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