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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.5 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.5 5.11
-
 Urea pH 7.4, 25°C Canavalia ensiformis

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.5 Canavalia ensiformis P07374
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.5 commercial preparation
-
 Canavalia ensiformis
-

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.5 25
-
 assay at Canavalia ensiformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.5 7.4
-
 assay at Canavalia ensiformis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.5.1.5 additional information
-
 additional information inhibition kinetics, modeling, overview Canavalia ensiformis
3.5.1.5 0.18
-
 Boric acid pH 7.4, 25°C Canavalia ensiformis