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Literature summary for 4.1.1.17 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
Search for more literature for 4.1.1.17

Crystallization (Commentary)

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

Protein Variants

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Trypanosoma brucei P07805
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

Cofactor

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