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Literature summary for 2.1.2.1 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
Search for more literature for 2.1.2.1

Cloned(Commentary)

Cloned (Comment) Organism
heterologously overproduced in Escherichia coli without a His6-tag Methanosarcina barkeri

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
 (6S)-tetrahydrofolate pH 7.2, 37°C Methanosarcina barkeri
0.2
-
 L-serine pH 7.2, 37°C Methanosarcina barkeri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
 2 * 43000, SDS-PAGE Methanosarcina barkeri
45047
-
 2 * 45047, calculated from sequence Methanosarcina barkeri
100000
-
 gel filtration Methanosarcina barkeri

Organism

Organism UniProt Comment Textmining
Methanosarcina barkeri Q46A52
-
-
Methanosarcina barkeri DSM 804 Q46A52
-
-

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
0.5
-
 pH 7.2, 37°C, extract from Escherichia coli cells carrying the expression vector Methanosarcina barkeri
4.3
-
 pH 7.2, 37°C, purified enzyme, recombinant Methanosarcina barkeri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(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
-
 ?
(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
-
 ?
additional information the enzyme also catalyzes the tetrahydrofolate-independent retroaldol cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde Methanosarcina barkeri ?
-
 ?
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 ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 43000, SDS-PAGE Methanosarcina barkeri
homodimer 2 * 45047, calculated from sequence Methanosarcina barkeri

Synonyms

Synonyms Comment Organism
GlyA
-
 Methanosarcina barkeri
serine hydroxymethyltransferase
-
 Methanosarcina barkeri
serine:H4F hydroxymethyltransferase
-
 Methanosarcina barkeri
serine:tetrahydrofolate hydroxymethyltransferase
-
 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
7.2
-
 assay at Methanosarcina barkeri

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Methanosarcina barkeri