Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step
Han Zhang et al. report molecular dynamics simulations and mutational analysis of a key process of the E. coli glycine cleavage system, an important enzyme complex in C1 metabolism. They identify a key amino acid residue controlling the release of the swinging aminomethyl lipoate arm and increase th...
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| Autores principales: | , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2020
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/78e895b2a82e49aea72b3a9bd99928e3 |
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| Sumario: | Han Zhang et al. report molecular dynamics simulations and mutational analysis of a key process of the E. coli glycine cleavage system, an important enzyme complex in C1 metabolism. They identify a key amino acid residue controlling the release of the swinging aminomethyl lipoate arm and increase the overall reaction rate of glycine cleavage by more than twice, providing a strategy for manipulating this reaction system for use in synthetic biology. |
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