Biochemical characterisation of prolyl aminopeptidase from shoots of triticale seedlings and its activity changes in response to suboptimal growth conditions

Szawłowska, Urszula; Zdunek‐Zastocka, Edyta; Bielawski, W

doi:10.1016/j.plaphy.2011.05.008

Cited by 16 publications

(4 citation statements)

References 43 publications

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“…22 Several proteases, especially aminopeptidases from other plants, were reported to show similar temperature optima. 12,[35][36][37][38] The pH profile of aminopeptidases activity and the pH optimum (Supporting Information, Fig. S6) for Phe-pNA was similar to that obtained for dry seeds of oilseed rape (pH 6.5 and smaller peak at pH 9.0).…”

Section: Profiles Of Aminopeptidases Activity During Oilseed Rape Germination Under Standard Conditionssupporting

confidence: 74%

“…A significant increase (sevenfold) of PAP activity was also observed in triticale seedlings treated with Cd ions. 12 The presence of Cd also caused an increase of aminopeptidases activity toward Leu, Pro, Arg, Lys, or Met in other plants. 30,31 Pb, the other toxic heavy metal, negatively influences processes of photosynthesis, metabolism of nitrogen, and cell division in plants.…”

Section: Profiles Of Aminopeptidases Activity During Oilseed Rape Germination Under Standard Conditionsmentioning

confidence: 96%

“…The results are comparable to other published data. For example, the negative effect of Zn, Cu, or Pb ions was described for prolyl aminopeptidase from triticale 12 and rye, 34 whereas Mg 2+ and Mn 2+ had an activating influence on enzymes from pigeonpea (Cajanas cajan), barley seeds, and potato. 35,36 Temperature profile, pH profile, and molecular mass of aminopeptidases contained in oilseed rape seedlings We previously presented the general characteristics of aminopeptidases from oilseed rape dry seeds that were active toward hydrophobic amino acids in our 2016 paper.…”

Section: Profiles Of Aminopeptidases Activity During Oilseed Rape Germination Under Standard Conditionsmentioning

confidence: 99%

“…[6][7][8][9][10] Some of the enzymes, crucial for germination process, are synthesized either during embryogenesis (and further activated during imbibition) or just during imbibition. Aminopeptidases with different substrate preferences have been characterized in various plant species, such as barley (Hordeum vulgare), 5 sunflower (Helianthus annuus), 11 triticale (Triticosecale), 12 soybean cotyledons (Glycine max), 13 and Solanum tuberosum tuber. 14 The most intensified activity of aminopeptidases was observed during storage proteins mobilization.…”

Section: Introductionmentioning

confidence: 99%

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Oilseed rape (Brassica napus): the importance of aminopeptidases in germination under normal and heavy metals stress conditions

2021

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BACKGROUND: Oilseed rape is one of the most important oilseed crops worldwide, crucial in the food and feed industries. Different environment and climatic conditions can influence its sustainable cultivation and crop yield. Aminopeptidases are crucial enzymes in many physiological processes in all organisms, including humans, so it is important to learn their behavior in food and feed sources. This study presents, for the first time, a detailed discussion on the importance of aminopeptidases, during the oilseed rape germination process, under standard and stress conditions. RESULTS: During the germination of oilseed rape under standard conditions, a significant increase in aminopeptidases activity toward N-terminal amino acidsphenylalanine (Phe), alanine (Ala), glycine (Gly), leucine (Leu), proline (Pro), methionine (Met) was observed. The change was substrate specific, with the highest increase being observed for Gly (3.2-fold), followed by Ala (2.9-fold), Pro (2.5-fold), Met (1.5-fold), and Phe (1.3-fold). Generally, N-terminal Phe was preferentially cleaved. Germination under stress conditions, caused by several heavy metal ions (e.g. divalent copper, zinc, cadmium, and lead ions), negatively influenced the plants' growth and quality, but significantly enhanced the expression of genes encoding aminopeptidases (or potentially activated aminopeptidases precursors), which was related to the dramatic increase of their activity.CONCLUSIONS: The activity/concentration of aminopeptidases in plants is adjusted to the needs at each stage of development and stress factors occurrence. The most significant increase of activity toward N-terminal Gly and Pro proved the key role of aminopeptidases in the defense mechanisms, by supplying the plants with osmoprotectants and organic nitrogen. The results provide new concepts of oilseed rape growth and cultivation under different conditions.

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Section: Profiles Of Aminopeptidases Activity During Oilseed Rape Germination Under Standard Conditionssupporting

confidence: 74%

Section: Profiles Of Aminopeptidases Activity During Oilseed Rape Germination Under Standard Conditionsmentioning

confidence: 96%

Section: Profiles Of Aminopeptidases Activity During Oilseed Rape Germination Under Standard Conditionsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Oilseed rape (Brassica napus): the importance of aminopeptidases in germination under normal and heavy metals stress conditions

2021

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Studies on the Molecular Docking and Amino Acid Residues Involving in Recognition of Substrate in Proline Iminopeptidase by Site-Directed Mutagenesis

Jing

Hong

2015

Protein J

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The proline iminopeptidase (PchPiPA) of Phanerochaete chrysosporium catalyze specifically hydrolysis of N-terminal proline from peptides. The substrate Pro-pNA was docked into the catalytic pocket and several amino acid residues were identified to interact or associate with the substrate. Eight residues were selected for site-directed mutagenesis. The wild-type and mutant proteins were expressed in Escherichia coli and purified. Kinetic parameters were calculated by hydrolyzing Pro-pNA for these enzymes. Substitution of two Glu residues (Glu198 and Glu227) which interact with the substrate via formation of hydrogen bond, led to deleterious effect on catalytic efficiency (k(cat)/K(m)) due to decrease of k(cat) and increase of K(m). Four Phe residues consisting of catalytic pocket and surrounding the docked substrate, were substituted with Ala, resulting in decrease in k(cat)/K(m) to various extents. Substitution of two residues (Val267 and Cys267) localized at the deep end of the catalytic pocket also yielded negative influence on the substrate hydrolysis. Besides, all the mutants except E227Q exhibited lower thermostability than the wild-type did, indicating that these mutations may modulate the local structure. In conclusion, these amino acid residues may play an important role in maintaining local environment of the impacted catalytic pocket and be involved in recognizing or positioning the substrate.

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Functional characterization of an Arabidopsis prolyl aminopeptidase AtPAP1 in response to salt and drought stresses

Sun

Wang

Cai

et al. 2013

Plant Cell Tiss Organ Cult

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Biochemical characterisation of prolyl aminopeptidase from shoots of triticale seedlings and its activity changes in response to suboptimal growth conditions

Cited by 16 publications

References 43 publications

Oilseed rape (Brassica napus): the importance of aminopeptidases in germination under normal and heavy metals stress conditions

Oilseed rape (Brassica napus): the importance of aminopeptidases in germination under normal and heavy metals stress conditions

Studies on the Molecular Docking and Amino Acid Residues Involving in Recognition of Substrate in Proline Iminopeptidase by Site-Directed Mutagenesis

Functional characterization of an Arabidopsis prolyl aminopeptidase AtPAP1 in response to salt and drought stresses

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