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Literature summary extracted from

  • Stojanovski, B.M.; Breydo, L.; Hunter, G.A.; Uversky, V.N.; Ferreira, G.C.
    Catalytically active alkaline molten globular enzyme: effect of pH and temperature on the structural integrity of 5-aminolevulinate synthase (2014), Biochim. Biophys. Acta, 1844, 2145-2154.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.37 Mus musculus P08680
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.37 succinyl-CoA + glycine
-
 Mus musculus 5-aminolevulinate + CoA + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.37 ALAS2
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.37 37
-
 assay at Mus musculus

Temperature Stability [°C]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.37 7.5 8.5
-
 Mus musculus

pH Range

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

pH Stability

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

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.37 pyridoxal 5'-phosphate dependent on Mus musculus

General Information

EC Number General Information Comment Organism
2.3.1.37 metabolism the enzyme catalyzes the first step of heme formation Mus musculus