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Literature summary for 2.1.2.1 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

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

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Homo sapiens

Inhibitors

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

Localization

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

Natural Substrates/ Products (Substrates)

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

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

Posttranslational Modification

Posttranslational Modification Comment Organism
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
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
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
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
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]

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

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate one mol/subunit bound to the epsilon-amino group of lysine Escherichia coli
pyridoxal 5'-phosphate one mol/subunit bound to the epsilon-amino group of lysine Homo sapiens
pyridoxal 5'-phosphate one mol/subunit bound to the epsilon-amino group of lysine Saccharomyces cerevisiae
pyridoxal 5'-phosphate one mol/subunit bound to the epsilon-amino group of lysine Oryctolagus cuniculus
pyridoxal 5'-phosphate one mol/subunit bound to the epsilon-amino group of lysine Ovis aries
pyridoxal 5'-phosphate one mol/subunit bound to the epsilon-amino group of lysine Pisum sativum
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
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
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
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
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
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