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Literature summary for 3.5.1.5 extracted from

  • Mazzei, L.; Cianci, M.; Musiani, F.; Lente, G.; Palombo, M.; Ciurli, S.
    Inactivation of urease by catechol kinetics and structure (2017), J. Inorg. Biochem., 166, 182-189 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop method at 20°C, the crystal structure of the enzyme-catechol complex, determined at 1.50 A resolution, reveals the structural details of the enzyme inhibition Sporosarcina pasteurii

Inhibitors

Inhibitors Comment Organism Structure
catechol irreversibly inactivates the enzyme with a complex radical-based autocatalytic multistep mechanism Canavalia ensiformis
catechol irreversibly inactivates the enzyme with a complex radical-based autocatalytic multistep mechanism Sporosarcina pasteurii

Metals/Ions

Metals/Ions Comment Organism Structure
Ni2+ Ni(II)-containing enzyme Canavalia ensiformis
Ni2+ Ni(II)-containing enzyme Sporosarcina pasteurii

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Canavalia ensiformis P07374
-
-
Sporosarcina pasteurii P41022
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sporosarcina pasteurii

Substrates and Products (Substrate)

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