Investigating effect of mutation on structure and function of G6PD enzyme: a comparative molecular dynamics simulation study

Investigating effect of mutation on structure and function of G6PD enzyme: a comparative molecular dynamics simulation study

Several natural mutants of the human G6PD enzyme exist and have been reported. Because the enzymatic activities of many mutants are different from that of the wildtype, the genetic polymorphism of G6PD plays an important role in the synthesis of nucleic acids via ribulose-5-phosphate and formation o...

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Bibliographic Details
Main Authors: Anwar, J. (Author), Malik, F.P (Author), Rani, S. (Author), Zafar Paracha, R. (Author)
Format: Article
Language:English
Published: PeerJ Inc. 2022
Subjects:
amino acid sequence
Article
Binding free energy
binding site
Binding site
catalysis
Catalysis
cholesterol metabolism
comparative study
computer model
conformational transition
controlled study
crystal structure
enzyme active site
enzyme activity
enzyme kinetics
enzyme structure
gene mutation
genetic polymorphism
glucose 6 phosphate dehydrogenase
glucose 6 phosphate dehydrogenase deficiency
human
hydrophobicity
Keywords G6PD mutants
ligand binding
mathematical analysis
MD simulations
molecular docking
molecular dynamics
molecular mechanics
nicotinamide adenine dinucleotide phosphate
physiology
protein function
protein secondary structure
protein stability
protein structure
reactive oxygen metabolite
receptor binding assay
sequence alignment
simulation
site directed mutagenesis
static electricity
Structural stability
structure activity relation
three-dimensional imaging
X ray analysis
X ray crystallography
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