ExplorEnz: EC 2.3.1.37

Your query returned 1 entry. Printable version

2.3.1.37

Accepted name:

5-aminolevulinate synthase

Reaction:

succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO₂

For diagram of porphyrin biosynthesis (early stages), click here

Other name(s):

ALAS; ALA synthase; α-aminolevulinic acid synthase; δ-aminolevulinate synthase; δ-aminolevulinate synthetase; δ-aminolevulinic acid synthase; δ-aminolevulinic acid synthetase; δ-aminolevulinic synthetase; 5-aminolevulinate synthetase; 5-aminolevulinic acid synthetase; ALA synthetase; aminolevulinate synthase; aminolevulinate synthetase; aminolevulinic acid synthase; aminolevulinic acid synthetase; aminolevulinic synthetase

Systematic name:

succinyl-CoA:glycine C-succinyltransferase (decarboxylating)

Comments:

A pyridoxal 5′-phosphate protein. The enzyme, which catalyses the first reaction of a tetrapyrrole biosynthesis pathway, is found in alphaproteobacteria and most eukaryotes, except plants. A genetically distinct form (ALAS2) is found in erythrocytes. The enzyme is also found in some bacteriophages from aquatic environments.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9037-14-3

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 (1990) 207–214. [PMID: 2347585]
2.	Kikuchi, G., Kumar, A., Talmage, P. and Shemin, D. The enzymatic synthesis of δ-aminolevulinic acid. J. Biol. Chem. 233 (1958) 1214–1219. [PMID: 13598764]
3.	Ramaswamy, N.K. and Nair, P.M. δ-Aminolevulinic acid synthetase from cold-stored potatoes. Biochim. Biophys. Acta 293 (1973) 269–277. [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 (1972) 4126–4131. [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 (1972) 4132–4137. [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 (1973) 389–403. [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 (1971) 6880–6885. [PMID: 5315997]
8.	Wegner, H., Roitman, S., Kupczok, A., Braun, V., Woodhouse, J.N., Grossart, H.P., Zehner, S., Beja, O. and Frankenberg-Dinkel, N. Identification of Shemin pathway genes for tetrapyrrole biosynthesis in bacteriophage sequences from aquatic environments. Nat. Commun. 15:8783 (2024). [DOI] [PMID: 39406702]

[EC 2.3.1.37 created 1972]