Primary sequence determination of a Kunitz inhibitor isolated from Delonix regia seeds

Pando, Silvana Cristina; Oliva, Maria Luíza Vilela; Sampaio, Cláudio Hoffmann; Ciero, Luciana Di; Novello, José Camillo; Marangoni, Sérgio

doi:10.1016/s0031-9422(01)00080-2

Cited by 45 publications

(27 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The CpaTI purified here is a protein with two polypeptide chains of molecular mass of 27.6 and 5.6 kDa, as observed by SDS-PAGE (reducing and non-reducing conditions) analysis, which is similar to the molecular mass of other trypsin inhibitors [38][39][40][41][42][43][44]. The specificity of the inhibitory activity of the Fabaceae family serine proteinase inhibitors varies.…”

Section: Discussionmentioning

confidence: 90%

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

Gomes

Barbosa

Macedo

et al. 2005

Plant Physiology and Biochemistry

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 90%

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

Gomes

Barbosa

Macedo

et al. 2005

Plant Physiology and Biochemistry

View full text Add to dashboard Cite

“…Other plant KTIs may have more atypical reactive sites. Glu-Ser are the reactive site residues of DrTI from Delonix regia seeds and sporamin from Ipomoea batatas tubers (Pando et al, 2001;Yao et al, 2001), and these are also the predicted residues for the poplar TI2 and TI3 reactive sites (Fig. 2).…”

Section: Biochemical Analysis Indicates Functional Diversification Ofmentioning

confidence: 92%

Functional Analysis of the Kunitz Trypsin Inhibitor Family in Poplar Reveals Biochemical Diversity and Multiplicity in Defense against Herbivores

2007

View full text Add to dashboard Cite

We investigated the functional and biochemical variability of Kunitz trypsin inhibitor (KTI) genes of Populus trichocarpa 3 Populus deltoides. Phylogenetic analysis, expressed sequence tag databases, and western-blot analysis confirmed that these genes belong to a large and diverse gene family with complex expression patterns. Five wound-and herbivore-induced genes representing the diversity of the KTI gene family were selected for functional analysis and shown to produce active KTI proteins in Escherichia coli. These recombinant KTI proteins were all biochemically distinct and showed clear differences in efficacy against trypsin-, chymotrypsin-, and elastase-type proteases, suggesting functional specialization of different members of this gene family. The in vitro stability of the KTIs in the presence of reducing agents and elevated temperature also varied widely, emphasizing the biochemical differences of these proteins. Significantly, the properties of the recombinant KTI proteins were not predictable from primary amino acid sequence data. Proteases in midgut extracts of Malacosoma disstria, a lepidopteran pest of Populus, were strongly inhibited by at least two of the KTI gene products. This study suggests that the large diversity in the poplar (Populus spp.) KTI family is important for biochemical and functional specialization, which may be important in the maintenance of pest resistance in long-lived plants such as poplar.

show abstract

“…This bifunctional property was detected in several Kunitz-type inhibitors, such as proteins isolated from seeds of Acacia confusa, Caesalpinia bonbuc (L.), Enterolobium contortisiliquum, Erythrina variegata, Swartizia pickelli (inhibitory activities toward trypsin and chymotrypsin), Pithecellobium dumosum, Crotalaria pallida (inhibitory activities toward trypsin, chymotrypsin and papain), Delonix regia (inhibitory activities toward trypsin and human plasma kallikrein), P. juliflora (inhibitory activity toward papain and trypsin) [3,6,7,[18][19][20][21][22][23][24]. In summary, the present study aims to provide new biochemical information about an unusual non-competitive Kunitz inhibitor with the ability to inhibit two different proteolytic enzyme classes, shedding some light on mechanistic inhibitory strategies.…”

Section: Introductionmentioning

confidence: 99%

Structural and mechanistic insights into a novel non-competitive Kunitz trypsin inhibitor from Adenanthera pavonina L. seeds with double activity toward serine- and cysteine-proteinases

Migliolo

Oliveira

Santos

et al. 2010

Journal of Molecular Graphics and Modelling

View full text Add to dashboard Cite

Primary sequence determination of a Kunitz inhibitor isolated from Delonix regia seeds

Cited by 45 publications

References 26 publications

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

Functional Analysis of the Kunitz Trypsin Inhibitor Family in Poplar Reveals Biochemical Diversity and Multiplicity in Defense against Herbivores

Structural and mechanistic insights into a novel non-competitive Kunitz trypsin inhibitor from Adenanthera pavonina L. seeds with double activity toward serine- and cysteine-proteinases

Contact Info

Product

Resources

About