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Literature summary extracted from

  • Na, I.; Catena, D.; Kong, M.J.; Ferreira, G.C.; Uversky, V.N.
    Anti-correlation between the dynamics of the active site loop and C-terminal tail in relation to the homodimer asymmetry of the mouse erythroid 5-aminolevulinate synthase (2018), Int. J. Mol. Sci., 19, 1899 .
    View publication on PubMedView publication on EuropePMC

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
-
-

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 isoform Mus musculus

Cofactor

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

General Information

EC Number General Information Comment Organism
2.3.1.37 malfunction genetic mutations in the erythroid-specific isoform ALAS2 are associated with two inherited blood disorders, X-linked sideroblastic anemia (XLSA) and X-linked protoporphyria (XLPP). XLSA is caused by diminished ALAS2 activity leading to decreased ALA and heme syntheses and ultimately ineffective erythropoiesis, whereas XLPP results from gain-of-function ALAS2 mutations and consequent overproduction of protoporphyrin IX and increase in Zn2+-protoporphyrin levels Mus musculus