“3,4-dihydroxyphenylacetate 2,3-dioxygenase”的意思、由来-开放百科全书

词条

3,4-dihydroxyphenylacetate 2,3-dioxygenase

释义

Structural studies
References

{{enzyme
| Name = 3,4-dihydroxyphenylacetate 2,3-dioxygenase
| EC_number = 1.13.11.15
| CAS_number = 37256-56-7
| IUBMB_EC_number = 1/13/11/15
| GO_code = 0008687
| image =
| width =
| caption =
}}

In enzymology, a 3,4-dihydroxyphenylacetate 2,3-dioxygenase ({{EC number|1.13.11.15}}) is an enzyme that catalyzes the chemical reaction

3,4-dihydroxyphenylacetate + O₂ 2-hydroxy-5-carboxymethylmuconate semialdehyde

Thus, the two substrates of this enzyme are 3,4-dihydroxyphenylacetate and O₂, whereas its product is 2-hydroxy-5-carboxymethylmuconate semialdehyde.

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 oxygen incorporated need not be derived from O₂. The systematic name of this enzyme class is 3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (decyclizing). Other names in common use include 3,4-dihydroxyphenylacetic acid 2,3-dioxygenase, HPC dioxygenase, and homoprotocatechuate 2,3-dioxygenase. This enzyme participates in tyrosine metabolism. It employs one cofactor, iron.

Structural studies

As of late 2007, eight structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1F1R}}, {{PDB link|1F1U}}, {{PDB link|1F1V}}, {{PDB link|1F1X}}, {{PDB link|1Q0C}}, {{PDB link|1Q0O}}, {{PDB link|2IG9}}, and {{PDB link|2IGA}}.

References

{{cite journal | vauthors = Adachi K, Takeda Y, Senoh S, Kita H | title = Metabolism of P-Hydroxyphenylacetic Acid In Pseudomonas ovalis | journal = Biochimica et Biophysica Acta | volume = 93 | pages = 483–93 | date = December 1964 | pmid = 14263147 | doi = 10.1016/0304-4165(64)90332-0 }}
{{cite journal | vauthors = Barbour MG, Bayly RC | title = Control of meta-cleavage degradation of 4-hydroxyphenylacetate in Pseudomonas putida | journal = Journal of Bacteriology | volume = 147 | issue = 3 | pages = 844–50 | date = September 1981 | pmid = 6895079 | pmc = 216120 }}
{{cite journal | vauthors = Kutty RK, Devi NA, Veeraswamy M, Ramesh S, Rao PV | title = Degradation of (+/-)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde | journal = The Biochemical Journal | volume = 167 | issue = 1 | pages = 163–70 | date = October 1977 | pmid = 588248 | pmc = 1183633 }}

3 : EC 1.13.11|Iron enzymes|Enzymes of known structure

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