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Literature summary for 2.3.1.37 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
Search for more literature for 2.3.1.37

General Stability

General Stability Organism
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
succinyl-CoA + glycine Mus musculus
-
 5-aminolevulinate + CoA + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus P08680
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
erythroid cell
-
 Mus musculus
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homodimer
-
 Mus musculus

Synonyms

Synonyms Comment Organism
ALAS2
-
 Mus musculus

Cofactor

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