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EC Tree
IUBMB Comments The enzyme catalyses the reaction in the direction of producing (5-formylfuran-3-yl)methyl phosphate, an intermediate in the biosynthesis of methanofuran. The sequence of events starts with the removal of a phosphate group, followed by aldol condensation and cyclization. Methanofuran is a carbon-carrier cofactor involved in the first step of the methanogenic reduction of carbon dioxide by methanogenic archaea.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
mj1099, 4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase,
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2-furaldehyde phosphate synthase
4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase
2-furaldehyde phosphate synthase
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2-furaldehyde phosphate synthase
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4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase
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4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase
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4-HFC-P synthase
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mfnB
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MJ1099
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2 D-glyceraldehyde 3-phosphate = (5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
2 D-glyceraldehyde 3-phosphate = (5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
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2 D-glyceraldehyde 3-phosphate = (5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
a phosphate elimination reaction and a triose phosphate isomerase-like reaction occur at the glyceraldehyde 3-phosphate binding site I and II, respectively, prior to the aldol condensation between the enzyme-bound enol form of methylglyoxal and dihydroxyacetone phosphate, after which the catalytic cycle is completed by a cyclization and two dehydration reactions assisted by several general acids/bases at the same active site
2 D-glyceraldehyde 3-phosphate = (5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
a phosphate elimination reaction and a triose phosphate isomerase-like reaction occur at the glyceraldehyde 3-phosphate binding site I and II, respectively, prior to the aldol condensation between the enzyme-bound enol form of methylglyoxal and dihydroxyacetone phosphate, after which the catalytic cycle is completed by a cyclization and two dehydration reactions assisted by several general acids/bases at the same active site
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D-glyceraldehyde-3-phosphate phosphate-lyase [D-glyceraldehyde-3-phosphate-adding; (5-formylfuran-3-yl)methyl-phosphate-forming]
The enzyme catalyses the reaction in the direction of producing (5-formylfuran-3-yl)methyl phosphate, an intermediate in the biosynthesis of methanofuran. The sequence of events starts with the removal of a phosphate group, followed by aldol condensation and cyclization. Methanofuran is a carbon-carrier cofactor involved in the first step of the methanogenic reduction of carbon dioxide by methanogenic archaea.
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2 D-glyceraldehyde 3-phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
D-glyceraldehyde 3-phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + H2O
D-glyceraldehyde 3-phosphate + glycerone phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
additional information
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2 D-glyceraldehyde 3-phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
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2 D-glyceraldehyde 3-phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
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(5-formylfuran-3-yl)methyl phosphate i.e. 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate
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2 D-glyceraldehyde 3-phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
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(5-formylfuran-3-yl)methyl phosphate i.e. 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate
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2 D-glyceraldehyde 3-phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
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D-glyceraldehyde 3-phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + H2O
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D-glyceraldehyde 3-phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + H2O
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D-glyceraldehyde 3-phosphate + glycerone phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
the enzyme is involved in biosynthesis of methanofuran, a coenzyme involved in the reduction of carbon dioxide to methane
(5-formylfuran-3-yl)methyl phosphate i.e. 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate
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D-glyceraldehyde 3-phosphate + glycerone phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
the enzyme is not able to use pyruvate as substrate
(5-formylfuran-3-yl)methyl phosphate i.e. 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate
?
D-glyceraldehyde 3-phosphate + glycerone phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
the enzyme is involved in biosynthesis of methanofuran, a coenzyme involved in the reduction of carbon dioxide to methane
(5-formylfuran-3-yl)methyl phosphate i.e. 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate
?
D-glyceraldehyde 3-phosphate + glycerone phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
the enzyme is not able to use pyruvate as substrate
(5-formylfuran-3-yl)methyl phosphate i.e. 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate
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additional information
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no substrates: pyruvate, methylglyoxal, phosphoenolpyruvate, oxaloacetic acid, dihydroxyacetone, and dihydroxyacetone phosphate
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additional information
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no substrates: pyruvate, methylglyoxal, phosphoenolpyruvate, oxaloacetic acid, dihydroxyacetone, and dihydroxyacetone phosphate
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additional information
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no substrates: pyruvate, methylglyoxal, phosphoenolpyruvate, oxaloacetic acid, dihydroxyacetone, and dihydroxyacetone phosphate
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D-glyceraldehyde 3-phosphate + glycerone phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
D-glyceraldehyde 3-phosphate + glycerone phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
the enzyme is involved in biosynthesis of methanofuran, a coenzyme involved in the reduction of carbon dioxide to methane
(5-formylfuran-3-yl)methyl phosphate i.e. 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate
-
?
D-glyceraldehyde 3-phosphate + glycerone phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
the enzyme is involved in biosynthesis of methanofuran, a coenzyme involved in the reduction of carbon dioxide to methane
(5-formylfuran-3-yl)methyl phosphate i.e. 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate
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?
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0.035 - 0.048
D-glyceraldehyde 3-phosphate
0.035
D-glyceraldehyde 3-phosphate
wild-type, pH 7.0, 70°C
0.048
D-glyceraldehyde 3-phosphate
mutant K155R, pH 7.0, 70°C
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0.022 - 0.026
D-glyceraldehyde 3-phosphate
0.022
D-glyceraldehyde 3-phosphate
mutant K155R, pH 7.0, 70°C
0.026
D-glyceraldehyde 3-phosphate
wild-type, pH 7.0, 70°C
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0.46 - 0.74
D-glyceraldehyde
0.46
D-glyceraldehyde
mutant K155R, pH 7.0, 70°C
0.74
D-glyceraldehyde
wild-type, pH 7.0, 70°C
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SwissProt
brenda
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SwissProt
brenda
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physiological function
the enzyme is involved in biosynthesis of methanofuran, a coenzyme involved in the reduction of carbon dioxide to methane
physiological function
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the enzyme is involved in biosynthesis of methanofuran, a coenzyme involved in the reduction of carbon dioxide to methane
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Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
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25000
x * 25000, SDS-PAGE
26053
6 * 26053, calculated and crystallization data
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?
x * 25000, SDS-PAGE
hexamer
6 * 26053, calculated and crystallization data
hexamer
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6 * 26053, calculated and crystallization data
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molecular docking of glycerinaldehyde 3-phosphate into the active site
to 1.7 A resolution. Enzyme is a member of the TIM-barrel superfamily and the biological unit is a homohexamer
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D151N
mutation of strictly conserved residue around the active site, complete inactivation
D25N
mutation of strictly conserved residue around the active site, complete inactivation
K155R
kcat/KM value comparable to the wild-type
K27R
mutation of strictly conserved residue around the active site, complete inactivation
K85R
mutation of strictly conserved residue around the active site, complete inactivation
D151N
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mutation of strictly conserved residue around the active site, complete inactivation
D25N
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mutation of strictly conserved residue around the active site, complete inactivation
K155R
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kcat/KM value comparable to the wild-type
K27R
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mutation of strictly conserved residue around the active site, complete inactivation
K85R
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mutation of strictly conserved residue around the active site, complete inactivation
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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Miller, D.; Wang, Y.; Xu, H.; Harich, K.; White, R.H.
Biosynthesis of the 5-(aminomethyl)-3-furanmethanol moiety of methanofuran
Biochemistry
53
4635-4647
2014
Methanocaldococcus jannaschii (Q58499), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58499)
brenda
Wang, Y.; Xu, H.; Harich, K.C.; White, R.H.
Identification and characterization of a tyramine-glutamate ligase (MfnD) involved in methanofuran biosynthesis
Biochemistry
53
6220-6230
2014
Methanocaldococcus jannaschii (Q58499), Methanocaldococcus jannaschii DSM 2661 (Q58499)
brenda
Bobik, T.A.; Morales, E.J.; Shin, A.; Cascio, D.; Sawaya, M.R.; Arbing, M.; Yeates, T.O.; Rasche, M.E.
Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii
Acta Crystallogr. Sect. F
70
1472-1479
2014
Methanocaldococcus jannaschii (Q58499), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58499)
brenda
Wang, Y.; Jones, M.K.; Xu, H.; Ray, W.K.; White, R.H.
Mechanism of the enzymatic synthesis of 4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate (4-HFC-P) from glyceraldehyde-3-phosphate catalyzed by 4-HFC-P synthase
Biochemistry
54
2997-3008
2015
Methanocaldococcus jannaschii (Q58499), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58499)
brenda
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4.2.3.153 (5-formylfuran-3-yl)methyl phosphate synthase
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