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Literature summary extracted from

  • Stojanovski, B.M.; Breydo, L.; Uversky, V.N.; Ferreira, G.C.
    The unfolding pathways of the native and molten globule states of 5-aminolevulinate synthase (2016), Biochem. Biophys. Res. Commun., 480, 321-327 .
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.3.1.37 in the presence of denaturing guanidine hydrochloride concentrations at pH 10.5, the rate of enzyme denaturation is 3times faster than at pH 7.5. Both guanidine hydrochloride- and temperature-induced denaturation reduce the enzyme stability at pH 10.5 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
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.37
-
 Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.37 erythroid cell
-
 Mus musculus
-

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
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.37 homodimer
-
 Mus musculus

Synonyms

EC Number Synonyms Comment Organism
2.3.1.37 ALAS2
-
 Mus musculus

Cofactor

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