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Literature summary for 1.4.99.6 extracted from

  • Yuan, H.; Fu, G.; Brooks, P.T.; Weber, I.; Gadda, G.
    Steady-state kinetic mechanism and reductive half-reaction of D-arginine dehydrogenase from Pseudomonas aeruginosa (2010), Biochemistry, 49, 9542-9550.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
D-arginine pH 8.7, 25°C Pseudomonas aeruginosa
8.8
-
D-histidine pH 8.7, 25°C Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9HXE3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-arginine + phenazine methosulfate fast substrate D-arginine leads to a dead-end complex of the reduced enzyme and the substrate at high concentrations of D-arginine yielding substrate inhibition, while the overall turnover is partially limited by the release of the iminoarginine product Pseudomonas aeruginosa 5-guanidino-2-oxopentanoate + NH3 + reduced phenazine methosulfate overall reaction ?
D-histidine + phenazine methosulfate slow substrate, the initial Michaelis complex undergoes an isomerization involving multiple conformations that are not all equally catalytically competent for the subsequent oxidation reaction, while the overall turnover is at least partially limited by flavin reduction Pseudomonas aeruginosa 3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced phenazine methosulfate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
35
-
D-histidine pH 8.7, 25°C Pseudomonas aeruginosa
204
-
D-arginine pH 8.7, 25°C Pseudomonas aeruginosa

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4
-
D-histidine pH 8.7, 25°C Pseudomonas aeruginosa
3400
-
D-arginine pH 8.7, 25°C Pseudomonas aeruginosa