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Literature summary extracted from

  • Jackson, L.K.; Baldwin, J.; Akella, R.; Goldsmith, E.J.; Phillips, M.A.
    Multiple active site conformations revealed by distant site mutation in ornithine decarboxylase (2004), Biochemistry, 43, 12990-12999.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.17 mutant K294A in complex with substrate analogue D-ornithine Trypanosoma brucei

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.17 K294A mutation increases the disorder of residues Leu166 - Ala172 and increases the population of inactive conformations Trypanosoma brucei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.17 0.37
-
 L-ornithine wild-type, pH 8.0, 37°C Trypanosoma brucei
4.1.1.17 43
-
 L-ornithine mutant K294A, pH 8.0, 37°C Trypanosoma brucei

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.17 Trypanosoma brucei P07805
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.17 L-ornithine
-
 Trypanosoma brucei putrescine + CO2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.17 3.5
-
 L-ornithine mutant K294A, pH 8.0, 37°C Trypanosoma brucei
4.1.1.17 15.4
-
 L-ornithine wild-type, pH 8.0, 37°C Trypanosoma brucei

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.17 pyridoxal 5'-phosphate apparent Km-value in wild-type 150 nM, in mutant K294A 36 microM Trypanosoma brucei