Monooxygenase: Difference between revisions

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Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman

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-<StructureSection load='3lgn' size='340' side='right' caption='Structure of heme-degrading monooxygenase with Fe containing heme complex with O2 molecule and Mg+2 (green) (PDB code [[3lgn]]).' scene=''>
+<StructureSection load='5tkh' size='350' side='right' scene='' caption='Glycosylated lytic polysaccharide monooxygenase complex with Cu(II) (orange) and peroxide (PDB code [[5tkh]])' >
+__TOC__
 == Function ==
-'''Monooxygenases''' (MO) catalyzes the incorporation of a hydroxyl group into a variety of substrates.  MO catalyzes the reduction of O2 to H2O while oxidating NADPH.
+'''Monooxygenases''' (MO) catalyzes the incorporation of a hydroxyl group into a variety of substrates.  MO catalyzes the reduction of O<sub>2</sub> to H<sub>2</sub>O while oxidating NADPH.
+*'''ActVA-Orf6 monooxygenase''' catalyses the oxidation of an aromatic intermediate of the actinorhodin pathway <ref>PMID:12514126</ref>.
-== Disease ==
+*'''Baeyer-Villigen monooxygenase''' is a bioanalytic tool which can catalyze reactions which are difficult to do via chemical means<ref>PMID:15599520</ref>.
+*'''TropB monooxygenase''' catalyses asymmetric oxidative dearomatization reactions <ref>PMID:31346489</ref>.
+*'''TetX monooxygenase''' inactivates the tetracycline antibiotic <ref>PMID:15452119</ref>.
+*'''Phenol 2-monooxygenase''' see [[Phenol hydroxylase (hebrew)]].
-== Relevance ==
+=== Peptidylglycine α-Hydroxylating Monooxygenase (PHM)-coordination of peroxide to Cu<sub>M</sub> center. Structural and computational study <ref >doi 10.1007/s00775-012-0967-z</ref>===
-== Structural highlights ==
+In recent years there has been a significant interest in describing the interactions of copper-containing enzymes with O<sub>2</sub>/H<sub>2</sub>O<sub>2</sub>-derived species. The short-lived intermediates resulting from the activation of dioxygen are the key players in the mechanistic cycles in many metalloenzymes. In the enzyme <scene name='Journal:JBIC:17/Cv/3'>peptidylglycine alpha-hydroxylating monooxygenase (PHM)</scene> various reduced Cu/oxygen species have been proposed to act as catalytically competent intermediates, yet their exact nature and their role in the enzymatic reaction is still unknown.
-</StructureSection>
+Structural and other studies showed that peptidylglycine &#945;-hydroxylating monooxygenase (PHM) contains <scene name='Journal:JBIC:17/Cv/4'>two non-equivalent copper sites (CuH and CuM)</scene>. CuM serves as an oxygen binding and hydrogen abstraction site, CuH is involved in electron transfer. In the structure of Cu(II)-PHM complexed with hydrogen peroxide determined to 1.98 Å resolution, <scene name='Journal:JBIC:17/Cv/7'>(hydro)peroxide binds exclusively to CuM in a slightly asymmetric side-on mode</scene>. The <scene name='Journal:JBIC:17/Cv/8'>interatomic O-O distance of the copper-bound ligand is 1.5, characteristic of peroxide/hydroperoxide species, and the copper-oxygen distances are 2.0 and 2.1</scene> Å. This Cu(II)-bound <scene name='Journal:JBIC:17/Cv/9'>peroxo moiety interacts closely with a molecule of water</scene>, forming <scene name='Journal:JBIC:17/Cv/10'>hydrogen bonds that stabilize the structure</scene>. DFT and QM/MM calculations indicate that this species is a Cu-bound doubly deprotonated peroxidate and that its energy is similar to that of its isomer Cu(I)-bound superoxide.
 ==3D structures of monooxygenase==
+[[Monooxygenase 3D structures]]
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+</StructureSection>
-{{#tree:id=OrganizedByTopic|openlevels=0|
-*'''Toluene 4-monooxygenase (TMO)'''
-**[[3dhg]], [[3i5j]] – PmTMO α+β+γ subunits + Fe – ''Pseudomonas mendocina''<br />
-**[[1sjg]] – PmTMO protein C + Fe <br />
-**[[1vm9]] – PmTMO protein C (mutant) + Fe <br />
-*TMO complexes
-**[[3dhh]], [[3q3n]], [[3q3o]] – PmTMO α+β+γ subunits + Fe + phenol derivative + TMO system effector protein<br />
-**[[3rmk]] – PmTMO α+β+γ subunits + Fe + phenol derivative<br />
-**[[3q14]] – PmTMO α+β+γ subunits + Fe + p-cresol + TMO system effector protein<br />
-**[[3q2a]], [[3q3m]] – PmTMO α+β+γ subunits + Fe + benzoate inhibitor + TMO system effector protein<br />
-**[[3dhi]] – PmTMO α+β+γ subunits + Fe + TMO system effector protein<br />
-**[[3ge3]], [[3ge8]], [[3ri7]] – PmTMO α (mutant)+β+γ subunits + Fe + TMO system effector protein<br />
-**[[3i63]] – PmTMO α+β+γ subunits + Fe + TMO system effector protein + H2O2<br />
-'''Luceferin 4-monooxygenase and Alkanal monooxygenase''' See [[Luciferase]]
-*'''Heme-degrading monooxygenase (IsdI)'''
-**[[2zdp]] – SaIsdI + heme-Co – ''Staphylococcus aureus''<br />
-**[[3lgm]] – SaIsdI + heme-Fe<br />
-**[[4fnh]] – SaIsdI (mutant) + heme-Fe<br />
-**[[3lgn]] – SaIsdI + heme-Fe + O2<br />
-**[[3qgp]] – SaIsdI + heme-Fe + CN<br />
-**[[4fni]] – SaIsdI (mutant) + heme-Fe + CN<br />
-*'''Kynurenine 3-monooxygenase (KMO)'''
-**[[4j2w]], [[4j31]], [[4j33]], [[4j34]] – yKMO + FAD – yeast<br />
-**[[4j36]] – yKMO + FAD + inhibitor<br />
-*'''Phenol 2-monooxygenase (PMO)'''
-**[[1foh]] – TcPMO + FAD – ''Trichosporon cutaneum''<br />
-**[[1pn0]] – TcPMO + FAD + phenol<br />
-*'''Phenylalanine 2-monooxygenase'''
-**[[5pah]], [[6pah]]. – FMO catalytic domain + inhibitor – human<br />
-*'''ActVA-Orf6 monooxygenase (AOMO)'''
-**[[1lq9]] – ScAOMO – ''Streptomyces coelicolor''<br />
-**[[1n5q]] – ScAOMO + sancycline <br />
-**[[1n5s]], [[1n5t]] – ScAOMO + acetyl dithranol<br />
-**[[1n5v]] – ScAOMO + nanaomycine <br />
-*'''Flavin-containing monooxygenase'''
-**[[2gv8]] – fyMO + FAD + NADP – fission yeast<br />
-**[[2gvc]] – fyMO + FAD + NADP + methimazole<br />
-**[[4a9w]] – MO + FAD – ''Stenotrophomonas maltophilia''<br />
-**[[2i7g]] – MO – ''Agrobacterium tumefaciens''<br />
-'''Methane monooxygenase''' See [[Methane monooxygenase]]
-'''Camphor 5-monooxygenase''' See [[Cytochrome P450]]
-}}
 == References ==