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Literature summary for extracted from

  • Huang, Y.; Duan, Y.; Zhang, Y.; Fan, P.; Li, Z.; Liu, W.; Cui, Z.
    Crystal structure of hydroxyquinol 1,2-dioxygenase PnpC from Pseudomonas putida DLL-E4 and its role of N-terminal domain for catalysis (2018), Biochem. Biophys. Res. Commun., 507, 267-273 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structure at 2.1 A resolution. The catalytic Fe(III) is pentacoordinated by the conserved Tyr160, Tyr194, His218 and His220 residues, the citrate anion and one water molecule. Asp80, Thr81 and Val248 are responsible for the substrate specificity. The N-terminal domain is required for its soluble expression and enzyme catalysis Pseudomonas putida


Organism UniProt Comment Textmining
Pseudomonas putida C6FI44


Synonyms Comment Organism
Pseudomonas putida