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Literature summary for 3.5.2.3 extracted from

  • Peng, W.F.; Huang, C.Y.
    Allantoinase and dihydroorotase binding and inhibition by flavonols and the substrates of cyclic amidohydrolases (2014), Biochimie, 101, 113-122.
    View publication on PubMed
Search for more literature for 3.5.2.3

Cloned(Commentary)

Cloned (Comment) Organism
recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Klebsiella pneumoniae

Inhibitors

Inhibitors Comment Organism Structure
galangin
-
 Klebsiella pneumoniae
kaempferol
-
 Klebsiella pneumoniae
additional information binding and inhibition of allantoinase dihydroorotase by flavonols and the substrates of other cyclic amidohydrolases, dissociation constants, docking analysis using three-dimensional structure model, PDB ID 3JZE, overview. Hydantoin and allantoin bind to dihydroorotase, but do not affect its activity, no inhibition by phthalimide Klebsiella pneumoniae
myricetin
-
 Klebsiella pneumoniae
quercetin
-
 Klebsiella pneumoniae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Klebsiella pneumoniae

Metals/Ions

Metals/Ions Comment Organism Structure
additional information binuclear metal center within the active site Klebsiella pneumoniae

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis Klebsiella pneumoniae

Reaction

Reaction Comment Organism Reaction ID
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate catalytic mechanism, overview Klebsiella pneumoniae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-dihydroorotate + H2O absolute substrate specificity Klebsiella pneumoniae N-carbamoyl-L-aspartate
-
 ?
additional information allantoin, hydantoin, and phthalimide are not hydrolyzed by dihydroorotase Klebsiella pneumoniae ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Klebsiella pneumoniae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Klebsiella pneumoniae

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.031
-
 pH 8.0, 25°C, recombinant enzyme Klebsiella pneumoniae kaempferol
0.04
-
 pH 8.0, 25°C, recombinant enzyme Klebsiella pneumoniae myricetin

General Information

General Information Comment Organism
additional information the enzyme contains four histidine, one aspartate, and one post-carboxylated lysine residue, which are required for metal binding and catalytic activity Klebsiella pneumoniae