Mandelate 4-monooxygenase: Difference between revisions
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{{Short description|Class of enzymes}} |
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{{enzyme |
{{infobox enzyme |
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| Name = mandelate 4-monooxygenase |
| Name = mandelate 4-monooxygenase |
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| EC_number = 1.14.16.6 |
| EC_number = 1.14.16.6 |
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| CAS_number = 39459-82-0 |
| CAS_number = 39459-82-0 |
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| GO_code = 0050481 |
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| IUBMB_EC_number = 1/14/16/6 |
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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]]. |
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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]]. |
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==References== |
==References== |
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{{reflist|1}} |
{{reflist|1}} |
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* {{cite journal | |
* {{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 = 314–23 | pmid = 9909 | doi = 10.1016/0003-9861(76)90170-3 | issue = 1 }} |
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{{Dioxygenases}} |
{{Dioxygenases}} |
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{{Enzymes}} |
{{Enzymes}} |
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{{Portal bar|Biology|border=no}} |
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[[Category:EC 1.14.16]] |
[[Category:EC 1.14.16]] |
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[[Category:Iron enzymes]] |
[[Category:Iron enzymes]] |
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[[Category:Enzymes of unknown structure]] |
[[Category:Enzymes of unknown structure]] |
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Latest revision as of 14:51, 26 August 2023
| mandelate 4-monooxygenase | |||||||||
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| Identifiers | |||||||||
| EC no. | 1.14.16.6 | ||||||||
| CAS no. | 39459-82-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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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.
