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Information on EC 2.3.1.101 - formylmethanofuran-tetrahydromethanopterin N-formyltransferase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O28076

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IUBMB Comments
Methanofuran is a complex 4-substituted furfurylamine and is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum.
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This record set is specific for:
Archaeoglobus fulgidus
UNIPROT: O28076
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The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
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:5,6,7,8-tetrahydromethanopterin N5-formyltransferase
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formylmethanofuran:tetrahydromethanopterin formyltransferase
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formyltransferase, formylmethanofuran-tetrahydromethanopterin
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formyltransferase/hydrolase complex
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FTR
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N-formylmethanofuran(CHO-MFR):tetrahydromethanopterin(H4MPT) formyltransferase
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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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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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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
show the reaction diagram
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-
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r
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
methanofuran + N5-formyl-5,6,7,8-tetrahydromethanopterin
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K3PO4
0.1 M salt concentration is required for 50% activity at 83°C. 1.0 M salt concentration is required for 100% activity at 83°C
(NH4)2SO4
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can substitute for K2HPO4 in stimulation
K2HPO4
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
5,6,7,8-tetrahydromethanopterin
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0.032
formylmethanofuran
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14.4
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pH 7.5, 65°C, cell extract
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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4 * 30000 SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
the enzyme already reveals a tetrameric state at salt concentrations below 0.1 M
tetramer
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4 * 30000 SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method at 4°C, crystal structure at 2.0 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
50% inactivation after 20 min at 0.005 M K3PO4. No inactivation after 20 min at 0.05 M K3PO4
80
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complete thermostability in presence of 0.5 M K2HPO4
90
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stable up to, in presence of salts
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
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enzyme soluble in 60% ammonium sulfate
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
relatively insensitive towards inactivation by molecular oxygen
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486086
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schwrer, B.; Breitung, J.; Klein, A.R.; Stetter, K.O.; Thauer, R.K.
Formylmethanofuran:tetrahydromethanopterin formyltransferase and N5,N10-methylenetetrahydromethanopterin dehydrogenase from the sulfate-reducing Archaeoglobus fulgidus: similarities with the enzymes from methanogenic Archaea
Arch. Microbiol.
159
225-232
1993
Archaeoglobus fulgidus, Archaeoglobus fulgidus VC-19 / DSM 4304
Manually annotated by BRENDA team
Vornolt, J.; Kunow, J.; Stetter, K.; Thauer, R.
Enzymes and coenzymes of the carbon monoxide dehydrogenase pathway for autotrophic CO2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus
Arch. Microbiol.
163
112-118
1995
Archaeoglobus fulgidus, Archaeoglobus lithotrophicus, Archaeoglobus lithotrophicus TF-2, Archaeoglobus profundus, Archaeoglobus profundus DSM 5631
-
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