Mechanistic Insight into the Cleavage Site Specificity of Collagenase VhaC to the Y-G Bonds in Collagen.
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| Format: | Artículo científico |
| Language: | en |
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Journal of agricultural and food chemistry
2025
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| author | Zhao, Wen-Xiao Liu, Rui Wang, Dan-Dan Gao, Chao Wang, Peng Cao, Hai-Yan Chen, Xiu-Lan Wang, Yan Zhang, Yu-Zhong |
| author_facet | Zhao, Wen-Xiao Liu, Rui Wang, Dan-Dan Gao, Chao Wang, Peng Cao, Hai-Yan Chen, Xiu-Lan Wang, Yan Zhang, Yu-Zhong Zhao, Wen-Xiao Liu, Rui Wang, Dan-Dan Gao, Chao Wang, Peng Cao, Hai-Yan Chen, Xiu-Lan Wang, Yan Zhang, Yu-Zhong |
| collection | PubMed - marine biology |
| contents | Mechanistic Insight into the Cleavage Site Specificity of Collagenase VhaC to the Y-G Bonds in Collagen. Zhao, Wen-Xiao Liu, Rui Wang, Dan-Dan Gao, Chao Wang, Peng Cao, Hai-Yan Chen, Xiu-Lan Wang, Yan Zhang, Yu-Zhong Substrate Specificity Collagen Collagenases Bacterial Proteins Vibrio Amino Acid Sequence Binding Sites Kinetics Amino Acid Motifs M9 collagenases have various biotechnological and medical applications due to their high activity and specificity to collagen. Although the collagenolytic mechanism of M9 collagenases has been studied, the molecular basis for their cleavage site specificity remains unknown. Here, the mechanism of the Y-G bond cleavage site specificity of M9 collagenase VhaC was studied. The double-G motif (G441 and G442) and Y549 of VhaC define a narrow S1' substrate binding pocket responsible for P1' substrate binding, among which Y549 functions as the structural determinant for the specific recognition of P1' glycine, because its bulky side chain restricts the accommodation of residues with a side chain. The S1' tyrosine corresponding to Y549 in VhaC is strictly conserved among M9 collagenases, suggesting its significance in the cleavage site specificity. This study advances the applications of M9 collagenases in disease treatment and collagen oligopeptide production. |
| format | Artículo científico |
| id | pubmed_40845237 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Journal of agricultural and food chemistry |
| record_format | pubmed |
| spellingShingle | Mechanistic Insight into the Cleavage Site Specificity of Collagenase VhaC to the Y-G Bonds in Collagen. Zhao, Wen-Xiao Liu, Rui Wang, Dan-Dan Gao, Chao Wang, Peng Cao, Hai-Yan Chen, Xiu-Lan Wang, Yan Zhang, Yu-Zhong Substrate Specificity Collagen Collagenases Bacterial Proteins Vibrio Amino Acid Sequence Binding Sites Kinetics Amino Acid Motifs Mechanistic Insight into the Cleavage Site Specificity of Collagenase VhaC to the Y-G Bonds in Collagen. Zhao, Wen-Xiao Liu, Rui Wang, Dan-Dan Gao, Chao Wang, Peng Cao, Hai-Yan Chen, Xiu-Lan Wang, Yan Zhang, Yu-Zhong Substrate Specificity Collagen Collagenases Bacterial Proteins Vibrio Amino Acid Sequence Binding Sites Kinetics Amino Acid Motifs M9 collagenases have various biotechnological and medical applications due to their high activity and specificity to collagen. Although the collagenolytic mechanism of M9 collagenases has been studied, the molecular basis for their cleavage site specificity remains unknown. Here, the mechanism of the Y-G bond cleavage site specificity of M9 collagenase VhaC was studied. The double-G motif (G441 and G442) and Y549 of VhaC define a narrow S1' substrate binding pocket responsible for P1' substrate binding, among which Y549 functions as the structural determinant for the specific recognition of P1' glycine, because its bulky side chain restricts the accommodation of residues with a side chain. The S1' tyrosine corresponding to Y549 in VhaC is strictly conserved among M9 collagenases, suggesting its significance in the cleavage site specificity. This study advances the applications of M9 collagenases in disease treatment and collagen oligopeptide production. |
| title | Mechanistic Insight into the Cleavage Site Specificity of Collagenase VhaC to the Y-G Bonds in Collagen. |
| topic | Substrate Specificity Collagen Collagenases Bacterial Proteins Vibrio Amino Acid Sequence Binding Sites Kinetics Amino Acid Motifs |
| url | https://pubmed.ncbi.nlm.nih.gov/40845237/ |