Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10140800 | Food Chemistry | 2019 | 8 Pages |
Abstract
This study aimed to determine the characteristics, metabolic pathways and cellular functions of S-nitrosylated proteins from pork postmortem muscle using bioinformatics analysis. The results showed that S-nitrosylated proteins had a broad range of molecular weight and pI value and were mainly located in the functional region of secondary structure. The motif revealed the lysine (K) positioned at â5, â7, +1 and +5 through the S-nitrosocysteine while “C-X-X-C” was identified as the motif for non-S-nitrosylation-modified cysteine. The proteins were widely localized in cell compartments and mostly belonged to enzymes participating in the metabolic process. Glycolysis was the most significant pathways of S-nitrosylated proteins in postmortem muscle. The cell death of muscle cells was predicted to be inhibited by S-nitrosylation with the potential influence on the apoptosis. Those identified pathways and cellular functions of S-nitrosylation are proposed to have a profound influence on meat quality and should be highly regarded.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Rui Liu, Chaoyang Zhang, Lujuan Xing, Lili Zhang, Guanghong Zhou, Wangang Zhang,