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Literature summary extracted from

  • Fu, T.F.; Hunt, S.; Schirch, V.; Safo, M.K.; Chen, B.H.
    Properties of human and rabbit cytosolic serine hydroxymethyltransferase are changed by single nucleotide polymorphic mutations (2005), Arch. Biochem. Biophys., 442, 92-101.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.1.2.1 pyridoxal 5'-phosphate
-
 Homo sapiens
2.1.2.1 pyridoxal 5'-phosphate
-
 Oryctolagus cuniculus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.1 mutations introduced into the cDNA for human cytosolic SHMT and expressed from an Escherichia coli expression system Homo sapiens
2.1.2.1 mutations introduced into the cDNA for rabbit cytosolic SHMT and expressed from an Escherichia coli expression system Oryctolagus cuniculus

Protein Variants

EC Number Protein Variants Comment Organism
2.1.2.1 L474F shows normal values for kcat and Km for serine, shows lowered affinity (increased dissociation constant) for only the pentaglutamate form of the folate ligand, decreased rates of pyridoxal phosphate addition to the mutant apo enzymes to form the active holo enzymes, thermal stability of SHMT or the rate at which it converts 5,10-methenyl tetrahydropteroyl pentaglutamate to 5-formyl tetrahydropteroyl pentaglutamate not affected Homo sapiens
2.1.2.1 L474F shows normal values for kcat and Km for serine, shows lowered affinity (increased dissociation constant) for only the pentaglutamate form of the folate ligand, shows decreased rates of pyridoxal phosphate addition to the mutant apo enzymes to form the active holo enzymes, thermal stability of SHMT or the rate at which it converts 5,10-methenyl tetrahydropteroyl pentaglutamate to 5-formyl tetrahydropteroyl pentaglutamate not affected Oryctolagus cuniculus
2.1.2.1 S394N shows normal values for kcat and Km for serine, has increased dissociation constant values for both glycine and tetrahydrofolate and its pentaglutamate form compared to wild-type enzyme, decreased rates of pyridoxal phosphate addition to the mutant apo enzymes to form the active holo enzymes, thermal stability of SHMT or the rate at which it converts 5,10-methenyl tetrahydropteroyl pentaglutamate to 5-formyl tetrahydropteroyl pentaglutamate not affected Homo sapiens
2.1.2.1 S394N shows normal values for kcat and Km for serine, has increased dissociation constant values for both glycine and tetrahydrofolate and its pentaglutamate form compared to wild-type enzyme, shows decreased rates of pyridoxal phosphate addition to the mutant apo enzymes to form the active holo enzymes, thermal stability of SHMT or the rate at which it converts 5,10-methenyl tetrahydropteroyl pentaglutamate to 5-formyl tetrahydropteroyl pentaglutamate not affected Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.1 0.0037
-
 tetrahydrofolate mutant L474F Homo sapiens
2.1.2.1 0.0041
-
 tetrahydrofolate wild-type Homo sapiens
2.1.2.1 0.009
-
 tetrahydrofolate mutant L474F Oryctolagus cuniculus
2.1.2.1 0.01
-
 tetrahydrofolate wild-type Oryctolagus cuniculus
2.1.2.1 0.01
-
 tetrahydrofolate mutant S394N Homo sapiens
2.1.2.1 0.025
-
 tetrahydrofolate mutant S394N Oryctolagus cuniculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.2.1 cytosol
-
 Homo sapiens 5829
-
2.1.2.1 cytosol
-
 Oryctolagus cuniculus 5829
-

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Homo sapiens
-
-
-
2.1.2.1 Oryctolagus cuniculus P07511
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.1 by ammonium sulfate precipitation and gel filtration, more than 95% pure Homo sapiens
2.1.2.1 by ammonium sulfate precipitation and gel filtration, more than 95% pure Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 5,10-methenyl-tetrahydropteroyl pentaglutamate + glycine + H2O
-
 Homo sapiens 5-formyl-tetrahydropteroyl pentaglutamate + L-serine
-
 ?
2.1.2.1 5,10-methenyl-tetrahydropteroyl pentaglutamate + glycine + H2O
-
 Oryctolagus cuniculus 5-formyl-tetrahydropteroyl pentaglutamate + L-serine
-
 ?
2.1.2.1 L-serine + tetrahydrofolate
-
 Homo sapiens glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate
-
 Oryctolagus cuniculus glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 serine hydroxymethyltransferase
-
 Homo sapiens
2.1.2.1 serine hydroxymethyltransferase
-
 Oryctolagus cuniculus
2.1.2.1 SHMT
-
 Homo sapiens
2.1.2.1 SHMT
-
 Oryctolagus cuniculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.2.1 0.02
-
 tetrahydrofolate mutant S394N, in the presence of pyridoxal phosphate Homo sapiens
2.1.2.1 0.02167
-
 tetrahydrofolate mutant L474F, in the presence of pyridoxal phosphate Homo sapiens
2.1.2.1 0.033
-
 tetrahydrofolate mutant L474F, in the presence of pyridoxal phosphate Oryctolagus cuniculus
2.1.2.1 0.04
-
 tetrahydrofolate wild-type, in the presence of pyridoxal phosphate Homo sapiens
2.1.2.1 0.045
-
 tetrahydrofolate mutant S394N, in the presence of pyridoxal phosphate Oryctolagus cuniculus
2.1.2.1 0.07
-
 tetrahydrofolate wild-type, in the presence of pyridoxal phosphate Oryctolagus cuniculus