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{{Short description|Class of enzymes}}
{{infobox enzyme
| Name = mandelate 4-monooxygenase
| EC_number = 1.14.16.6
| CAS_number = 39459-82-0
| GO_code = 0050481
| image =
| width =
| caption =
}}
In [[enzymology]], a '''mandelate 4-monooxygenase''' ({{EC number|1.14.16.6}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
In [[enzymology]], a '''mandelate 4-monooxygenase''' ({{EC number|1.14.16.6}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]


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The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[(S)-2-hydroxy-2-phenylacetate]], [[tetrahydrobiopterin]], and [[oxygen|O<sub>2</sub>]], whereas its 3 [[product (chemistry)|products]] are [[(S)-4-hydroxymandelate]], [[dihydrobiopterin]], and [[water|H<sub>2</sub>O]].
The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[(S)-2-hydroxy-2-phenylacetate]], [[tetrahydrobiopterin]], and [[oxygen|O<sub>2</sub>]], whereas its 3 [[product (chemistry)|products]] are [[(S)-4-hydroxymandelate]], [[dihydrobiopterin]], and [[water|H<sub>2</sub>O]].


This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced pteridine as one donor, and incorporation of one ato of oxygen into the other donor. The systematic name of this enzyme class is '''(S)-2-hydroxy-2-phenylacetate,tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating)'''. Other names in common use include '''L-mandelate 4-hydroxylase''', and '''mandelic acid 4-hydroxylase'''. It employs one [[cofactor (biochemistry)|cofactor]], [[iron]].
This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced pteridine as one donor, and incorporation of one ato of oxygen into the other donor. The [[List of enzymes|systematic name]] of this enzyme class is '''(S)-2-hydroxy-2-phenylacetate,tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating)'''. Other names in common use include '''L-mandelate 4-hydroxylase''', and '''mandelic acid 4-hydroxylase'''. It employs one [[cofactor (biochemistry)|cofactor]], [[iron]].


==References==
==References==
{{reflist|1}}
{{reflist|1}}
* {{cite journal | vauthors = Bhat SG, Vaidyanathan CS | date = 1976 | title = Purifications and properties of L-mandelate- 4-hydroxylase from Pseudomonas convexa | journal = Arch. Biochem. Biophys. | volume = 176 | pages = 314&ndash;23 | pmid = 9909 | doi = 10.1016/0003-9861(76)90170-3 | issue = 1 }}
{{Enzyme references|EC_number=1.14.16.6|IUBMB_EC_number=1/14/16/6}}
* {{cite journal | author = Bhat SG, Vaidyanathan CS | date = 1976 | title = Purifications and properties of L-mandelate- 4-hydroxylase from Pseudomonas convexa | journal = Arch. Biochem. Biophys. | volume = 176 | pages = 314&ndash;23 | pmid = 9909 | doi = 10.1016/0003-9861(76)90170-3 }}


{{Dioxygenases}}
==External links==
{{Enzymes}}
::''The [[CAS registry number]] for this enzyme class is {{CAS registry|39459-82-0}}.''
{{Portal bar|Biology|border=no}}
{{Enzyme links|EC_number=1.14.16.6|IUBMB_EC_number=1/14/16/6}}

===Gene Ontology (GO) codes===
{{GO code links | GO_code=0050481 | name=mandelate 4-monooxygenase}}

{{1.14-enzyme-stub}}


[[Category:EC 1.14.16]]
[[Category:EC 1.14.16]]
[[Category:Iron enzymes]]
[[Category:Iron enzymes]]
[[Category:Enzymes of unknown structure]]
[[Category:Enzymes of unknown structure]]


{{1.14-enzyme-stub}}

Latest revision as of 14:51, 26 August 2023

mandelate 4-monooxygenase
Identifiers
EC no.1.14.16.6
CAS no.39459-82-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a mandelate 4-monooxygenase (EC 1.14.16.6) is an enzyme that catalyzes the chemical reaction

(S)-2-hydroxy-2-phenylacetate + tetrahydrobiopterin + O2 (S)-4-hydroxymandelate + dihydrobiopterin + H2O

The 3 substrates of this enzyme are (S)-2-hydroxy-2-phenylacetate, tetrahydrobiopterin, and O2, whereas its 3 products are (S)-4-hydroxymandelate, dihydrobiopterin, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced pteridine as one donor, and incorporation of one ato of oxygen into the other donor. The systematic name of this enzyme class is (S)-2-hydroxy-2-phenylacetate,tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating). Other names in common use include L-mandelate 4-hydroxylase, and mandelic acid 4-hydroxylase. It employs one cofactor, iron.

References

[edit]
  • Bhat SG, Vaidyanathan CS (1976). "Purifications and properties of L-mandelate- 4-hydroxylase from Pseudomonas convexa". Arch. Biochem. Biophys. 176 (1): 314–23. doi:10.1016/0003-9861(76)90170-3. PMID 9909.