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Literature summary extracted from

  • Turbeville, T.D.; Zhang, J.; Adams, W.C.; Hunter, G.A.; Ferreira, G.C.
    Functional asymmetry for the active sites of linked 5-aminolevulinate synthase and 8-amino-7-oxononanoate synthase (2011), Arch. Biochem. Biophys., 511, 107-117.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.37 expressed in Escherichia coli Mus musculus
2.3.1.47 His-tagged protein and murine 5-aminolevulinate synthase-fusion protein (single chain chimeric dimer) expressed in Escherichia coli HU227, R872 and DH5alpha Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.37 additional information a single chain dimeric ALAS variant is created, in which one of the two active sites harbors a K313A mutation eliminating measurable enzyme activity in order to investigate the unusual enhanced enzymatic activity resulting from linking ALAS dimmers. The two active sites in ALAS/ALAS differentially contribute to the enhanced activity of the enzyme, even though the amount of ALA produced during the first turnover is identical in both active sites. The kcat values of the K313A variants differ significantly depending on which of the two active sites harbors the mutation Mus musculus
2.3.1.47 K236A active site lysine involved in the Schiff base linkage with the PLP cofactor Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.37 0.00032
-
 glycine pH 7.5, 30°C, ALAS(K313A mutant)/ALAS Mus musculus
2.3.1.37 0.00045
-
 glycine pH 7.5, 30°C, ALAS/ALAS Mus musculus
2.3.1.37 0.0018
-
 glycine pH 7.5, 30°C, ALAS/ALAS (K313A mutant) Mus musculus
2.3.1.37 0.002
-
 glycine pH 7.5, 30°C, ALAS Mus musculus
2.3.1.37 2 3 glycine pH 7.5, 30°C, ALAS Mus musculus
2.3.1.37 11.8
-
 glycine pH 7.5, 30°C, ALAS/ALAS (K313A mutant) Mus musculus
2.3.1.37 14.8
-
 glycine pH 7.5, 30°C, ALAS(K313A mutant)/ALAS Mus musculus
2.3.1.37 16.7
-
 glycine pH 7.5, 30°C, ALAS/ALAS Mus musculus
2.3.1.47 0.01
-
 pimeloyl-CoA 5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30°C Escherichia coli
2.3.1.47 0.025
-
 pimeloyl-CoA wild type protein, pH not specified in the publication, temperature not specified in the publication Escherichia coli
2.3.1.47 0.25
-
 L-alanine 5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30°C Escherichia coli
2.3.1.47 0.5
-
 L-alanine wild type protein, pH not specified in the publication, temperature not specified in the publication Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.37 Mus musculus
-
-
-
2.3.1.47 Escherichia coli P12998
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.47 from Escherichia coli DH5alpha, ammonium sulfate fractionation, gel filtration, hydrophobic interaction chromatography, ion exchange chromatography Escherichia coli

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
-
 ?
2.3.1.47 L-alanine + pimeloyl-CoA
-
 Escherichia coli 8-amino-7-oxononanoate + CoA + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.47 homodimer 2 x 40000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.3.1.37 5-aminolevulinate synthase
-
 Mus musculus
2.3.1.37 ALAS
-
 Mus musculus
2.3.1.47 8-amino-7-oxononanoate synthase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.37 30
-
 assay at Mus musculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.37 0.07
-
 glycine pH 7.5, 30°C, ALAS/ALAS (K313A mutant) Mus musculus
2.3.1.37 0.166
-
 glycine pH 7.5, 30°C, ALAS Mus musculus
2.3.1.37 0.36
-
 glycine pH 7.5, 30°C, ALAS(K313A mutant)/ALAS Mus musculus
2.3.1.37 0.92
-
 glycine pH 7.5, 30°C, ALAS/ALAS Mus musculus
2.3.1.47 0.028
-
 L-alanine 5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30°C Escherichia coli
2.3.1.47 0.06
-
 L-alanine wild type protein, pH not specified in the publication, temperature not specified in the publication Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.37 7.5
-
 assay at Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.37 pyridoxal 5'-phosphate
-
 Mus musculus
2.3.1.47 pyridoxal 5'-phosphate
-
 Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.47 0.11
-
 L-alanine 5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30°C Escherichia coli
2.3.1.47 0.12
-
 L-alanine wild type protein, pH not specified in the publication, temperature not specified in the publication Escherichia coli
2.3.1.47 2.33
-
 pimeloyl-CoA wild type protein, pH not specified in the publication, temperature not specified in the publication Escherichia coli
2.3.1.47 2.67
-
 pimeloyl-CoA 5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30°C Escherichia coli