Nicotiana tabaccum L. katalaz proteininin in siliko analizi

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.

Anahtar Kelimeler:

Nicotiana tabaccum L., katalaz, in siliko

In silico analysis on catalase protein from Nicotiana tabaccum L.

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.

Keywords:

Nicotiana tabaccum L., catalase, in silico.,

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