shows sequence identities with the subunits of formylmethanofuran-dehydrogenase and are required for stability of enzyme, the subunits are present in 2:2:2:2 stoichiometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method at 4°C, crystal structure at 2.0 A resolution
crystal form P is grown at a salt concentration of 0.3 M (NH4)2SO4, pH 7.0
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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
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vapor diffusion method at 4°C, crystal structure at 1.9 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
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stable for more than 4 h
70
up to, in presence of 1.5 M K2HPO4, hyperthermophilic enzyme
130
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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
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potassium cyclic 2,3-diphosphoglycerate and potassium phosphate stabilize the enzyme
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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
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salts protect against heat inactivation, order of efficiency: K2HPO4, (NH4)2SO4, KCl, NH4Cl, Na2SO4, Na2HPO4
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
if a single chromatographic step was performed 90% loss of activity, in 24 h 100% loss of activity
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486095
inactivated slowly under oxic conditions, purification in anaerobic chamber
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486097
relatively insensitive towards inactivation by molecular oxygen
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486086
stable in presence of molecular oxygen
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486089
stable under oxic conditions
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726828
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM Tricine/KOH, pH 8, stable for 1 week
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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