Literature summary for 3.5.1.5 extracted from

Balasubramanian, A.; Ponnuraj, K.
Crystal structure of the first plant urease from jack bean: 83 years of journey from its first crystal to molecular structure (2010), J. Mol. Biol., 400, 274-283.

Crystallization (Commentary)

Crystallization (Comment)	Organism
urease is crystallized at 2.05 A resolution. The active-site architecture of JBU is similar to that of bacterial ureases containing a bi-nickel center. JBU has a bound phosphate and covalently modified residue (Cys592) by beta-mercaptoethanol at its active site. By correlating the structural information of JBU with the available biophysical and biochemical data on insecticidal properties of plant ureases, it is hypothesized that the amphipathic beta-hairpin located in the entomotoxic peptide region of plant ureases might form a membrane insertion beta-barrel as found in beta-poreforming toxins	Canavalia ensiformis

Crystallization (Comment)

Organism

urease is crystallized at 2.05 A resolution. The active-site architecture of JBU is similar to that of bacterial ureases containing a bi-nickel center. JBU has a bound phosphate and covalently modified residue (Cys592) by beta-mercaptoethanol at its active site. By correlating the structural information of JBU with the available biophysical and biochemical data on insecticidal properties of plant ureases, it is hypothesized that the amphipathic beta-hairpin located in the entomotoxic peptide region of plant ureases might form a membrane insertion beta-barrel as found in beta-poreforming toxins

Canavalia ensiformis

Organism

Organism	UniProt	Comment	Textmining
Canavalia ensiformis	P07374	-	-

Synonyms

Synonyms	Comment	Organism
JBU	-	Canavalia ensiformis
urease	-	Canavalia ensiformis

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Release 2023.1 (January 2023)