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Literature summary extracted from

  • Bertoldi, M.; Carbone, V.; Borri Voltattorni, C.
    Ornithine and glutamate decarboxylases catalyze an oxidative deamination of their a-methyl substrates (1999), Biochem. J., 342, 509-512.
No PubMed abstract available

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.15 1.04
-
 L-alpha-Methylglutamate pH 4.6, 25°C Escherichia coli
4.1.1.17 0.092
-
 alpha-Methylornithine 25°C, pH 5.8 Lactobacillus sp. 30a

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.15 Escherichia coli
-
-
-
4.1.1.17 Lactobacillus sp. 30a
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.17
-
 Lactobacillus sp. 30a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.15 L-alpha-methylglutamate + O2
-
 Escherichia coli laevulinic acid + NH3
-
 ?
4.1.1.17 alpha-methylornithine
-
 Lactobacillus sp. 30a 2-methyl-1-pyrroline + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.17 ODC
-
 Lactobacillus sp. 30a

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.15 9.53
-
 L-alpha-Methylglutamate pH 4.6, 25°C Escherichia coli
4.1.1.17 0.02
-
 alpha-Methylornithine 25°C, pH 5.8 Lactobacillus sp. 30a