Crystallization (Comment) | Organism |
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native crystal structures at pH 4.2 at a resolution of 1.18 A, and at pH 7.3 at a resolution of 1.23 A. At pH 4.2 the enzyme is assigned as a tetrapeptide, Asp-Ala-Ile-Tyr, whereas at pH 7.3 it is assigned as a tyrosine molecule and a leucine molecule existing at equal occupancies in both of the SGPB molecules in the asymmetric unit | synthetic construct |
Organism | UniProt | Comment | Textmining |
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synthetic construct | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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additional information | upon the formation of the tetrahedral intermediate, residues Glu192A to Gly193 of SGPB move towards the alpha-carboxylate O of residue P1 of the bound species, and adjustments in the side-chain conformational angles of His57 and Ser195 of SGPB favor the progression of the catalytic mechanism of SGPB | synthetic construct | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
SGPB | - |
synthetic construct |