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OJVRTM

 

Online Journal of Veterinary Research©

(Including Medical and Laboratory Research)

Established 1994

ISSN 1328-925X

 

Volume 28 (8): 445-455, 2024.

 In silico endogenous superoxide dismutase from Dinoccocus radiodurans.

 

Ashokan KV, Pillai MM.

 

PVP College, Kavathe Mahankal, Sangli, Mharashtrea, KIIT Engineering, Gokulshirgoan, Kolhapur, India

 

ABSTRACT

 

Ashokan KV, Pillai MM., In silico endogenous superoxide dismutase from Dinoccocus radiodurans, Onl J Vet Res., 28 (8): 445-455, 2024. We report copper In Silico (Cu), zinc (Zn) superoxide dismutase protein of Dinococcus radiodurans R1. Primary sequence was determined by positive charged arginine and lysine alkaline >7 (9.8) and ~54% hydrophobicity. We found 1 myristic, 3 phosphorylated and 1 N-glycosylated sites. Secondary structure showed predominant β-turn disulphide bonds. We identified Cu, Zn superoxide dismutase (SOD) binding, 6 bladed propeller, TOIB and SMP-30/Gluconolaconase/LRE. Findings suggested Cu, Zn SOD binding is part of oxidoreductase fold and metal binding, TOIB peptidoglycan lipoprotein and SMP-30 domain assigned as hydrolyzing enzyme which protects stress against aging. The 3D- structure of domains are imaged.   

 

Key words: In silico, Cu, Zn superoxide dismutase, Dinococcus radiodurans. 3D Image.

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