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Literature summary for 2.3.1.37 extracted from

  • Zhang, J.; Cheltsov, A.V.; Ferreira, G.C.
    Conversion of 5-aminolevulinate synthase into a more active enzyme by linking the two subunits: spectroscopic and kinetic properties (2005), Protein Sci., 14, 1190-1200.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.37

Protein Variants

Protein Variants Comment Organism
additional information linkage of two subunits into a single polypeptide chain dimer 2XALAS, results in enzyme with about 7fold greater turnover number than wild-type and with greater A410/A330 ratio Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.45
-
 succinyl-CoA pH 7.5, 30°C, mutant 2XALAS Mus musculus
0.63
-
 succinyl-CoA pH 7.5, 20°C, mutant 2XALAS Mus musculus
2 3 glycine pH 7.5, 30°C, wild-type Mus musculus
2.3
-
 succinyl-CoA pH 7.5, 30°C, wild-type Mus musculus
11
-
 succinyl-CoA pH 7.5, 20°C, wild-type Mus musculus
11.7
-
 glycine pH 7.5, 20°C, mutant 2XALAS Mus musculus
14
-
 glycine pH 7.5, 20°C, wild-type Mus musculus
16.7
-
 glycine pH 7.5, 30°C, mutant 2XALAS Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
 erythroid specific isoform
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
succinyl-CoA + glycine
-
 Mus musculus 5-aminolevulinate + CoA + CO2
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.016
-
 glycine pH 7.5, 20°C, wild-type Mus musculus
0.11
-
 glycine pH 7.5, 20°C, mutant 2XALAS Mus musculus
0.167
-
 glycine pH 7.5, 30°C, wild-type Mus musculus
0.92
-
 glycine pH 7.5, 30°C, mutant 2XALAS Mus musculus