Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.37 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)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
C145R mutant strain G205, lacks enzyme activity, but can complement mutant strain Ole3 with mutation G344C Saccharomyces cerevisiae
K313A mutation site located at the active site of 1 subunit, functional complementation of Escherichia coli mutant strain hemA-, no activity Mus musculus
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
N157Y/N162S mutant strain G101, lacks enzyme activity, but can complement mutant strain G220 with mutation T452R Saccharomyces cerevisiae
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]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Mus musculus
-
gene hemA
-
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 Tyr121, Asp279, Arg439, and Lys313 are involved in substrate and cofactor binding, mechanism, subunit localisation Mus musculus
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
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

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

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