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Literature summary extracted from

  • Abu-Farha, M.; Niles, J.; Willmore, W.G.
    Erythroid-specific 5-aminolevulinate synthase protein is stabilized by low oxygen and proteasomal inhibition (2005), Biochem. Cell Biol., 83, 620-630.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.37
-
Homo sapiens

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 Homo sapiens ALAS2 synthesizes heme specifically for haemoglobin 5-aminolevulinate + CoA + CO2
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.37 Homo sapiens
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
2.3.1.37 ALAS2 is broken down under normoxic conditions by the proteasome Homo sapiens

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.1.37 additional information ALAS2 is hydroxylated under normoxic conditions Homo sapiens
2.3.1.37 ubiquitinylation ALAS2 appears to be ubiquitinated as rapidly as at is produced Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.37 K-562 cell ALAS2 is expressed exclusively in erythroid cells Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.37 succinyl-CoA + glycine ALAS2 synthesizes heme specifically for haemoglobin Homo sapiens 5-aminolevulinate + CoA + CO2
-
?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.37 ALAS2
-
Homo sapiens