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Literature summary for 2.3.1.35 extracted from

  • Iqbal, A.; Clifton, I.J.; Bagonis, M.; Kershaw, N.J.; Domene, C.; Claridge, T.D.; Wharton, C.W.; Schofield, C.J.
    Anatomy of a simple acyl intermediate in enzyme catalysis: combined biophysical and modeling studies on ornithine acetyl transferase (2009), J. Am. Chem. Soc., 131, 749-757.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Streptomyces clavuligerus P0DJQ5 isoform OAT2
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Reaction

Reaction Comment Organism Reaction ID
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