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Literature summary extracted from

  • Buchenau, B.; Thauer, R.K.
    Tetrahydrofolate-specific enzymes in Methanosarcina barkeri and growth dependence of this methanogenic archaeon on folic acid or p-aminobenzoic acid (2004), Arch. Microbiol., 182, 313-325.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.15 heterologously overproduced in Escherichia coli with a C-terminal His6-tag Methanosarcina barkeri
2.1.2.1 heterologously overproduced in Escherichia coli without a His6-tag Methanosarcina barkeri
3.5.4.9 heterologously overproduced in Escherichia coli with a C-terminal His6-tag Methanosarcina barkeri

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.2.1 tetrahydrofolate at concentrations above 0.015 mM, substrate inhibition is observed Methanosarcina barkeri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.15 additional information
-
 5,10-methylenetetrahydrofolate pH 6.0, 37°C, the Km-value for 5,10-methylenetetrahydrofolate in the presence of 2.7 mM NAD+ is below 0.005 mM Methanosarcina barkeri
1.5.1.15 0.15
-
 NAD+ pH 6.0, 37°C Methanosarcina barkeri
2.1.2.1 0.002
-
 (6S)-tetrahydrofolate pH 7.2, 37°C Methanosarcina barkeri
2.1.2.1 0.2
-
 L-serine pH 7.2, 37°C Methanosarcina barkeri

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.15 31000
-
 x * 31000, SDS-PAGE Methanosarcina barkeri
1.5.1.15 318700
-
 x * 318700, calculated from sequence Methanosarcina barkeri
2.1.2.1 43000
-
 2 * 43000, SDS-PAGE Methanosarcina barkeri
2.1.2.1 45047
-
 2 * 45047, calculated from sequence Methanosarcina barkeri
2.1.2.1 100000
-
 gel filtration Methanosarcina barkeri
3.5.4.9 31000
-
 x * 31000, SDS-PAGE Methanosarcina barkeri
3.5.4.9 318700
-
 x * 318700, calculated from sequence Methanosarcina barkeri

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.15 Methanosarcina barkeri Q46A53
-
-
1.5.1.15 Methanosarcina barkeri DSM 804 Q46A53
-
-
2.1.2.1 Methanosarcina barkeri Q46A52
-
-
2.1.2.1 Methanosarcina barkeri DSM 804 Q46A52
-
-
3.5.4.9 Methanosarcina barkeri Q46A53
-
-
3.5.4.9 Methanosarcina barkeri DSM 804 Q46A53
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.15
-
 Methanosarcina barkeri
2.1.2.1
-
 Methanosarcina barkeri
3.5.4.9
-
 Methanosarcina barkeri

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.15 1 2 pH 6.0, 37°C, purified enzyme, recombinant Methanosarcina barkeri
1.5.1.15 5
-
 pH 6.0, 37°C, extract from Escherichia coli cells carrying the expression vector Methanosarcina barkeri
2.1.2.1 0.5
-
 pH 7.2, 37°C, extract from Escherichia coli cells carrying the expression vector Methanosarcina barkeri
2.1.2.1 4.3
-
 pH 7.2, 37°C, purified enzyme, recombinant Methanosarcina barkeri
3.5.4.9 2 3 pH 8.0, 37°C, extract from Escherichia coli cells carrying the expression vector Methanosarcina barkeri
3.5.4.9 66
-
 pH 8.0, 37°C, purified enzyme, recombinant Methanosarcina barkeri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.15 5,10-methylenetetrahydrofolate + NAD+ the bifunctional enzyme also shows N5,N10-methenyltetrahydrofolate cyclohydrolase activity EC 3.5.4.9. with NADP+ (1 mM), the enzyme shows less than 0.1% of the activity obtained with NAD+ (1 mM). The purified enzyme shows no activity with methylene-tetrahydromethanopterin or with 5,10-methylenetetrahydrosarcinapterin either in the presence of NAD+ or NADP+ or in the presence of F420 Methanosarcina barkeri 5,10-methenyltetrahydrofolate + NADH + H+
-
 ?
1.5.1.15 5,10-methylenetetrahydrofolate + NAD+ the bifunctional enzyme also shows N5,N10-methenyltetrahydrofolate cyclohydrolase activity EC 3.5.4.9. with NADP+ (1 mM), the enzyme shows less than 0.1% of the activity obtained with NAD+ (1 mM). The purified enzyme shows no activity with methylene-tetrahydromethanopterin or with 5,10-methylenetetrahydrosarcinapterin either in the presence of NAD+ or NADP+ or in the presence of F420 Methanosarcina barkeri DSM 804 5,10-methenyltetrahydrofolate + NADH + H+
-
 ?
2.1.2.1 (6S)-tetrahydrofolate + L-serine the enzyme also catalyzes the formation of methylene-tetrahydromethanopterin from tetrahydromethanopterin and L-serine, albeit with a catalytic efficiency which is less than 1% of that with (6S)-tetrahydrofolate as substrate. The catalytic efficiency with methylene-tetrahydrosarcinapterin as substrate is even lower Methanosarcina barkeri 5,10-methylenetetrahydrofolate + glycine + H2O
-
 ?
2.1.2.1 (6S)-tetrahydrofolate + L-serine the enzyme also catalyzes the formation of methylene-tetrahydromethanopterin from tetrahydromethanopterin and L-serine, albeit with a catalytic efficiency which is less than 1% of that with (6S)-tetrahydrofolate as substrate. The catalytic efficiency with methylene-tetrahydrosarcinapterin as substrate is even lower Methanosarcina barkeri DSM 804 5,10-methylenetetrahydrofolate + glycine + H2O
-
 ?
2.1.2.1 additional information the enzyme also catalyzes the tetrahydrofolate-independent retroaldol cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde Methanosarcina barkeri ?
-
 ?
2.1.2.1 additional information the enzyme also catalyzes the tetrahydrofolate-independent retroaldol cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde Methanosarcina barkeri DSM 804 ?
-
 ?
3.5.4.9 5,10-methenyltetrahydrofolate + H2O the bifunctional enzyme also shows N5,N10-methylene-H4F dehydrogenase activity, EC 1.5.1.15 Methanosarcina barkeri 10-formyltetrahydrofolate
-
 ?
3.5.4.9 5,10-methenyltetrahydrofolate + H2O the bifunctional enzyme also shows N5,N10-methylene-H4F dehydrogenase activity, EC 1.5.1.15 Methanosarcina barkeri DSM 804 10-formyltetrahydrofolate
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.15 ? x * 31000, SDS-PAGE Methanosarcina barkeri
1.5.1.15 ? x * 318700, calculated from sequence Methanosarcina barkeri
2.1.2.1 homodimer 2 * 43000, SDS-PAGE Methanosarcina barkeri
2.1.2.1 homodimer 2 * 45047, calculated from sequence Methanosarcina barkeri
3.5.4.9 ? x * 31000, SDS-PAGE Methanosarcina barkeri
3.5.4.9 ? x * 318700, calculated from sequence Methanosarcina barkeri

Synonyms

EC Number Synonyms Comment Organism
1.5.1.15 bifunctional N5,N10-methylene-H4F dehydrogenase/N5,N10-methenyltetrahydrofolate cyclohydrolase bifunctional enzyme EC 1.5.1.15/EC 3.5.4.9 Methanosarcina barkeri
1.5.1.15 FolD bifunctional enzyme EC 1.5.1.15/EC 3.5.4.9 Methanosarcina barkeri
1.5.1.15 NAD+-dependent methylene-H4F dehydrogenase
-
 Methanosarcina barkeri
2.1.2.1 GlyA
-
 Methanosarcina barkeri
2.1.2.1 serine hydroxymethyltransferase
-
 Methanosarcina barkeri
2.1.2.1 serine:H4F hydroxymethyltransferase
-
 Methanosarcina barkeri
2.1.2.1 serine:tetrahydrofolate hydroxymethyltransferase
-
 Methanosarcina barkeri
3.5.4.9 bifunctional N5,N10-methylene-H4F dehydrogenase/N5,N10-methenyl-H4F cyclohydrolase bifunctional enzyme EC 1.5.1.15/EC 3.5.4.9 Methanosarcina barkeri
3.5.4.9 FolD bifunctional enzyme EC 1.5.1.15/EC 3.5.4.9 Methanosarcina barkeri
3.5.4.9 methenyl-H4F cyclohydrolase
-
 Methanosarcina barkeri

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.15 37
-
 assay at Methanosarcina barkeri
2.1.2.1 37
-
 assay at Methanosarcina barkeri
3.5.4.9 37
-
 assay at Methanosarcina barkeri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.15 6
-
-
 Methanosarcina barkeri
2.1.2.1 7.2
-
 assay at Methanosarcina barkeri
3.5.4.9 8
-
 assay at Methanosarcina barkeri

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.15 NAD+ with NADP+ (1 mM), the enzyme shows less than 0.1% of the activity obtained with NAD+ (1 mM) Methanosarcina barkeri
2.1.2.1 pyridoxal 5'-phosphate
-
 Methanosarcina barkeri