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Literature summary extracted from

  • Appaji Rao, N.; Talwar, R.; Savithri, H.S.
    Molecular organization, catalytic mechanism and function of serine hydroxymethyltransferase - a potential target for cancer chemotherapy (2000), Int. J. Biochem. Cell Biol., 32, 405-416.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.1.2.1 medicine enzyme is a potential target for cancer chemotherapy Escherichia coli
2.1.2.1 medicine enzyme is a potential target for cancer chemotherapy Homo sapiens
2.1.2.1 medicine enzyme is a potential target for cancer chemotherapy Saccharomyces cerevisiae
2.1.2.1 medicine enzyme is a potential target for cancer chemotherapy Oryctolagus cuniculus
2.1.2.1 medicine enzyme is a potential target for cancer chemotherapy Ovis aries
2.1.2.1 medicine enzyme is a potential target for cancer chemotherapy Pisum sativum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.1
-
 Escherichia coli
2.1.2.1
-
 Homo sapiens
2.1.2.1
-
 Oryctolagus cuniculus
2.1.2.1
-
 Ovis aries

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.2.1
-
 Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.2.1 4-chloro-L-threonine
-
 Escherichia coli
2.1.2.1 4-chloro-L-threonine
-
 Homo sapiens
2.1.2.1 4-chloro-L-threonine
-
 Oryctolagus cuniculus
2.1.2.1 4-chloro-L-threonine
-
 Ovis aries
2.1.2.1 4-chloro-L-threonine
-
 Pisum sativum
2.1.2.1 4-chloro-L-threonine
-
 Saccharomyces cerevisiae
2.1.2.1 beta-trifluoroallothreonine
-
 Escherichia coli
2.1.2.1 beta-trifluoroallothreonine
-
 Homo sapiens
2.1.2.1 beta-trifluoroallothreonine
-
 Oryctolagus cuniculus
2.1.2.1 beta-trifluoroallothreonine
-
 Pisum sativum
2.1.2.1 beta-trifluoroallothreonine
-
 Saccharomyces cerevisiae
2.1.2.1 beta-trifluorothreonine
-
 Escherichia coli
2.1.2.1 beta-trifluorothreonine
-
 Homo sapiens
2.1.2.1 beta-trifluorothreonine
-
 Oryctolagus cuniculus
2.1.2.1 beta-trifluorothreonine
-
 Ovis aries
2.1.2.1 beta-trifluorothreonine
-
 Pisum sativum
2.1.2.1 beta-trifluorothreonine
-
 Saccharomyces cerevisiae
2.1.2.1 D-cycloserine
-
 Oryctolagus cuniculus
2.1.2.1 D-cycloserine
-
 Ovis aries
2.1.2.1 substituted hydroxylamine derivates
-
 Escherichia coli
2.1.2.1 substituted hydroxylamine derivates
-
 Homo sapiens
2.1.2.1 substituted hydroxylamine derivates
-
 Oryctolagus cuniculus
2.1.2.1 substituted hydroxylamine derivates
-
 Ovis aries
2.1.2.1 substituted hydroxylamine derivates
-
 Pisum sativum
2.1.2.1 substituted hydroxylamine derivates
-
 Saccharomyces cerevisiae
2.1.2.1 sulfonyl fluoride triazine derivates
-
 Escherichia coli
2.1.2.1 sulfonyl fluoride triazine derivates
-
 Homo sapiens
2.1.2.1 sulfonyl fluoride triazine derivates
-
 Oryctolagus cuniculus
2.1.2.1 sulfonyl fluoride triazine derivates
-
 Ovis aries
2.1.2.1 sulfonyl fluoride triazine derivates
-
 Pisum sativum
2.1.2.1 sulfonyl fluoride triazine derivates
-
 Saccharomyces cerevisiae
2.1.2.1 Thiosemicarbazide
-
 Escherichia coli
2.1.2.1 Thiosemicarbazide
-
 Homo sapiens
2.1.2.1 Thiosemicarbazide
-
 Oryctolagus cuniculus
2.1.2.1 Thiosemicarbazide
-
 Pisum sativum
2.1.2.1 Thiosemicarbazide
-
 Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.2.1 cytoplasm
-
 Escherichia coli 5737
-
2.1.2.1 cytoplasm
-
 Homo sapiens 5737
-
2.1.2.1 cytoplasm
-
 Saccharomyces cerevisiae 5737
-
2.1.2.1 cytoplasm
-
 Oryctolagus cuniculus 5737
-
2.1.2.1 cytoplasm
-
 Ovis aries 5737
-
2.1.2.1 mitochondrion
-
 Escherichia coli 5739
-
2.1.2.1 mitochondrion
-
 Homo sapiens 5739
-
2.1.2.1 mitochondrion
-
 Saccharomyces cerevisiae 5739
-
2.1.2.1 mitochondrion
-
 Oryctolagus cuniculus 5739
-
2.1.2.1 mitochondrion
-
 Ovis aries 5739
-
2.1.2.1 mitochondrion
-
 Pisum sativum 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.1 L-serine + tetrahydrofolate Escherichia coli enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate Homo sapiens enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate Saccharomyces cerevisiae enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate Oryctolagus cuniculus enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate Ovis aries enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate Pisum sativum enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Escherichia coli
-
-
-
2.1.2.1 Homo sapiens
-
-
-
2.1.2.1 Oryctolagus cuniculus
-
-
-
2.1.2.1 Ovis aries
-
-
-
2.1.2.1 Pisum sativum
-
-
-
2.1.2.1 Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.1.2.1 side-chain modification in addition to the lysine residue involved in Schiff base formation with the PLP, other residues like arginine, histidine, cysteine and tryptophan essential for catalysis, review Escherichia coli
2.1.2.1 side-chain modification in addition to the lysine residue involved in Schiff base formation with the PLP, other residues like arginine, histidine, cysteine and tryptophan essential for catalysis, review Homo sapiens
2.1.2.1 side-chain modification in addition to the lysine residue involved in Schiff base formation with the PLP, other residues like arginine, histidine, cysteine and tryptophan essential for catalysis, review Saccharomyces cerevisiae
2.1.2.1 side-chain modification in addition to the lysine residue involved in Schiff base formation with the PLP, other residues like arginine, histidine, cysteine and tryptophan essential for catalysis, review Oryctolagus cuniculus
2.1.2.1 side-chain modification in addition to the lysine residue involved in Schiff base formation with the PLP, other residues like arginine, histidine, cysteine and tryptophan essential for catalysis, review Pisum sativum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.2.1 additional information
-
-
 Escherichia coli
2.1.2.1 additional information
-
-
 Homo sapiens
2.1.2.1 additional information
-
-
 Saccharomyces cerevisiae
2.1.2.1 additional information
-
-
 Oryctolagus cuniculus
2.1.2.1 additional information
-
-
 Ovis aries
2.1.2.1 additional information
-
-
 Pisum sativum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 alpha-methylserine + tetrahydrofolate
-
 Escherichia coli D-alanine + 5,10-methylenetetrahydrofolate
-
 ?
2.1.2.1 alpha-methylserine + tetrahydrofolate
-
 Homo sapiens D-alanine + 5,10-methylenetetrahydrofolate
-
 ?
2.1.2.1 alpha-methylserine + tetrahydrofolate
-
 Saccharomyces cerevisiae D-alanine + 5,10-methylenetetrahydrofolate
-
 ?
2.1.2.1 alpha-methylserine + tetrahydrofolate
-
 Oryctolagus cuniculus D-alanine + 5,10-methylenetetrahydrofolate
-
 ?
2.1.2.1 alpha-methylserine + tetrahydrofolate
-
 Ovis aries D-alanine + 5,10-methylenetetrahydrofolate
-
 ?
2.1.2.1 alpha-methylserine + tetrahydrofolate
-
 Pisum sativum D-alanine + 5,10-methylenetetrahydrofolate
-
 ?
2.1.2.1 L-serine + tetrahydrofolate
-
 Escherichia coli glycine + 5,10-methylenetetrahydrofolate + H2O
-
 r
2.1.2.1 L-serine + tetrahydrofolate
-
 Homo sapiens glycine + 5,10-methylenetetrahydrofolate + H2O
-
 r
2.1.2.1 L-serine + tetrahydrofolate
-
 Saccharomyces cerevisiae glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate
-
 Oryctolagus cuniculus glycine + 5,10-methylenetetrahydrofolate + H2O
-
 r
2.1.2.1 L-serine + tetrahydrofolate
-
 Ovis aries glycine + 5,10-methylenetetrahydrofolate + H2O
-
 r
2.1.2.1 L-serine + tetrahydrofolate
-
 Pisum sativum glycine + 5,10-methylenetetrahydrofolate + H2O
-
 r
2.1.2.1 L-serine + tetrahydrofolate enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism Escherichia coli glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism Homo sapiens glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism Saccharomyces cerevisiae glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism Oryctolagus cuniculus glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism Ovis aries glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism Pisum sativum glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 additional information
-
 Homo sapiens ?
-
 ?
2.1.2.1 additional information
-
 Saccharomyces cerevisiae ?
-
 ?
2.1.2.1 additional information
-
 Pisum sativum ?
-
 ?
2.1.2.1 additional information enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate Escherichia coli ?
-
 ?
2.1.2.1 additional information enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate Oryctolagus cuniculus ?
-
 ?
2.1.2.1 additional information enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate Ovis aries ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.2.1 dimer
-
 Escherichia coli
2.1.2.1 dimer
-
 Homo sapiens
2.1.2.1 dimer
-
 Saccharomyces cerevisiae
2.1.2.1 dimer
-
 Ovis aries
2.1.2.1 dimer
-
 Pisum sativum
2.1.2.1 homotetramer actually a dimer of dimers Escherichia coli
2.1.2.1 homotetramer actually a dimer of dimers Homo sapiens
2.1.2.1 homotetramer actually a dimer of dimers Saccharomyces cerevisiae
2.1.2.1 homotetramer actually a dimer of dimers Oryctolagus cuniculus
2.1.2.1 homotetramer actually a dimer of dimers Ovis aries
2.1.2.1 homotetramer actually a dimer of dimers Pisum sativum

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 pyridoxal 5'-phosphate one mol/subunit bound to the epsilon-amino group of lysine Escherichia coli
2.1.2.1 pyridoxal 5'-phosphate one mol/subunit bound to the epsilon-amino group of lysine Homo sapiens
2.1.2.1 pyridoxal 5'-phosphate one mol/subunit bound to the epsilon-amino group of lysine Saccharomyces cerevisiae
2.1.2.1 pyridoxal 5'-phosphate one mol/subunit bound to the epsilon-amino group of lysine Oryctolagus cuniculus
2.1.2.1 pyridoxal 5'-phosphate one mol/subunit bound to the epsilon-amino group of lysine Ovis aries
2.1.2.1 pyridoxal 5'-phosphate one mol/subunit bound to the epsilon-amino group of lysine Pisum sativum
2.1.2.1 pyridoxal 5'-phosphate important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis Escherichia coli
2.1.2.1 pyridoxal 5'-phosphate important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis Homo sapiens
2.1.2.1 pyridoxal 5'-phosphate important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis Saccharomyces cerevisiae
2.1.2.1 pyridoxal 5'-phosphate important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis Oryctolagus cuniculus
2.1.2.1 pyridoxal 5'-phosphate important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis Ovis aries
2.1.2.1 pyridoxal 5'-phosphate important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis Pisum sativum