EC 2.3.1.37 - 5-aminolevulinate synthase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 2.3.1.37

Names

Accepted name:
5-aminolevulinate synthase
Other names:
5-aminolevulinate synthetase
5-aminolevulinic acid synthetase
α-aminolevulinic acid synthase
δ-aminolevulinate synthase
δ-aminolevulinate synthetase
δ-aminolevulinic acid synthase
δ-aminolevulinic acid synthetase
δ-aminolevulinic synthetase
ALA synthase
ALA synthetase
ALAS
aminolevulinate synthase
aminolevulinate synthetase
aminolevulinic acid synthase
aminolevulinic acid synthetase
aminolevulinic synthetase
Systematic name:
succinyl-CoA:glycine C-succinyltransferase (decarboxylating)

Reaction

Cofactor

Comments:

A pyridoxal-phosphate protein. The enzyme in erythrocytes is genetically distinct from that in other tissues.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00518
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003870
CAS Registry Number: 9037-14-3
UniProtKB/Swiss-Prot: (40) [show] [UniProt]

References

  1. Bishop, D.F., Henderson, A.S. and Astrin, K.H.
    Human δ-aminolevulinate synthase - assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X-chromosome.
    Genomics 7: 207-214 (1990).
  2. Kikuchi, G., Kumar, A., Talmage, P. and Shemin, D.
    The enzymatic synthesis of δ-aminolevulinic acid.
    J. Biol. Chem. 233: 1214-1219 (1958).
  3. Ramaswamy, N.K. and Nair, P.M.
    δ-Aminolevulinic acid synthetase from cold-stored potatoes.
    Biochim. Biophys. Acta 293: 269-277 (1973). [PMID: 4685279]
  4. Scholnick, P.L., Hammaker, L.E. and Marver, H.S.
    Soluble δ-aminolevulinic acid synthetase of rat liver. I. Some properties of the partially purified enzyme.
    J. Biol. Chem. 247: 4126-4131 (1972). [PMID: 4624703]
  5. Scholnick, P.L., Hammaker, L.E. and Marver, H.S.
    Soluble δ-aminolevulinic acid synthetase of rat liver. II. Studies related to the mechanism of enzyme action and hemin inhibition.
    J. Biol. Chem. 247: 4132-4137 (1972). [PMID: 5035685]
  6. Tait, G.H.
    Aminolaevulinate synthetase of Micrococcus denitrificans. Purification and properties of the enzyme, and the effect of growth conditions on the enzyme activity in cells.
    Biochem. J. 131: 389-403 (1973). [PMID: 4722442]
  7. Warnick, G.R. and Burnham, B.F.
    Regulation of porphyrin biosynthesis. Purification and characterization of δ-aminolevulinic acid synthase.
    J. Biol. Chem. 246: 6880-6885 (1971). [PMID: 5315997]

[EC 2.3.1.37 created 1972]