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Literature summary for 1.17.4.1 extracted from
- Site-specific replacement of Y356 with 3,4-dihydroxyphenylalanine in the beta2 subunit of E. coli ribonucleotide reductase (2006), J. Am. Chem. Soc., 128, 2522-2523.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | site-specific replacement of Y356 with 3,4-dihydroxyphenylalanine in the beta2 subunit and trapping the 3,4-dihydroxyphenylalanine radical intermediate in the presence of alpha2 subunit dimer, substrate and effector ATP or TTP. 3,4-Dihydroxyphenylalanine radical formation shows fast and slow phases, rapid phases are substrate-mediated conformational changes that place about 50% of the alpha2beta2 complex into an active conformation for turnover. Substrate plays a major role in conformational gating | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
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