Protocatechuate 3,4-dioxygenase

In enzymology, a protocatechuate 3,4-dioxygenase (EC 1.13.11.3) is an enzyme that catalyzes the chemical reaction

3,4-dihydroxybenzoate + O2 3-carboxy-cis,cis-muconate
protocatechuate 3,4-dioxygenase
Protocatechuate 3,4-dioxygenase hetero24mer, Pseudomonas putida
Identifiers
EC no.1.13.11.3
CAS no.9029-47-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Thus, the two substrates of this enzyme are 3,4-dihydroxybenzoate (protocatechuic acid) and O2, whereas its product is 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.[1] Commercial preps of the enzyme isolated from Pseudomonas spp. generally require further purification to remove strong contaminating nuclease activity.

Structural studies

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.

See also

References
  1. Aitken CE, Marshall RA, Puglisi JD (2008). "An Oxygen Scavenging System for Improvement of Dye Stability in Single-Molecule Fluorescence Experiments". Biophys. J. 94 (5): 1826–1835. Bibcode:2008BpJ....94.1826A. doi:10.1529/biophysj.107.117689. PMC 2242739. PMID 17921203.
  • 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, Ingraham JL (1954). "Protocatechuic acid oxidase". J. Biol. Chem. 210 (2): 799–820. PMID 13211618.


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