Antibacterial based on IPBCC.08.610 glucose oxidase against UDP-N-acetyl glucosamine enolpyruvyl transferase and elongation factor G enzymes in silico

5th International Seminar on Sciences

自然科学（总论）

Hakim, M.R.^1 ; Sumaryada, T.^2 ; Ambarsari, L.^1

Department of Biochemistry, IPB University, Bogor

16680, Indonesia^1

Department of Physics, IPB University, Bogor

16680, Indonesia^2

关键词: Antibacterials;    Computational investigation;    Elongation factor;    Enzyme catalysis;    Gene sequences;    Gluconic acids;    Gluconolactone;    N acetyls;   

Others  :  https://iopscience.iop.org/article/10.1088/1755-1315/299/1/012035/pdf
DOI  :  10.1088/1755-1315/299/1/012035

学科分类：自然科学（综合）

来源: IOP

【 摘 要 】

The use of a synthetic antibacterial agent as food preservatives could develop several health problems thus the user should be reduced. Enzyme-based antibacterial is a natural antibacterial that could substitute the latter antibacterials. Enzyme-based antibacterials have several ways that can be used to inactivate microbes, one of them utilize enzyme catalysis products. The aim of this research is to study the interaction between IPBCC.08.610 glucose oxidase (NCBI accession number MH593586) catalysis product against MurA and EFG enzymes using computational investigation. We confirmed that the gene sequence from previous research is truly encoding the IPBCC.08.610 glucose oxidase. Gluconolactone and gluconic acid are less effectively absorbed by microbes. Gluconolactone and gluconic acid are capable to interact with Cys115 and Asp305 of MurA, meanwhile, it does not interact with Phe90 and Thr84 of EFG. Gluconolactone and gluconic acid can inhibit MurA effectively but not on EFG.