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Literature summary extracted from

  • Tan, D.; Ferreira, G.C.
    Active site of 5-aminolevulinate synthase resides at the subunit interface. Evidence from in vivo heterodimer formation (1996), Biochemistry, 35, 8934-8941.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.37 expression of His-tagged wild-type, mutant K313A, mutant R149A and dimer mutant K313A/R149A, each subunit from 1 plasmid, in Escherichia coli hemA- mutant Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.37 C145R mutant strain G205, lacks enzyme activity, but can complement mutant strain Ole3 with mutation G344C Saccharomyces cerevisiae
2.3.1.37 K313A mutation site located at the active site of 1 subunit, functional complementation of Escherichia coli mutant strain hemA-, no activity Mus musculus
2.3.1.37 K313A/R149A each mutation site located on 1 subunit, 2 plasmids, coexpression of the dimer in Escherichia coli hemA-, functional complementation, 26% activity compared to wild-type Mus musculus
2.3.1.37 N157Y/N162S mutant strain G101, lacks enzyme activity, but can complement mutant strain G220 with mutation T452R Saccharomyces cerevisiae
2.3.1.37 R149A mutation site located at the active site of 1 subunit, functional complementation of Escherichia coli mutant strain hemA-, no activity Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.37 1.52
-
 succinyl-CoA recombinant mutant dimer K149A/K313A Mus musculus
2.3.1.37 1.82
-
 succinyl-CoA
-
 Mus musculus
2.3.1.37 6.95
-
 glycine recombinant mutant dimer K149A/K313A Mus musculus
2.3.1.37 8.39
-
 glycine
-
 Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.37 additional information
-
 amino acid sequence alignment Mus musculus
2.3.1.37 additional information
-
 amino acid sequence alignment Saccharomyces cerevisiae
2.3.1.37 56000
-
 2 * 56000, SDS-PAGE Mus musculus
2.3.1.37 112000
-
 gel filtration Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.37 succinyl-CoA + glycine Mus musculus rate-limiting enzyme of heme biosynthesis 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine Saccharomyces cerevisiae rate-limiting enzyme of heme biosynthesis 5-aminolevulinate + CoA + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.37 Mus musculus
-
 gene hemA
-
2.3.1.37 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.37 recombinant of His-tagged wild-type and mutants from E. coli Mus musculus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 Tyr121, Asp279, Arg439, and Lys313 are involved in substrate and cofactor binding, mechanism, subunit localisation Mus musculus
a
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 the active site is located at the subunit interface and contains catalytically essential residues from the two subunits Mus musculus
a
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 the active site is located at the subunit interface and contains catalytically essential residues from the two subunits Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.37 succinyl-CoA + glycine
-
 Mus musculus 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine
-
 Saccharomyces cerevisiae 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine rate-limiting enzyme of heme biosynthesis Mus musculus 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine rate-limiting enzyme of heme biosynthesis Saccharomyces cerevisiae 5-aminolevulinate + CoA + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.37 dimer
-
 Saccharomyces cerevisiae
2.3.1.37 dimer 2 * 56000, SDS-PAGE Mus musculus
2.3.1.37 More the active site is located at the subunit interface and contains catalytically essential residues from the two subunits Mus musculus
2.3.1.37 More the active site is located at the subunit interface and contains catalytically essential residues from the two subunits Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.37 pyridoxal 5'-phosphate
-
 Mus musculus
2.3.1.37 pyridoxal 5'-phosphate
-
 Saccharomyces cerevisiae