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Literature summary for 2.3.1.37 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)

Cloned (Comment) Organism
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Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
succinyl-CoA + glycine Homo sapiens ALAS2 synthesizes heme specifically for haemoglobin 5-aminolevulinate + CoA + CO2
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Oxidation Stability

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

Posttranslational Modification

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

Source Tissue

Source Tissue Comment Organism Textmining
K-562 cell ALAS2 is expressed exclusively in erythroid cells Homo sapiens
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Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
ALAS2
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Homo sapiens