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Literature summary extracted from

  • Stojanovski, B.M.; Ferreira, G.C.
    Asn-150 of murine erythroid 5-aminolevulinate synthase modulates the catalytic balance between the rates of the reversible reaction (2015), J. Biol. Chem., 290, 30750-30761.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.37 recombinant expression of wild-type and mutant enzymes Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.37 additional information selection of functional mALAS2 variants from the Thr148/Asn150 library of constructs is accomplished by reversing the 5-aminolevulinate auxotrophic phenotype of Escherichia coli hemA (HU227) cells Mus musculus
2.3.1.37 N150A site-directed mutagenesis, the mutation significantly reduces the rate of quinonoid intermediate formation in the forward direction Mus musculus
2.3.1.37 N150F site-directed mutagenesis, the mutation significantly reduces the rate of quinonoid intermediate formation in the forward direction, while increasing the reverse reaction rate Mus musculus
2.3.1.37 N150G site-directed mutagenesis, the mutation significantly reduces the rate of quinonoid intermediate formation in the forward direction Mus musculus
2.3.1.37 N150H site-directed mutagenesis, the mutation significantly reduces the rate of quinonoid intermediate formation in the forward direction, while increasing the reverse reaction rate Mus musculus
2.3.1.37 N150W site-directed mutagenesis, the mutation significantly reduces the rate of quinonoid intermediate formation in the forward direction Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.37 additional information
-
 additional information pre-steady-state and steady-state kinetics of wild-type and mutant enzymes, stopped-flow measurements, single and mutiple turnover rates, equilibrium dissociation constants, binding isotherms, detailed overview Mus musculus
2.3.1.37 0.0011
-
 succinyl-CoA mutant N150W, pH 7.5, 18°C Mus musculus
2.3.1.37 0.0012
-
 succinyl-CoA mutant N150H, pH 7.5, 18°C Mus musculus
2.3.1.37 0.0021
-
 succinyl-CoA mutant N150G, pH 7.5, 18°C Mus musculus
2.3.1.37 0.0022
-
 succinyl-CoA mutant N150F, pH 7.5, 18°C Mus musculus
2.3.1.37 0.0023
-
 succinyl-CoA wild-type enzyme, pH 7.5, 18°C Mus musculus
2.3.1.37 0.0038
-
 succinyl-CoA mutant N150A, pH 7.5, 18°C Mus musculus
2.3.1.37 2 3 glycine wild-type enzyme, pH 7.5, 18°C Mus musculus
2.3.1.37 11
-
 glycine mutant N150G, pH 7.5, 18°C Mus musculus
2.3.1.37 12
-
 glycine mutant N150F, pH 7.5, 18°C Mus musculus
2.3.1.37 16
-
 glycine mutant N150A, pH 7.5, 18°C Mus musculus
2.3.1.37 16
-
 glycine mutant N150H, pH 7.5, 18°C Mus musculus
2.3.1.37 39
-
 glycine mutant N150W, pH 7.5, 18°C 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
-
 5-aminolevulinate + CoA + CO2
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.37 Mus musculus P08680
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.37 recombinant wild-type and mutant enzymes Mus musculus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 proposed chemical mechanism of enzyme ALAS2 via (I) internal aldimine complex, (II) glycine-external aldimine, (III) quinonoid intermediate I, (IV) glycine-succinyl-CoA condensation intermediate, (V) 2-amino-3-ketoadipate intermediate, (VI) enol intermediate, (VII) quinonoid intermediate II, and (VIII) 5-aminolevulinate-external aldimine Mus musculus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.37 additional information the wild-type enzyme catalyzes the conversion of 5-aminolevulinate into the quinonoid intermediate at a rate 6.3fold slower than the formation of the same quinonoid intermediate from glycine and succinyl-CoA. The mutant N150F enzyme catalyzes the forward reaction at a 1.2fold faster rate than that of the reverse reaction, and the N150H variant reverses the rate values with a 1.7fold faster rate for the reverse reaction than that for the forward reaction. Steric constraints imposed by the active site of wild-type enzyme ALAS contribute toward the amino acid substrate specificity Mus musculus ?
-
 ?
2.3.1.37 succinyl-CoA + glycine
-
 Mus musculus 5-aminolevulinate + CoA + CO2
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.3.1.37 ALAS2
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.37 18 37 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 0.04
-
 succinyl-CoA mutant N150H, pH 7.5, 18°C Mus musculus
2.3.1.37 0.06
-
 succinyl-CoA mutant N150F, pH 7.5, 18°C Mus musculus
2.3.1.37 0.09
-
 succinyl-CoA mutant N150W, pH 7.5, 18°C Mus musculus
2.3.1.37 0.13
-
 succinyl-CoA mutant N150A, pH 7.5, 18°C Mus musculus
2.3.1.37 0.15
-
 succinyl-CoA mutant N150G, pH 7.5, 18°C Mus musculus
2.3.1.37 0.16
-
 succinyl-CoA wild-type enzyme, pH 7.5, 18°C Mus musculus

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 dependent on Mus musculus

General Information

EC Number General Information Comment Organism
2.3.1.37 metabolism 5-aminolevulinate synthase catalyzes the initial step of mammalian heme biosynthesis Mus musculus
2.3.1.37 additional information residue Asn150 is essential for establishing a catalytic balance between the forward and reverse reactions Mus musculus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.37 0.0023
-
 glycine mutant N150W, pH 7.5, 18°C Mus musculus
2.3.1.37 0.0025
-
 glycine mutant N150H, pH 7.5, 18°C Mus musculus
2.3.1.37 0.005
-
 glycine mutant N150F, pH 7.5, 18°C Mus musculus
2.3.1.37 0.007
-
 glycine wild-type enzyme, pH 7.5, 18°C Mus musculus
2.3.1.37 0.0081
-
 glycine mutant N150A, pH 7.5, 18°C Mus musculus
2.3.1.37 0.0136
-
 glycine mutant N150G, pH 7.5, 18°C Mus musculus
2.3.1.37 27
-
 succinyl-CoA mutant N150F, pH 7.5, 18°C Mus musculus
2.3.1.37 33
-
 succinyl-CoA mutant N150H, pH 7.5, 18°C Mus musculus
2.3.1.37 34
-
 succinyl-CoA mutant N150A, pH 7.5, 18°C Mus musculus
2.3.1.37 70
-
 succinyl-CoA wild-type enzyme, pH 7.5, 18°C Mus musculus
2.3.1.37 71
-
 succinyl-CoA mutant N150G, pH 7.5, 18°C Mus musculus
2.3.1.37 82
-
 succinyl-CoA mutant N150W, pH 7.5, 18°C Mus musculus