Primary Structure of Potato Kunitz-Type Serine Proteinase Inhibitor

Valueva, T. A.; Revina, T. A.; Mosolov, V. V.; Mentele, Reinhard

doi:10.1515/bc.2000.149

Cited by 37 publications

(49 citation statements)

References 30 publications

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“…Thus, potato group A and B KTIs strongly inhibit trypsin, whereas potato group C KTIs do so only weakly. In contrast to poplar KTIs, potato KTIs also inhibit other enzymes, including subtilisin, the aspartic proteinases cathepsin D and aspergillopepsin, and Cys proteinases (Ritonja et al, 1990;Rowan et al, 1990;Valueva et al, 2000;Heibges et al, 2003b;Revina et al, 2004).…”

Section: Biochemical Analysis Indicates Functional Diversification Ofmentioning

confidence: 97%

“…By contrast, TI3 and TI5 inhibited both trypsin and chymotrypsin with similar efficiency. TI6 was the only elastase inhibitor, a rare activity among plant KTIs (Valueva et al, 2000;Araujo et al, 2005;Sumikawa et al, 2006). These functional differences presumably reflect the sequence diversity of the KTI family.…”

Section: Biochemical Analysis Indicates Functional Diversification Ofmentioning

confidence: 99%

“…Individual KTIs typically have more specific activities. Whereas many plant KTIs inhibit trypsin or chymotrypsin, some can inhibit other Ser proteinases, such as elastase and subtilisin (Terada et al, 1994;Valueva et al, 2000;Revina et al, 2004;Sumikawa et al, 2006). KTIs that inhibit Cys or aspartic proteinases are also reported (Ritonja et al, 1990;Rowan et al, 1990;Heibges et al, 2003b).…”

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confidence: 99%

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

2007

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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.

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Section: Biochemical Analysis Indicates Functional Diversification Ofmentioning

confidence: 97%

Section: Biochemical Analysis Indicates Functional Diversification Ofmentioning

confidence: 99%

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confidence: 99%

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

2007

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“…The products of these genes include inhibitors of serine, aspartic, and cysteine proteinases, as well as proteins exhibiting other types of biological activity [13,71,72]. In addition to trypsin and chymotrypsin inhibitors, the group of potato SKTI proteins contains inhibitors of other serine proteinases, such as subtilisin [73,74] and leukocyte elastase (the inhibitor PSPI-21 is a potent inhibitor of this enzyme) [75]. Some potato inhibitors contain two active sites [76,77].…”

Section: Properties Of Proteinase Inhibitorsmentioning

confidence: 99%

“…In addition to trypsin and chymotrypsin inhibitors, the group of potato SKTI proteins contains inhibitors of other serine proteinases, such as subtilisin [73,74] and leukocyte elastase (the inhibitor PSPI-21 is a potent inhibitor of this enzyme) [75]. Some potato inhibitors contain two active sites [76,77]. Similar to certain inhibitors from leguminous plants, PSPI-21 is composed of two disulfide-bridged polypeptide chains of 16.5 and 4.5 kDa [78].…”

Section: Properties Of Proteinase Inhibitorsmentioning

confidence: 99%

Proteinase inhibitors and their function in plants: A review

Mosolov

Valueva

2005

Appl Biochem Microbiol

112

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Kunitz‐type protease inhibitors group B from Solanum palustre

Speransky

Cimaglia

Krinitsina

et al. 2007

Biotechnology Journal

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Five Kunitz protease inhibitor group B genes were isolated from the genome of the diploid non-tuber-forming potato species Solanum palustre. Three of five new genes share 99% identity to the published KPI-B genes from various cultivated potato accessions, while others exhibit 96% identity. Spls-KPI-B2 and Spls-KPI-B4 proteins contain unique substitutions of the most conserved residues usually involved to trypsin and chymotrypsin-specific binding sites of Kunitz-type protease inhibitor (KPI)-B, respectively. To test the inhibition of trypsin and chymotrypsin by Spls-KPI proteins, five of them were produced in E. coli purified using a Ni-sepharose resin and ion-exchange chromatography. All recombinant Spls-KPI-B inhibited trypsin; K(i) values ranged from 84.8 (Spls-KPI-B4), 345.5 (Spls-KPI-B1), and 1310.6 nM (Spls-KPI-B2) to 3883.5 (Spls-KPI-B5) and 8370 nM (Spls-KPI-B3). In addition, Spls-KPI-B1 and Spls-KPI-B4 inhibited chymotrypsin. These data suggest that regardless of substitutions of key active-center residues both Spls-KPI-B4 and Spls-KPI-B1 are functional trypsin-chymotrypsin inhibitors.

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Primary Structure of Potato Kunitz-Type Serine Proteinase Inhibitor

Cited by 37 publications

References 30 publications

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

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

Proteinase inhibitors and their function in plants: A review

Kunitz‐type protease inhibitors group B from Solanum palustre

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