EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.37 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics, overview | Mus musculus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.37 | succinyl-CoA + glycine | Mus musculus | - |
5-aminolevulinate + CoA + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.37 | Mus musculus | P08680 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.37 | succinyl-CoA + glycine | - |
Mus musculus | 5-aminolevulinate + CoA + CO2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.37 | ALAS2 | - |
Mus musculus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.37 | 37 | - |
assay at | Mus musculus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.37 | additional information | - |
the secondary structure of the enzyme is mostly resilient to temperature changes, overview | Mus musculus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.37 | 7.5 | 8.5 | - |
Mus musculus |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.37 | 1 | 3 | inactive at | Mus musculus |
2.3.1.37 | 9.5 | 10 | poorly active at | Mus musculus |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.37 | additional information | - |
the secondary structure of the enzyme is mostly resilient to pH changes. Partial unfolding is observed at pH 2.0, but further decreasing pH results in acid-induced refolding of the secondary structure to nearly native levels. The tertiary structure rigidity is lost under acidic and specific alkaline conditions, pH 10.5 and pH 9.5 at 37°C, where ALAS populates a molten globule state. As the enzyme becomes less structured with increased alkalinity, the chiral environment of the internal aldimine is also modified. Under acidic conditions, the pyridoxal 5-phosphate cofactor dissociates from the enzyme. Reaction with 8-anilino-1-naphthalenesulfonic acid corroborates increased exposure of hydrophobic clusters in the alkaline and acidic molten globules, far-UV and near-UV circular dichroism study, detailed overview. The alkaline molten globule state of ALAS is catalytically active | Mus musculus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.37 | pyridoxal 5'-phosphate | dependent on | Mus musculus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.1.37 | metabolism | the enzyme catalyzes the first step of heme formation | Mus musculus |