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Literature summary for 2.3.1.37 extracted from

  • Kadirvel, S.; Furuyama, K.; Harigae, H.; Kaneko, K.; Tamai, Y.; Ishida, Y.; Shibahara, S.
    The carboxyl-terminal region of erythroid-specific 5-aminolevulinate synthase acts as an intrinsic modifier for its catalytic activity and protein stability (2012), Exp. Hematol., 40, 477-486.e1.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in eukaryotic cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
M567I mutant shows 25% of wild-type activity, while its half-life is longer than that of wild-type Homo sapiens
additional information the deletion of 33 amino acids at C-terminal end results in higher catalytic activity both in vitro and in vivo with the longer half-life compared to wild-type Homo sapiens
S568G mutant shows decreased catalytic activity in vitro (20% compared to wild-type), but a higher half-life compared to those of wild-type ALAS2 Homo sapiens
V562A mutant shows a higher catalytic activity in vitro, but a shorter half-life in vivo compared to those of wild-type ALAS2 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
5-aminolevulinate synthase
-
Homo sapiens
ALAS2
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Homo sapiens