Artikel ; Online: Effects of Distal Mutations on Prolyl-Adenylate Formation of Escherichia coli Prolyl-tRNA Synthetase.
2020 Band 39, Heft 5, Seite(n) 542–553
Abstract: Enzymes play important roles in many biological processes. Amino acid residues in the active site pocket of an enzyme, which are in direct contact with the substrate(s), are generally believed to be critical for substrate recognition and catalysis. ... ...
| Abstract | Enzymes play important roles in many biological processes. Amino acid residues in the active site pocket of an enzyme, which are in direct contact with the substrate(s), are generally believed to be critical for substrate recognition and catalysis. Identifying and understanding how these "catalytic" residues help enzymes achieve enormous rate enhancement has been the focus of many structural and biochemical studies over the past several decades. Recent studies have shown that enzymes are intrinsically dynamic and dynamic coupling between distant structural elements is essential for effective catalysis in modular enzymes. Therefore, distal residues are expected to have impact on enzyme function. However, few studies have investigated the role of distal residues on enzymatic catalysis. In the present study, the effects of distal residue mutations on the catalytic function of an aminoacyl-tRNA synthetase, namely, prolyl-tRNA synthase, were investigated. The present study demonstrates that distal residues significantly contribute to catalysis of the modular Escherichia coli prolyl-tRNA synthetase by maintaining intrinsic protein flexibility. |
|---|---|
| Mesh-Begriff(e) | Amino Acyl-tRNA Synthetases/chemistry ; Amino Acyl-tRNA Synthetases/genetics ; Amino Acyl-tRNA Synthetases/metabolism ; Catalysis ; Catalytic Domain ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Mutation |
| Chemische Substanzen | Escherichia coli Proteins ; Amino Acyl-tRNA Synthetases (EC 6.1.1.-) ; prolyl T RNA synthetase (EC 6.1.1.15) |
| Sprache | Englisch |
| Erscheinungsdatum | 2020-07-17 |
| Erscheinungsland | Netherlands |
| Dokumenttyp | Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't |
| ZDB-ID | 2143071-8 |
| ISSN | 1875-8355 ; 1572-3887 |
| ISSN (online) | 1875-8355 |
| ISSN | 1572-3887 |
| DOI | 10.1007/s10930-020-09910-3 |
| Datenquelle | MEDical Literature Analysis and Retrieval System OnLINE |
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