A bioinformatics study on characteristics, metabolic pathways, and cellular functions of the identified S-nitrosylated proteins in postmortem pork muscle. (15th February 2019)
- Record Type:
- Journal Article
- Title:
- A bioinformatics study on characteristics, metabolic pathways, and cellular functions of the identified S-nitrosylated proteins in postmortem pork muscle. (15th February 2019)
- Main Title:
- A bioinformatics study on characteristics, metabolic pathways, and cellular functions of the identified S-nitrosylated proteins in postmortem pork muscle
- Authors:
- Liu, Rui
Zhang, Chaoyang
Xing, Lujuan
Zhang, Lili
Zhou, Guanghong
Zhang, Wangang - Abstract:
- Highlights: We firstly studied the metabolic pathways of S-nitrosylation in postmortem pork. The motif of S-nitrosylated proteins was explored in postmortem pork muscle. The S-nitrosylated proteins mostly belong to enzyme involved in metabolic process. S-nitrosylation likely inhibits cell death of muscle cells in postmortem pork meat. 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 −5, −7, +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.
- Is Part Of:
- Food chemistry. Volume 274(2019)
- Journal:
- Food chemistry
- Issue:
- Volume 274(2019)
- Issue Display:
- Volume 274, Issue 2019 (2019)
- Year:
- 2019
- Volume:
- 274
- Issue:
- 2019
- Issue Sort Value:
- 2019-0274-2019-0000
- Page Start:
- 407
- Page End:
- 414
- Publication Date:
- 2019-02-15
- Subjects:
- S-nitrosylation -- Properties -- Motif -- Gene ontology -- Integrity pathway analysis
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2018.09.038 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 7966.xml