|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
- 3,4-dihydroxybenzoate + O2 3-carboxy-cis,cis-muconate
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The systematic name of this enzyme class is protocatechuate:oxygen 3,4-oxidoreductase (decyclizing). Other names in common use include protocatechuate oxygenase, protocatechuic acid oxidase, protocatechuic 3,4-dioxygenase, and protocatechuic 3,4-oxygenase. This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, iron.
This enzyme has been found effective at improving organic fluorophore-stability in single-molecule experiments.
As of late 2007, 37 structures have been solved for this class of enzymes, with PDB accession codes 1EO2, 1EO9, 1EOA, 1EOB, 1EOC, 1YKK, 1YKL, 1YKM, 1YKN, 1YKO, 1YKP, 2BUM, 2BUQ, 2BUR, 2BUT, 2BUU, 2BUV, 2BUW, 2BUX, 2BUY, 2BUZ, 2BV0, 2PCD, 3PCA, 3PCB, 3PCC, 3PCD, 3PCE, 3PCF, 3PCG, 3PCH, 3PCI, 3PCJ, 3PCK, 3PCL, 3PCM, and 3PCN.
- Fujisawa H, Hayaishi O (1968). "Protocatechuate 3,4-dioxygenase. I. Crystallization and characterization". J. Biol. Chem. 243 (10): 2673–81. PMID 4967959.
- GROSS SR, GAFFORD RD, TATUM EL (1956). "The metabolism of protocatechuic acid by Neurospora". J. Biol. Chem. 219 (2): 781–96. PMID 13319299.
- Stanier RY and Ingraham JL (1954). "Protocatechuic acid oxidase". J. Biol. Chem. 210 (2): 799–820. PMID 13211618.
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