Crystallization (Comment) | Organism |
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crystallization of OAT2 in the presence of N-alpha-acetyl-L-glutamate leads to a structure in which residue T181 is acetylated, the carbonyl oxygen of the acyl-enzyme complex is located in an oxyanion hole and positioned to hydrogen bond with the backbone amide-NH of G112 and the alcohol of T111. Presence of two distinct acyl-enzyme complex structures. The two acyl-enzyme complex structures can interconvert by movement of the T111 side-chain alcohol hydrogen away from the oxyanion hole to hydrogen bond with the backbone carbonyl of the acylated residue, T181 | Streptomyces clavuligerus |
Organism | UniProt | Comment | Textmining |
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Streptomyces clavuligerus | P0DJQ5 | isoform OAT2 | - |
Reaction | Comment | Organism | Reaction ID |
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N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate | residue T181 becomes acetylated and the carbonyl oxygen of the acyl-enzyme complex is located in an oxyanion hole and positioned to hydrogen bond with the backbone amide-NH of G112 and the alcohol of T111. Presence of two distinct acyl-enzyme complex structures which can interconvert by movement of the T111 side-chain alcohol hydrogen away from the oxyanion hole to hydrogen bond with the backbone carbonyl of the acylated residue, T181 | Streptomyces clavuligerus |