In silico analyses of predicted substitutions in fibrinolytic protein ‘Lumbrokinase-6’ suggest enhanced activity

[Display omitted] •Lumbrokinases are group of serine proteases.•Serine found at position 214 in lumbrokinase improved the activity of lumbrokinase.•In silico tools were used for characterization of mutant Lk-6 proteins.•Serine-Valin214 substitution were direct activation of breaking Arg561-Val562 bo...

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Veröffentlicht in:	Process biochemistry (1991) 2021-11, Vol.110, p.292-301
Hauptverfasser:	Munawar, Sadam, Sagir, Muhammad, Mustafa, Ghulam, Ali, Muhammad Amjad, Niazi, Adnan Khan, Parvaiz, Aqsa, Yasmin, Farkhanda, Mansoor, Farukh, Kanwal, Shamsa, Rasheed, Majeeda, Kehfulvara, Hafiza, Ali, Habib, Ullah, Sami, Al-Sehemi, Abdullah G., Khan, Muhammad Sarwar, Joyia, Faiz Ahmad
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Fibrin Fibrinolytics Genetic engineering Glutamic acid In silico tools Lk-6 Molecular docking Molecular modelling Molecular structure Mutants Mutation Phylogeny Plasmin Proline Protein engineering Protein interaction Protein structure Proteins Proteolysis Serine Serine proteinase Substitutes Substitution mutation Substrates Thromboembolism Thrombosis Valine
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