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Literature summary for 2.3.1.37 extracted from

  • Gong, J.; Kay, C.J.; Barber, M.J.; Ferreira, G.C.
    Mutations at a glycine loop in aminolevulinate synthase affect pyridoxal phosphate cofactor binding and catalysis (1996), Biochemistry, 35, 14109-14117.
    View publication on PubMed
Search for more literature for 2.3.1.37

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutants in Escherichia coli Mus musculus

Protein Variants

Protein Variants Comment Organism
G142C glycine-rich motif mutant, 15fold increased dissociation constant value for binding of cofactor pyridoxal 5'-phosphate, 6% turnover compared to the wild-type, 4fold increase of Km-value for glycine Mus musculus
G144A glycine-rich motif mutant, 8.5fold increased dissociation constant value for binding of cofactor pyridoxal 5'-phosphate, 43% turnover compared to the wild-type, unaltered Km-values for the substrates Mus musculus
G144S glycine-rich motif mutant, 8fold increased dissociation constant value for binding of cofactor pyridoxal 5'-phosphate, 39% turnover compared to the wild-type, unaltered Km-values for the substrates Mus musculus
G144T glycine-rich motif mutant, 24.5fold increased dissociation constant value for binding of cofactor pyridoxal 5'-phosphate, 21% turnover compared to the wild-type, unaltered Km-values for the substrates Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00064
-
 succinyl-CoA recombinant mutant G144A Mus musculus
0.0012
-
 succinyl-CoA recombinant erythroid isoform and mutant G144S Mus musculus
0.0019
-
 succinyl-CoA recombinant mutant G144T Mus musculus
0.002
-
 succinyl-CoA recombinant mutant G142C Mus musculus
0.002
-
 succinyl-CoA recombinant mutant G142C Rattus norvegicus
6.2
-
 glycine recombinant mutant G144T Mus musculus
9.3
-
 glycine recombinant mutant G144A Mus musculus
11.9
-
 glycine recombinant mutant G144S Mus musculus
12.5
-
 glycine recombinant erythroid isoform Mus musculus
52.2
-
 glycine recombinant mutant G142C Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant 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
a
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 pyridoxal 5'-phosphate binding site, sequence and function of glycine-rich motif Mus musculus
a

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
-
 Rattus norvegicus 5-aminolevulinate + CoA + CO2
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
-
 Rattus norvegicus
additional information
-
 thermal stability of glycine-rich motif mutants is reduced compared to the wild-type Mus musculus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0183
-
 succinyl-CoA recombinant erythroid isoform mutant G142C Mus musculus
0.0633
-
 succinyl-CoA recombinant erythroid isoform mutant G144T Mus musculus
0.12
-
 succinyl-CoA recombinant erythroid isoform mutant G144S Mus musculus
0.132
-
 succinyl-CoA recombinant erythroid isoform mutant G144A Mus musculus
0.308
-
 succinyl-CoA recombinant erythroid isoform Mus musculus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Mus musculus
pyridoxal 5'-phosphate
-
 Rattus norvegicus