Jackbean, soybean and Bacillus pasteurii ureases

In this work we compared two plant ureases, jackbean urease (JBU) and embryo‐specific soybean urease (SBU) and a bacterial (Bacillus pasteurii) urease, for kinetic parameters and other biological properties described recently for ureases that are independent of the ureolytic activity. The insecticid...

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Veröffentlicht in:European journal of biochemistry 2004-04, Vol.271 (7), p.1357-1363
Hauptverfasser: Follmer, Cristian, Real‐Guerra, Rafael, Wasserman, German E., Olivera‐Severo, Deiber, Carlini, Célia R.
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container_end_page 1363
container_issue 7
container_start_page 1357
container_title European journal of biochemistry
container_volume 271
creator Follmer, Cristian
Real‐Guerra, Rafael
Wasserman, German E.
Olivera‐Severo, Deiber
Carlini, Célia R.
description In this work we compared two plant ureases, jackbean urease (JBU) and embryo‐specific soybean urease (SBU) and a bacterial (Bacillus pasteurii) urease, for kinetic parameters and other biological properties described recently for ureases that are independent of the ureolytic activity. The insecticidal effect of ureases was investigated in feeding trials with the cotton sucker bug, Dysdercus peruvianus (Hemiptera) as an insect model. Contrasting with B. pasteurii urease (PBU), both plant ureases presented potent insecticidal activity, with LD50 values of 0.017% (w/w) and 0.052% (w/w) for JBU and SBU, respectively. The insecticidal property of JBU or SBU was not affected by treatment with p‐hydroxymercuribenzoate, an irreversible inhibitor of ureolytic activity of both proteins. Also, contrasting with canatoxin – a urease isoform from jackbean seeds that displays a toxic effect in mice (LD50 = 2 mg·kg−1) – no lethality was seen in mice injected intraperitoneally with JBU or SBU (20 mg·kg−1). Similarly to canatoxin, the three enzymes promoted aggregation of blood platelets (EC50 = 400.0 µg·mL−1, 22.2 µg·mL−1, 15.8 µg·mL−1 for BPU, SBU and JBU, respectively). This platelet activating property was also independent of urease activity. Comparison of the kinetic properties indicated that SBU is fivefold less susceptible than JBU to inhibition by acetohydroxamic acid, a chelator of Ni+2 and Zn+2 ions. The ureases also showed different susceptibility to agents that modify cysteine residues, such as p‐hydroxymercuribenzoate and p‐benzoquinone. Altogether, these data emphasize that biological properties that are independent of ureolytic activity are not restricted to jackbean ureases and that these proteins may have a role in plant defense against insect predators.
doi_str_mv 10.1111/j.1432-1033.2004.04046.x
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The insecticidal effect of ureases was investigated in feeding trials with the cotton sucker bug, Dysdercus peruvianus (Hemiptera) as an insect model. Contrasting with B. pasteurii urease (PBU), both plant ureases presented potent insecticidal activity, with LD50 values of 0.017% (w/w) and 0.052% (w/w) for JBU and SBU, respectively. The insecticidal property of JBU or SBU was not affected by treatment with p‐hydroxymercuribenzoate, an irreversible inhibitor of ureolytic activity of both proteins. Also, contrasting with canatoxin – a urease isoform from jackbean seeds that displays a toxic effect in mice (LD50 = 2 mg·kg−1) – no lethality was seen in mice injected intraperitoneally with JBU or SBU (20 mg·kg−1). Similarly to canatoxin, the three enzymes promoted aggregation of blood platelets (EC50 = 400.0 µg·mL−1, 22.2 µg·mL−1, 15.8 µg·mL−1 for BPU, SBU and JBU, respectively). This platelet activating property was also independent of urease activity. Comparison of the kinetic properties indicated that SBU is fivefold less susceptible than JBU to inhibition by acetohydroxamic acid, a chelator of Ni+2 and Zn+2 ions. The ureases also showed different susceptibility to agents that modify cysteine residues, such as p‐hydroxymercuribenzoate and p‐benzoquinone. 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The insecticidal effect of ureases was investigated in feeding trials with the cotton sucker bug, Dysdercus peruvianus (Hemiptera) as an insect model. Contrasting with B. pasteurii urease (PBU), both plant ureases presented potent insecticidal activity, with LD50 values of 0.017% (w/w) and 0.052% (w/w) for JBU and SBU, respectively. The insecticidal property of JBU or SBU was not affected by treatment with p‐hydroxymercuribenzoate, an irreversible inhibitor of ureolytic activity of both proteins. Also, contrasting with canatoxin – a urease isoform from jackbean seeds that displays a toxic effect in mice (LD50 = 2 mg·kg−1) – no lethality was seen in mice injected intraperitoneally with JBU or SBU (20 mg·kg−1). Similarly to canatoxin, the three enzymes promoted aggregation of blood platelets (EC50 = 400.0 µg·mL−1, 22.2 µg·mL−1, 15.8 µg·mL−1 for BPU, SBU and JBU, respectively). This platelet activating property was also independent of urease activity. Comparison of the kinetic properties indicated that SBU is fivefold less susceptible than JBU to inhibition by acetohydroxamic acid, a chelator of Ni+2 and Zn+2 ions. The ureases also showed different susceptibility to agents that modify cysteine residues, such as p‐hydroxymercuribenzoate and p‐benzoquinone. 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The insecticidal effect of ureases was investigated in feeding trials with the cotton sucker bug, Dysdercus peruvianus (Hemiptera) as an insect model. Contrasting with B. pasteurii urease (PBU), both plant ureases presented potent insecticidal activity, with LD50 values of 0.017% (w/w) and 0.052% (w/w) for JBU and SBU, respectively. The insecticidal property of JBU or SBU was not affected by treatment with p‐hydroxymercuribenzoate, an irreversible inhibitor of ureolytic activity of both proteins. Also, contrasting with canatoxin – a urease isoform from jackbean seeds that displays a toxic effect in mice (LD50 = 2 mg·kg−1) – no lethality was seen in mice injected intraperitoneally with JBU or SBU (20 mg·kg−1). Similarly to canatoxin, the three enzymes promoted aggregation of blood platelets (EC50 = 400.0 µg·mL−1, 22.2 µg·mL−1, 15.8 µg·mL−1 for BPU, SBU and JBU, respectively). This platelet activating property was also independent of urease activity. 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source Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection
subjects Bacillus pasteurii
Bacillus pasteurii urease
Dysdercus peruvianus
Hemiptera
insecticide
jackbean urease
platelet aggregation
soybean urease
title Jackbean, soybean and Bacillus pasteurii ureases
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