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Literature summary for 3.5.1.5 extracted from

  • Tekiner, P.; Percin, I.; Erguen, B.; Yavuz, H.; Aksoez, E.
    Purification of urease from jack bean (Canavalia ensiformis) with copper (II) chelated poly(hydroxyethyl methacrylate-N-methacryloyl-(L)-histidine methyl ester) cryogels (2012), J. Mol. Recognit., 25, 549-554.
    View publication on PubMed

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
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 162fold from jack bean meal by immobilized metal affinity chromatography using Cu2+ chelated poly(hydroxyethyl methacrylate-N-methacryloyl-(L)-histidine methyl ester) [PHEMAH-Cu2+]-based cryogels, gel resin synthesis and method evaluation and optimization, first- and second-order kinetic constants for enzyme binding, overview. The enzyme can be repeatedly bound and eluted from (PHEMAH)-Cu2+ cryogel with less than 10% loss in column capacity Canavalia ensiformis

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
Canavalia ensiformis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
8.82
-
purified enzyme, pH 7.0, 25°C Canavalia ensiformis

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
jack bean urease
-
Canavalia ensiformis
JBU
-
Canavalia ensiformis

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
-
assay at Canavalia ensiformis