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Literature summary for 3.5.1.5 extracted from

  • Du, N.; Sheng, L.; Xu, H.; Song, C.; Chen, S.
    Kinetics of competitive inhibition of jack bean urease by boric acid (2012), J. Mol. Catal. B, 82, 53-58.
No PubMed abstract available
Search for more literature for 3.5.1.5

Inhibitors

Inhibitors Comment Organism Structure
Boric acid competitive inhibition, which is a reversible reaction with residual activity at lower than 0.25 mM boric acid, maximal inhibition at pH 7.0-9.0 and 30°C. Boric acid binds to the active site of the enzyme Canavalia ensiformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.11
-
 Urea pH 7.4, 25°C Canavalia ensiformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
urea + H2O Canavalia ensiformis
-
 CO2 + 2 NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Canavalia ensiformis P07374
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Canavalia ensiformis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
urea + H2O
-
 Canavalia ensiformis CO2 + 2 NH3
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Canavalia ensiformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Canavalia ensiformis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information inhibition kinetics, modeling, overview Canavalia ensiformis
0.18
-
 Boric acid pH 7.4, 25°C Canavalia ensiformis