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Proteins/UNIPROT:P22557
Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products. Contributes significantly to heme formation during erythropoiesis..
[Isoform 3]: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products. Catalytic activity is 75-85% of isoform 1 activity..
[Isoform 4]: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products. Catalytic activity is 65-75% of isoform 1 activity..
Function from UniProtKB (P22557), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 1 · substrate of
1 compound
1 compound.
0 reported routes1 assembled route
2 rows
43 statements
43 statements · 7 reference databases · Subject: ALAS2 · Sources: Bgee, Hetionet, Human-GEM, Reactome, Rhea, UniProt, WikiPathways
3 reactions
MAM00630m+proton5-aminolevulinic acid+carbon dioxide
Catalysed by ALAS1 or ALAS2 or CPNE7
Reaction pageLeft to rightBalancedEC 2.3.1.37mitochondrial matrix
Human-GEM MAR04657CC BY 4.0Reference data
glycine+proton+CHEBI:153805-aminolevulinic acid+carbon dioxide+CHEBI:1146900
6 names
Resolves to: ALAS2
Reaction pageLeft to rightBalancedEC 2.3.1.37mitochondrial matrix
Human-GEM MAR04742CC BY 4.0Reference data
succinyl-CoA+glycine+hydron5-aminolevulinate+carbon dioxide+coenzyme A(4-)
Reaction pageLeft to rightBalanced
Rhea RHEA:12921CC BY 4.0Reference data