词条 | Protocatechuate 3,4-dioxygenase |
释义 |
| Name = protocatechuate 3,4-dioxygenase | EC_number = 1.13.11.3 | CAS_number = 9029-47-4 | IUBMB_EC_number = 1/13/11/3 | GO_code = 0018578 | image = 3pca.jpg | width = 270 | caption = Protocatechuate 3,4-dioxygenase hetero24mer, Pseudomonas putida }} In enzymology, a protocatechuate 3,4-dioxygenase ({{EC number|1.13.11.3}}) is an enzyme that catalyzes the chemical reaction 3,4-dihydroxybenzoate + O2 3-carboxy-cis,cis-muconate 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 sp generally require further purification to remove strong contaminating nuclease activity. Structural studiesAs of late 2007, 37 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1EO2}}, {{PDB link|1EO9}}, {{PDB link|1EOA}}, {{PDB link|1EOB}}, {{PDB link|1EOC}}, {{PDB link|1YKK}}, {{PDB link|1YKL}}, {{PDB link|1YKM}}, {{PDB link|1YKN}}, {{PDB link|1YKO}}, {{PDB link|1YKP}}, {{PDB link|2BUM}}, {{PDB link|2BUQ}}, {{PDB link|2BUR}}, {{PDB link|2BUT}}, {{PDB link|2BUU}}, {{PDB link|2BUV}}, {{PDB link|2BUW}}, {{PDB link|2BUX}}, {{PDB link|2BUY}}, {{PDB link|2BUZ}}, {{PDB link|2BV0}}, {{PDB link|2PCD}}, {{PDB link|3PCA}}, {{PDB link|3PCB}}, {{PDB link|3PCC}}, {{PDB link|3PCD}}, {{PDB link|3PCE}}, {{PDB link|3PCF}}, {{PDB link|3PCG}}, {{PDB link|3PCH}}, {{PDB link|3PCI}}, {{PDB link|3PCJ}}, {{PDB link|3PCK}}, {{PDB link|3PCL}}, {{PDB link|3PCM}}, and {{PDB link|3PCN}}. See also
References1. ^{{cite journal | vauthors = Aitken CE, Marshall RA, Puglisi JD | year = 2008 | title = An Oxygen Scavenging System for Improvement of Dye Stability in Single-Molecule Fluorescence Experiments | journal = Biophys. J. | volume = 94 | pages = 1826–1835 | doi = 10.1529/biophysj.107.117689 | pmid = 17921203 | issue = 5 | pmc = 2242739 }}
4 : EC 1.13.11|Iron enzymes|Enzymes of known structure|Natural phenols metabolism |
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