Abstract: Urease has a place with the super group of amidohydrolases and phosphotriestreases.

Urease includes the nitrogen digestion; urea degradation; creating CO2 and NH3 from urea.
Urease has wide clinical applications. Urease catalyst fills in as a destructiveness factor and is
capable for pathogenesis in people. Urease movement of microbial sources has added to the
improvement of numerous infections and urease from plant sources is utilized as immunization
against microbial contamination based on its inhibitory movement.

Introduction: Urease (urea amidohydrolase, EC 3.5.1.5) is a nickel-containing compound

delivered by plants, parasites, and microbes that catalyses the hydrolysis of urea into ammonia
and carbamate. Urease is of verifiable significance in Biochemistry as it was the very first
compound to be solidified (1926). Tracking down nickel in urease's dynamic site (1975) was
the main sign of an organic job for this metal. In this assignment, authentic and primary
highlights, energy perspectives, enactment of the metallocentre and inhibitors of the urea
hydrolysing movement of ureases are talked about. The assignment likewise manages the non-
enzymatic natural properties, whose revelation quite a while back began another section in the
investigation of ureases. All around perceived as destructiveness factors because of the
development of ammonia and alkalinization in illnesses by urease-positive microorganisms,
ureases have favourable to provocative, endocytosis-prompting, and neurotoxic exercises that
don't need ureolysis. Especially significant in plants, ureases apply insecticidal and fungitoxic
impacts. Information on the jack bean urease and on jaburetox, a recombinant urease-
determined peptide, have shown that connections with cell layer lipids might be the premise of
the non-enzymatic natural properties of ureases1,2,3,4.

Historical Background: Ureases are pervasive metalloenzymes, created by plants, growths,

and microorganisms, yet not by creatures. The most capable chemicals known to date, ureases
catalyse the hydrolysis of urea into ammonia and carbamate (which then deteriorates into
another alkali particle and carbon dioxide), speeding up the pace of this response by a variable
of something like 1014 when contrasted with the urea decay by disposal response.
Computational demonstrating of urease capability prompted the proposition of a worth up to
multiple times the hypothetical pace of uncatalyzed urea hydrolysis. Nonetheless, one can
contend that, in arrangement, this worth isn't practical because of cut off points forced by the
dissemination of the substrate in water1,2,3,4.

Urea, the regular substrate of ureases, was first detached from human pee by Rouelle in 1773
and about 50 years after the fact, Wöhler accomplished the combination of urea, the main
natural atom to be gotten from inorganic ones6. The first ureolytic microorganism, Micrococcus
ureae, was segregated by van Tiehem in 1864, and the principal protein with ureolytic
movement was disengaged from rotten pee by Musculus in 1874. The name "urease" was
proposed in 1890 by Miquel4. Urease contributed two authentic tourist spots in Biochemistry.
In the first place, the crystallization of urease segregated from jack bean (Canavalia ensiformis)
seeds by James B. Sumner, in 1926, showed the proteinaceous idea of compounds, a disclosure
laureated with the Nobel Prize in Science in 19467. Second, the organic meaning of nickel was
perceived in 1975, after investigations of Zerner's gathering uncovering the presence of nickel
particles in the dynamic site of the jack bean urease (JBU), mandatory for its reactant
movement8. The recognizable proof of a plant poison as a urease in 2001 can be considered as
a third advancement including ureases, as it prompted the revelation of non-reactant properties
of these proteins9. This finding augmented our insight on the variety of capabilities performed
by these proteins, other than their job in nitrogen digestion10.

Ureases are individuals from the superfamily of amidohydrolases and phosphotriesterases,

which show chemically dynamic metal(s) in their dynamic destinations. With a couple of
special cases detailed11,12, ureases convey two Ni2+ particles in their dynamic destinations4,13.
Ureases from various sources share around 55% character in their essential groupings
recommending difference from a typical tribal protein. X-beam crystallography concentrates
on uncovered that plant and bacterial ureases share a typical essential "trimeric" structure4,14.
The quantity of polypeptide chains that structure the "monomer" or utilitarian unit differs as
indicated by the wellspring of urease. For plant and parasitic ureases this utilitarian unit is a
solitary polypeptide chain (α). The practical unit of bacterial ureases is shaped by two subunits
(α and β, up until this point tracked down just in the variety Helicobacter) or three (α, β and γ)
kinds of polypeptide chains. The most plentiful design of plant ureases is a dimer of trimers
(α3)2 albeit a couple dimeric/trimeric/tetrameric plant and furthermore parasites ureases have
been portrayed. Bacterial ureases are trimers ([αβ γ]3) while Helicobacter pylori's urease has
been crystalized as a tetramer of trimers of dimers ([αβ]3)410,14. The amino corrosive groupings
of more modest subunits of prokaryotic ureases are collinear to the comparing locale in the
single chain of eukaryotic ureases4.

The crude condition of these proteins - single-or three-affixed - is one of the unanswered
inquiries with respect to ureases. Utilizing phylogenetic deduction and two calculations applied
to three distinct datasets, a 3-to-1 change in the quantity of urease's subunits was noticed,
suggesting a three-fastened tribal urease from which every one of the current compounds
determined. In that situation, the two-tied ureases in the family Helicobacter are not
developmental intermediates of the eukaryotic single-fastened ureases15.
Enactment and synergist properties of ureases: The active site of ureases comprises, other
than the two nickel particles, of one carbamylated lysine, four histidines and one aspartate
buildup. The crystal designs of bacterial ureases from Klebsiella aerogenes16 and Sporosarcina
pasteurii17 first uncovered the engineering of the compounds dynamic site. These two ureases
have almost superimposable dynamic locales, basically the same as those of different ureases
described a short time later, suggesting that this engineering is illustrative of all ureases. In the
dynamic site, the carbamylated lysine spans the two nickel particles, with Ni (1) further
organized by two histidines and Ni (2) by the other two histidines and by an aspartate buildup.
Moreover, a hydroxide particle spans the two Ni ions, which alongside other three terminal
water atoms (W1, W2, W3), structures a H-bond water tetrahedral group in the active site2,4,14.

Biochemical roles of ureases that require ureolytic activity: Urease action empowers
microorganisms to involve urea as their only nitrogen source. Urease union might be
constitutive or integrated as a pressure related reaction of microbes to neutralize low ecological
pH18. Ureolytic action of the human stomach microbiota hydrolyzes up to 30% of all urea
delivered in our bodies19. Microbial ureases are significant likewise in dental wellbeing20. The
creation of salt resulting to salivary urea cleavage by oral microbiota urease was displayed to
restrain dental cavities and plaque arrangement21. In ruminants, creature determined urea is
severed by bacterial ureases in the forestomach, delivering smelling salts as nitrogen hotspot
for the rumen microbiota, which thusly fills in as biomass to take care of the creatures22,23.
Pathogenesis of numerous clinical circumstances in people and different creatures are
connected straightforwardly to the ureolytic movement of bacterial or contagious
chemicals24,25. A few models are as per the following. Proteus mirabilis is the most well-known
living being that causes urinary stones in people, because of pee alkalization advanced by its
urease, adding to the pathogenesis of pyelonephritis and catheter encrustation. Precipitation of
urinary salts in the alkalinized pee results in struvite and carbonate apatite crystallization26. The
bacterium H. pylori colonizes the stomach mucosa of half of the total populace, fundamentally
expanding the gamble of gastric ulcers and malignant growth24,27,28. HPU, which comprises
around 10% of the complete cell protein, empowers bacterial endurance in the stomach by
killing the acidic medium29. Ureolytic creatures in the stomach related or urinary plot possibly
add to hepatic encephalopathy and trance state coming about in hyperammonemia and
cerebrum inebriation30. Decrease of the ureolytic microorganisms load and the utilization of
acetohydroxamic corrosive as a urease inhibitor are viewed as helpful methodologies under
these circumstances31,32,33. Different microbes likewise produce urease to secure corrosive
obstruction and empower colonization, among which are Shiga-poison delivering Escherichia
coli34, Yersinia enterocolitica35, K. pneumoniae36, Brucella abortus37, and Haemophilus flu38.
Parasitic ureases are engaged with the pathogenesis of human cryptococcosis by Cryptococcus
neoformans38,39, and Cryptococcus gattii40, and of coccidiodomycosis (San Joaquin Valley
fever) by Coccidioides immitis and C. posadasii41. In any case, the job of microbial ureases as
harmfulness factors has a still to a great extent overlooked commitment of non-enzymatic
properties of these proteins, a subject that will be canvassed in the accompanying segment.

Contributions of ureases to plant defense against predators and pathogens: The principal
portrayal of the insecticidal impact of a urease was distributed in 1997 appearance that
ingestion of CNTX killed bugs. The powerlessness of the bugs to CNTX's deadly impact42
relied upon the sort of their stomach related catalysts. Bugs with acidic midguts and cathepsin-
like proteinases, like the cowpea weaver Callosobruchus maculatus (Bruchidae) and the kissing
bug Rhodnius prolixus (Hemiptera), were vulnerable to CNTX while bugs with basic midguts
and trypsin-like compounds were not. This information was deciphered as proof for the need
of proteolytic enactment of CNTX that, once ingested, is hydrolyzed by bug cathepsin-like
enzyme(s) delivering an inner peptide(s) with insecticidal action. As a matter of fact,
forestalling CNTX hydrolysis by adding a cathepsin B inhibitor at the same time with the
poison in the bugs' eating routine safeguarded them against the deadly impact43. Before very
long we portrayed that JBU/CNTX and the incipient organism explicit soybean urease were
insecticidal against the hemipterans Nezara viridula44, Dysdercus peruvianus45,46, Oncopeltus
fasciatus47, and K. Ponnuraj's gathering in India revealed the insecticidal impact of the pigeon
pea urease (Cajanus cajan) against Callosobruchus chinensis25.

The proteolytic actuation of CNTX by bug cathepsin-like chemicals was additionally explored.
Insecticidal peptides were segregated from CNTX's pieces after processing with C. maculatus
compounds48. The most dynamic peptide, pepcanatox, with a sub-atomic mass of ∼10 kDa had
its N still up in the air and, considering this data, a recombinant peptide named jaburetox was
gotten by heterologous articulation in E. coli49. Cathepsin D-like compounds from D.
peruvianus midgut that had the option to perform hydrolysis of CNTX/JBU and discharge the
insecticidal peptide were described45,50,51. A comparable report was performed with JBU and
the milkweed bug Oncopeltus fasciatus, recognizing a cathepsin L that hydrolyzed the urease
to deliver a ∼10 kDa entomotoxic peptide46.
The recombinant peptide jaburetox was cloned utilizing as layout the cDNA of JBURE-II, a
third isoform of urease saw as in C. ensiformis52,53. Considering jaburetox's succession, a
recombinant insecticidal peptide called soyuretox was created54 having as format the cDNA of
the universal soybean urease which, like the undeveloped organism explicit urease, likewise
kills R. prolixus55. Curiously, the locale that incorporates the jaburetox/soyuretox grouping,
containing around 90 amino corrosive buildups, shows a lower closeness when contrasted with
that of the total succession of various ureases, proposing less developmental strain to monitor
this entomotoxic "space" of plant ureases15,49.

Yet, the proteolytic arrival of entomotoxic peptides doesn't recount the entire story of urease's
entomotoxicity. Confirmations showing that the whole urease particle is entomotoxic in
essence begun to include up with concentrates on the counter diuretic impact of C. ensiformis
ureases. In Carlini et al.42, we showed that CNTX delivered a significant enemy of diuretic
outcome in R. prolixus that topped around 4 h after the bugs got the "dinner" containing the
poison, vanishing after 24 h. In any case, the hydrolysis of CNTX in the bug midgut was not
identified before 18 h, recommending that the counter diuretic impact was delivered by the
whole protein. Afterward, JBU and the jaburetox peptide were displayed to cause against
diuresis in R. prolixus' detached Malpighian tubules in the fixation scope of 10−10 and 10−15
M, separately. Shockingly, albeit the two atoms instigated antidiuretic impacts, JBU and
jaburetox set off various flagging pathways prompting antidiuresis. Before long different
papers were distributed by our gathering depicting a rundown of entomotoxic impacts of JBU,
some of which are not imparted to jaburetox, for example, change in water transport and of the
contractility in the yield of R. prolixus. Like the information demonstrating enrollment by
ureases of eicosanoid-interceded pathways in mammalian frameworks, JBU impacts in bugs
required a phospholipase A2 type XII and prostaglandins. JBU and jaburetox designated the
safe arrangement of R. prolixus, prompting an eicosanoid-subordinate collection of hemocytes
and adjustments in cell morphology that render the bug more vulnerable to entomopathogenic
microscopic organisms10,56,57,58.

Both JBU and jaburetox are neurotoxic to bugs from various orders. Jaburetox was
immunolocalized in the mind of Triatoma infestans (Hemiptera) and neurotoxic side effects
went before death of the bugs infused with the peptide. JBU-actuated impacts were
concentrated on in the cockroach Nauphoeta cinerea (Blatodea) uncovering that both, the focal
and the fringe sensory systems are designated by the urease, with adjustments of the
cholinergic, octopaminergic and GABAergic pathways as a feature of its entomotoxic method
of activity. The impacts of JBU were additionally examined on neuromuscular intersections of
Locusta migratoria (Orthoptera) and of Drosophila melanogaster (Diptera), and the subsequent
information highlighted obstruction of JBU on synapse discharge, most likely by disturbance
of the calcium apparatus in the pre-synaptic locale of bug neurons59,60,61.

Past examinations with B.(S.) pasteurii urease recommended absence of insecticidal properties
for microbial ureases, which was credited to the shortfall of part of jaburetox's grouping in
those proteins. Notwithstanding, later reports on insecticidal movement of ureases of microbes
from Photorhabdus and Xenorhabdus genera, Yersinia pseudotuberculosis and P. mirabilis
(Broll, V. et al., unpublished outcomes) showed that bacterial ureases are without a doubt
entomotoxic and insecticidal, in consent to the way that ureases contain other entomotoxic
spaces other than the succession comparing to jaburetox.

Ureases are poisonous against filamentous growths and yeasts. The fungitoxic action of CNTX
was the primary detailed showing that the protein at 2% fixation caused development hindrance
of the phytopathogenic filamentous parasites Macrophomina phaseolina, Colletotrichum
gloesporioides and Sclerotium rolfsii. Becker-Ritt et al., 2007, revealed that JBU and the
soybean incipient organism explicit ureases hindered development as well as spore germination
of seven different types of filamentous parasites at sub-micromolar fixations and made harm
cell wall, even after blockage of their ureolytic dynamic locales. In this equivalent review, the
two-binded HPU likewise restrained parasitic development although,
with less proficiency. The local ureases of cotton seeds (G. hirsutum) and of pigeon pea25,
35

and the recombinant non-ureolytic apoureases, JBURE-IIb and a pervasive soybean urease
melded to glutathione transferase, were likewise demonstrated to be unfavorable to filamentous
growths.

Conclusion and Future aspects of Ureases: While the historical backdrop of exploration on
urease as a catalyst is very nearly 150 years of age, tracing all the way back to the 1870s, the
information that ureases perform other organic jobs irrelevant to ureolysis is significantly more
youthful, not 50 years yet. An impartial perspective on these particles as more than compounds
is expected to permit disclosure of yet unsuspected natural properties of ureases. Finding
ureases in sources little investigated up to this point, unraveling the underlying portrayal of a
wide scope of ureases including non-ureolytic proteins, and to examine an expected
collaboration among synergist and non-reactant properties of ureases, are a couple of the open
fields in the investigation of these compounds.

There are many proposed mechanical utilizations of ureases which investigate only the
protein's all's reactant action. There are however considerably more to be investigated with
these proteins, beginning with the biotechnological utilization of ureases (and of urease-
determined peptides) as transgenes to safeguard crops against bug herbivory and infection
causing parasites, or as ecofriendly insect poisons to control bug borne sicknesses. The
cognizance of ureases as destructiveness factors not just as a ammonia delivering and
alkalinizing specialist however acting in a substantially more complicated manner, enriched of
exocytosis-instigating and supportive of fiery exercises, and enlisting the cooperation of
eicosanoids, may show the best approach to tracking down new pharmacological ways to deal
with numerous pathologies.
References: 1) R. Real-Guerra, F. Staniscuaski, C.R. Carlini
Soybean urease: over a hundred years of knowledge
J.E. Board (Ed.), A comprehensive survey of international soybean research – genetics,
physiology, agronomy and nitrogen relationships, Intech, Rijeka, Croatia (2013), pp. 317-339
2) M.J. Maroney, S. Ciurli
Nonredox nickel enzymes
Chem Rev, 114 (8) (2014), pp. 4206-4228
3) H.L.T. Mobley, R.P. Hausinger
Microbial ureases – significance, regulation, and molecular characterization
Microbiol Rev, 53 (1) (1989), pp. 85-108
4) B. Krajewska, I. Ureases
Functional, catalytic and kinetic properties: a review
J Mol Catal B-Enzym, 59 (1–3) (2009), pp. 9-2
5) B.P. Callahan, Y. Yuan, R. Wolfenden
The burden borne by urease
J Am Chem Soc, 127 (31) (2005), pp. 10828-10829
6) F. Wöhler
Ueber künstliche Bildung des Harnstoffs
Ann Phys-Berlin, 12 (1828), pp. 253-256
7) J.B. Sumner
The isolation and crystallization of the enzyme urease
J Biol Chem, 69 (1926), pp. 435-441
8) N.E. Dixon, T.C. Gazzola, R.L. Blakeley, B. Zermer
Letter: Jack bean urease (EC 3.5.1.5). A metalloenzyme. A simple biological role for nickel?
J Am Chem Soc, 97 (14) (1975), pp. 4131-4133
9) C. Follmer, G.B. Barcellos, R.B. Zingali, O.L.T. Machado, E.W. Alves, C. Barja-Fidalgo,
et al.
Canatoxin, a toxic protein from jack beans (Canavalia ensiformis), is a variant form of urease
(EC 3.5.1.5): biological effects of urease independent of its ureolytic activity
Biochem J, 360 (2001), pp. 217-224
10) C.R. Carlini, R. Ligabue-Braun
Ureases as multifunctional toxic proteins: a review
Toxicon, 110 (2016), pp. 90-109
11) E.L. Carter, D.E. Tronrud, S.R. Taber, P.A. Karplus, R.P. Hausinger
Iron-containing urease in a pathogenic bacterium
P Natl Acad Sci USA, 108 (32) (2011), pp. 13095-13099
12) C. Follmer, C.R. Carlini, M.L. Yoneama, J.F. Dias
PIXE analysis of urease isoenzymes isolated from Canavalia ensiformis (jack bean) seeds
Nucl Instrum Meth B, 189 (2002), pp. 482-486
13) B. Zambelli, F. Musiani, S. Benini, S. Ciurli
Chemistry of Ni(2+) in urease: sensing, trafficking, and catalysis
Acc Chem Res, 44 (7) (2011), pp. 520-530
14) Mazzei L, Musiani F, Ciurli S. Urease. In: Zamble DB, Rowinska-Zyrek M, Kozlowski H,
editors. The Biological Chemistry of Nickel, Roy Soc Ch; 2017, 60–97.
15) R. Ligabue-Braun, F.C. Andreis, H. Verli, C.R. Carlini
3-to-1: unraveling structural transitions in ureases
Naturwissenschaften, 100 (5) (2013), pp. 459-467
16) E. Jabri, M.B. Carr, R.P. Hausinger, P.A. Karplus
The crystal structure of urease from Klebsiella aerogenes
Science, 268 (5213) (1995), pp. 998-1004
17) S. Benini, W.R. Rypniewski, K.S. Wilson, S. Ciurli, S. Mangani
The complex of Bacillus pasteurii urease with beta-mercaptoethanol from X-ray data at 1.65-
A resolution
J Biol Inorg Chem, 3 (1998), pp. 268-273
18) P.D. Cotter, C. Hill
Surviving the acid test: responses of gram-positive bacteria to low pH
Microbiol Mol Biol R, 67 (3) (2003), pp. 429-453
19) D. Mora, S. Arioli
Microbial urease in health and disease
PLoS Pathog, 10 (12) (2014), p. e1004472
20) R.A. Burne, L. Zeng, S.J. Ahn, S.R. Palmer, Y. Liu, T. Lefebure, et al.
Progress dissecting the oral microbiome in caries and health
Adv Dent Res, 24 (2) (2012), pp. 77-80
21) Y.L. Liu, M. Nascimento, R.A. Burne
Progress toward understanding the contribution of alkali generation in dental biofilms to
inhibition of dental caries
Int J Oral Sci, 4 (3) (2012), pp. 135-140
22) P. Javorsky, E. Rybosova, I. Havassy, K. Horsky, V. Kmet
Urease activity of adherent bacteria and rumen fluid bacteria
Physiol Bohemoslov, 36 (1) (1987), pp. 75-81
23) A. Laukova, I. Koniarova
Survey of urease activity in ruminal bacteria isolated from domestic and wild ruminants
Microbios, 84 (338) (1995), pp. 7-11
24) I. Konieczna, P. Zarnowiec, M. Kwinkowski, B. Kolesinska, J. Fraczyk, Z. Kaminski, et
al.
Bacterial urease and its role in long-lasting human diseases
Curr Protein Pept Sc, 13 (8) (2012), pp. 789-806
25) J.C. Rutherford
The emerging role of urease as a general microbial virulence factor
PLoS Pathog, 10 (5) (2014), pp. 1-3
26) H.L.T. Mobley, M.D. Island, R.P. Hausinger
Molecular biology of microbial ureases
Microbiol Rev, 59 (3) (1995), pp. 451-480
27) W. Fischbach
Helicobacter pylori
Internist, 50 (8) (2009), pp. 979-986
28) S. Diaconu, A. Predescu, A. Moldoveanu, C.S. Pop, C. Fierbinteanu-Braticevici
Helicobacter pylori infection: old and new
J Med Life, 10 (2) (2017), pp. 112-117
29) H.L. Mobley, L.T. Hu, P.A. Foxall
Helicobacter pylori urease: properties and role in pathogenesis
Scand J Gastroentero, 187 (1991), pp. 39-46
30) A. Auron, P.D. Brophy
Hyperammonemia in review: pathophysiology, diagnosis, and treatment
Pediatr Nephrol, 27 (2) (2012), pp. 207-222

31) W.N. Fishbein, P.P. Carbone, H.D. Hochstein

Acetohydroxamate: bacterial urease inhibitor with therapeutic potential in hyperammonaemic
states
Nature, 208 (5005) (1965), pp. 46-48
32) W.H. Summerskill, F. Thorsell, J.H. Feinberg, J.S. Aldrete
Effects of urease inhibition in hyperammonemia: clinical and experimental studies with
acetohydroxamic acid
Gastroenterology, 54 (1) (1968), pp. 20-26
33) J. Haberle
Clinical practice: the management of hyperammonemia
Eur J Pediatr, 170 (1) (2011), pp. 21-34
34) Close
S.R. Steyert, J.B. Kaper
Contribution of urease to colonization by Shiga toxin-producing Escherichia coli
Infect Immun, 80 (8) (2012), pp. 2589-2600
35) T.F. de Koning-Ward, A.C. Ward, E.L. Hartland, R.M. Robins-Browne
The urease complex gene of Yersinia enterocolitica and its role in virulence
Contrib Microbiol Immunol, 13 (1995), pp. 262-263
36) N. Maroncle, C. Rich, C. Forestier
The role of Klebsiella pneumoniae urease in intestinal colonization and resistance to
gastrointestinal stress
Res Microbiol, 157 (2) (2006), pp. 184-193
37) F.J. Sangari, A. Seoane, M.C. Rodriguez, J. Aguero, J.M. Garcia Lobo
Characterization of the urease operon of Brucella abortus and assessment of its role in virulence
of the bacterium
Infect Immun, 75 (2) (2007), pp. 774-780
38) T.F. Murphy, A.L. Brauer
Expression of urease by Haemophilus influenzae during human respiratory tract infection and
role in survival in an acid environment
BMC Microbiol, 11 (2011), p. 183

39) M.A. Olszewski, M.C. Noverr, G.H. Chen, G.B. Toews, G.M. Cox, J.R. Perfect, et al.
Urease expression by Cryptococcus neoformans promotes microvascular sequestration,
thereby enhancing central nervous system invasion
Am J Pathol, 164 (5) (2004), pp. 1761-1771
40) M. Shi, S.S. Li, C. Zheng, G.J. Jones, K.S. Kim, H. Zhou, et al.
Real-time imaging of trapping and urease-dependent transmigration of Cryptococcus
neoformans in mouse brain
J Clin Invest, 120 (5) (2010), pp. 1683-1693
41) V. Feder, L. Kmetzsch, C.C. Staats, N. Vidal-Figueiredo, R. Ligabue-Braun, C.R. Carlini,
et al.
Cryptococcus gattii urease as a virulence factor and the relevance of enzymatic activity in
cryptococcosis pathogenesis
FEBS J, 282 (8) (2015), pp. 1406-1418
42) C.R. Carlini, A.E. Oliveira, P. Azambuja, J. Xavier-Filho, M.A. Wells
Biological effects of canatoxin in different insect models: evidence for a proteolytic activation
of the toxin by insect cathepsinlike enzymes
J Econ Entomol, 90 (2) (1997), pp. 340-348
43) C.R. Carlini, M.F. Grossi-de-Sa
Plant toxic proteins with insecticidal properties. A review on their potentialities as
bioinsecticides
Toxicon, 40 (11) (2002), pp. 1515-1539
44) C. Follmer, R. Real-Guerra, G.E. Wasserman, D. Olivera-Severo, C.R. Carlini
Jackbean, soybean and Bacillus pasteurii ureases – biological effects unrelated to ureolytic
activity
Eur J Biochem, 271 (7) (2004), pp. 1357-1363
45) F. Staniscuaski, C.T. Ferreira-Dasilva, F. Mulinari, M. Pires-Alves, C.R. Carlini
Insecticidal effects of canatoxin on the cotton stainer bug Dysdercus peruvianus (Hemiptera:
Pyrrhocoridae)
Toxicon, 45 (6) (2005), pp. 753-760
46) M. Defferrari, D. Demartini, T. Marcelino, P. Pinto, C. Carlini
Insecticidal effect of Canavalia ensiformis major urease on nymphs of the milkweed bug
Oncopeltus fasciatus and characterization of digestive peptidases
Insect Biochem Molec, 41 (6) (2011), pp. 388-399
47) C.T. Ferreira-DaSilva, M.E. Gombarovits, H. Masuda, C.M. Oliveira, C.R. Carlini
Proteolytic activation of canatoxin, a plant toxic protein, by insect cathepsin-like enzymes
Arch Insect Biochem, 44 (4) (2000), pp. 161-171
48) F. Mulinari, F. Staniscuaski, L.R. Berthodo-Vargas, M. Postal, O.B. OliveiraNeto, D.J.
Ridgen, et al.
Jaburetox-2Ec: an insecticidal peptide derived from an isoform of urease form the Canavalia
ensiformis plant
Peptides, 28 (2007), pp. 2042-2050
49) A.R. Piovesan, F. Staniscuaski, J. Marco-Salvadori, R. Real-Guerra, M.S. Defferrari, C.R.
Carlini
Stage-specific gut proteinases of the cotton stainer bug Dysdercus peruvianus: role in the
release of entomotoxic peptides from Canavalia ensiformis urease
Insect Biochem Molec, 38 (11) (2008), pp. 1023-1032
50) R. Real-Guerra, C.R. Carlini, F. Staniscuaski
Role of lysine and acidic amino acid residues on the insecticidal activity of Jackbean urease
Toxicon, 71 (2013), pp. 76-83