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  4. Regulation of directed mutations of Asp-68 and Tyr-70 in H-protein on the overall enzyme activity of the glycine cleavage system
 
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Regulation of directed mutations of Asp-68 and Tyr-70 in H-protein on the overall enzyme activity of the glycine cleavage system

Publikationstyp
Journal Article
Date Issued
2021-11-20
Sprache
Chinese
Author(s)
Zhang, Han  
Li, Yuchen  
Nie, Jinglei  
Ren, Jie  
Zeng, An-Ping  orcid-logo
Institut
Bioprozess- und Biosystemtechnik V-1  
TORE-URI
http://hdl.handle.net/11420/11397
Journal
Beijing Huagong Daxue Xuebao  
Volume
48
Issue
6
Start Page
48
End Page
56
Citation
Beijing Huagong Daxue Xuebao - Natural Science Edition 48 (6): 48-56 (2021-11-20)
Publisher DOI
10.13543/j.bhxbzr.2021.06.007
Scopus ID
2-s2.0-85121665760
The reductive glycine pathway is considered to be the most promising one carbon (C1) synthesis pathway, and its core enzyme is the glycine cleavage system (GCS). In a previous study, we preliminarily identified the potential key amino acid residues in the H-protein cavity as Ser-67, Asp-68 and Tyr-70 in a study of the "unlocking self-protection" process of H-protein in the glycine cleavage system, and showed that the Ser-67 site had an important impact on the overall enzyme activity of the glycine cleavage system. In this paper, side-chain positively charged mutations (H-D68K, H-D68H, H-D68R and H-Y70K, H-Y70H, H-Y70R mutants) and side-chain nonpolar mutations (H-D68G, H-D68V, H-D68M, H-D68L and H-Y70G, H-Y70V, H-Y70M, H-Y70L mutants) were performed on the Asp-68 and Tyr-70 sites of H-protein, and the enzyme activities of each mutant in the glycine cleavage direction were determined. The results showed that positively charged mutations at Asp-68 tended to decrease the overall enzyme activity of the glycine cleavage system, while nonpolar mutations at Asp-68, positively charged mutations and nonpolar mutations at Tyr-70 tended to maintain or increase the overall enzyme activity. Compared with the wild-type H-protein, the enzyme activity of the H-D68R mutant decreased by 90.2%, and those of H-Y70R, H-D68G and H-Y70L mutant increased by 75.6%, 53.6% and 146%, respectively. An analysis of the interactions between lipoamide and residues in the cavity of H-protein showed that the change in the overall enzyme activity of the glycine cleavage system was due to the mutation at 68 and 70 residues of H-protein that hinders or promotes the release of lipoamide.
Subjects
C1 synthesis
Glycine cleavage system
H-protein
Reductive glycine pathway
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