EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.2.3.1 | comparative QM/MM calculations. The base that abstracts a proton from the attacking water is the epsilon-amino group of Lys61 rather than the phosphate ion. The phosphate ion is important for stabilizing the transition state of the normal transaldimination to form L-threonine by making a hydrogen bond with the hydroxy group of the L-threonine moiety. Proposal of a mechanism, in which a proton temporarily resides at the phenolate O3' of pyridoxal-5'-phosphate, for the transaldimination process | Thermus thermophilus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.3.1 | Thermus thermophilus | - |
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EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.2.3.1 | ThrS | - |
Thermus thermophilus |