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Literature summary for 1.5.1.15 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)

Cloned (Comment) Organism
heterologously overproduced in Escherichia coli with a C-terminal His6-tag Methanosarcina barkeri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
0.15
-
NAD+ pH 6.0, 37°C Methanosarcina barkeri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31000
-
x * 31000, SDS-PAGE Methanosarcina barkeri
318700
-
x * 318700, calculated from sequence Methanosarcina barkeri

Organism

Organism UniProt Comment Textmining
Methanosarcina barkeri Q46A53
-
-
Methanosarcina barkeri DSM 804 Q46A53
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methanosarcina barkeri

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1 2 pH 6.0, 37°C, purified enzyme, recombinant Methanosarcina barkeri
5
-
pH 6.0, 37°C, extract from Escherichia coli cells carrying the expression vector Methanosarcina barkeri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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+
-
?
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+
-
?

Subunits

Subunits Comment Organism
? x * 31000, SDS-PAGE Methanosarcina barkeri
? x * 318700, calculated from sequence Methanosarcina barkeri

Synonyms

Synonyms Comment Organism
bifunctional N5,N10-methylene-H4F dehydrogenase/N5,N10-methenyltetrahydrofolate cyclohydrolase bifunctional enzyme EC 1.5.1.15/EC 3.5.4.9 Methanosarcina barkeri
FolD bifunctional enzyme EC 1.5.1.15/EC 3.5.4.9 Methanosarcina barkeri
NAD+-dependent methylene-H4F dehydrogenase
-
Methanosarcina barkeri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Methanosarcina barkeri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
Methanosarcina barkeri

Cofactor

Cofactor Comment Organism Structure
NAD+ with NADP+ (1 mM), the enzyme shows less than 0.1% of the activity obtained with NAD+ (1 mM) Methanosarcina barkeri