Journals / Balıkesir Üniversitesi Fen Bilimleri Enstitüsü Dergisi / 2022 / Cilt: 24 - Sayı: 2

In silico analysis on catalase protein from Nicotiana tabaccum L.

Nicotiana tabaccum L. katalaz proteininin in siliko analizi

Pages
818–829
Publication Date
2022-07-08
DOI
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

A highly reliable 3D structure was obtained and from Ramachandran plot analysis it was found that the portion of residues falling into the most favoured regions was 97.23%.

📌 3 Key Takeaways

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Objective & Hypothesis:Catalases are antioxidant enzymes which are responsible for decomposition of hydrogen peroxide to water and oxygen.
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Key Findings & Data:The results of this sudy suggested that the ORF of NtCAT-1 gene is 1479 bp and encodes a polypeptide of 492 amino acids.
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Conclusion & Impact:A highly reliable 3D structure was obtained and from Ramachandran plot analysis it was found that the portion of residues falling into the most favoured regions was 97.23%.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Nicotiana tabaccum L. · katalaz · in siliko

Abstract

Catalases are antioxidant enzymes which are responsible for decomposition of hydrogen peroxide to water and oxygen. Catalase activities have been shown to be influenced by environmental factors and stress conditions. In this study, in silico analysis of Nicotiana tabaccum L. was performed via bioinformatic tools. The results of this sudy suggested that the ORF of NtCAT-1 gene is 1479 bp and encodes a polypeptide of 492 amino acids. The predicted polypeptide was revealed as a 56.82 kDa protein with a pI of 6.27. The polypeptide had an aliphatic index of 71.52 and the grand average of hydropathicity (GRAVY) of -0.519. NtCAT-1 protein is hydrophilic and localised in Peroxisome. NtCAT-1 had two conserved domains at the positions of 18-399 and 421 and 486. had the catalase activity motif (CAM) at the position of 54–70 and heme-binding site (HBS) at the position of 344– 352. A highly reliable 3D structure was obtained and from Ramachandran plot analysis it was found that the portion of residues falling into the most favoured regions was 97.23%. The results of this study will provide fundamental information for further research in silico studies on catalase protein in different plant species.

Özet

Katalazlar, hidrojen peroksitin su ve oksijene ayrışmasından sorumlu olan antioksidan enzimlerdir. Katalaz aktivitelerinin çevresel faktörlerden ve stres koşullarından etkilendiği gösterilmiştir. Bu çalışmada Nicotiana tabaccum L. katalaz proteininin biyoinformatik araçlarla in siliko analizi yapılmıştır. Bu araştırmanın sonuçları, NtCAT-1 geninin ORF'sinin 1479 bp olduğunu ve 492 amino asitlik bir polipeptidi kodladığını göstermiştir. Öngörülen polipeptit, 6.27'lik bir pl ile 56.82 kDa'lık bir protein olarak ortaya çıkmıştır. Polipeptit, 71.52'lik bir alifatik indekse ve -0.519'luk büyük hidropatisite (GRAVY) ortalamasına sahiptir. NtCAT-1 proteini hidrofiliktir ve peroksizomda lokalizedir. NtCAT-1, 18-399 ve 421 ve 486 pozisyonlarında iki korunmuş domaine sahiptir. 54-70 pozisyonunda katalaz aktivite motifine (CAM) ve 344-352 pozisyonunda heme-bağlama bölgesine (HBS) sahiptir. Son derece güvenilir bir 3B yapı elde edilmiş ve Ramachandran çizim analizinden, en çok tercih edilen bölgelere düşen rezidülerin %97.23 olduğu bulunmuştur. Bu çalışmanın sonuçları, farklı bitki türlerinde katalaz proteini ile ilgili in siliko çalışmalarında daha ileri araştırmalar için temel bilgiler sağlayacaktır.

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Cite This Article

SÖNMEZ, G. D. (2022). In silico analysis on catalase protein from Nicotiana tabaccum L.. Balıkesir Üniversitesi Fen Bilimleri Enstitüsü Dergisi, Cilt: 24 - Sayı: 2, 818–829. https://ajindex.com/articles/472779

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References (13)

  1. Cruz de Carvalho M. H. Drought stress and reactive oxygen species: Production, scavenging and signaling, Plant signaling & behavior, 3, 3, 156–165, (2008).
  2. Sachdev. S., Ansari, S.A., Ansari. M.I., Fujita. M., Hasanuzzaman. M. Abiotic Stress and Reactive Oxygen Species: Generation, Signaling, and Defense Mechanisms, Antioxidants (Basel), 10, 2, 277, (2021).
  3. Sharma, P., Jha, A.B., Dubey, R.S. and Pessarakli, M. Reactive Oxygen Species, Oxidative Damage, and Antioxidative Defense Mechanism in Plants under Stressful Conditions, Journal of Botany, 1, 26, (2012).
  4. Dat J.F., Inzé, D., Van Breusegem, F. Catalase-deficient tobacco plants: tools for in planta studies on the role of hydrogen peroxide, Redox Report, 6, 1, 37-42, (2001).
  5. Zamocky, M., Furtmüller, P. G., and Obinger, C. Evolution of catalases from bacteria to humans, Antioxidants & redox signaling, 10, 9, 1527–1548, (2008).
  6. Wutipraditkul, N., Boonkomrat, S. and Buaboocha, T. Cloning and characterization of catalases from rice, Oryza sativa L., Bioscience, Biotechnology, and Biochemistry, 75, 10, 1900-6, (2011).
  7. Sofo, A., Scopa, A., Nuzzaci, M., Vitti, A. Ascorbate Peroxidase and Catalase Activities and Their Genetic Regulation in Plants Subjected to Drought and Salinity Stresses, International Journal of Molecular Sciences, 12, 16, 6, 13561-78, (2015).
  8. Polidoros, A.N., Mylona, P.V. and Scandalios, J.G. Transgenic tobacco plants expressing the maize Cat2 gene have altered catalase levels that affect plant-pathogen interactions and resistance to oxidative stress, Transgenic Research, 10, 6, 555-69, (2001).
  9. Lukasik, I. Changes in activity of superoxide dismutase and catalase within cereal aphids in response to plant o-dihydroxyphenols. Journal of Applied Entomology, 131, 209-214, (2007).
  10. Havir, E.A. and McHale, N.A. Regulation of Catalase Activity in Leaves of Nicotiana sylvestris by High CO(2), Plant Physiology, 8, 3, 952-957, (1989).
  11. Isman, M.B. Botanical insecticides: for richer, for poorer, Pest Management Science, 64, 8-11, (2008).
  12. Sayers, E.W., Bolton, E.E., Brister, J.R., Canese, K., Chan, J., Comeau, D.C., Connor, R., Funk, K., Kelly, C., Kim, S., Madej, T., Marchler-Bauer, A., Lanczycki, C., Lathrop, S., Lu, Z., Thibaud-Nissen, F., Murphy, T., Phan, L., Skripchenko, Y., Tse, T., Wang, J., Williams, R., Trawick, B.W., Pruitt, K.D., Sherry, S.T. Database resources of the national center for biotechnology information, Nucleic Acids Research, 50, D1, D20-D26, (2022).
  13. Gasteiger E., Hoogland C., Gattiker