Monooxygenase: Difference between revisions

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<StructureSection load='5tkh' size='350' side='right' scene='' caption='Glycosylated lytic polysaccharide monooxygenase complex with Cu(II) (orange) and peroxide (PDB code [[5tkh]])' >
<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 ==
== Function ==


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</StructureSection>
</StructureSection>
==3D structures of monooxygenase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*'''Toluene 4-monooxygenase (TMO)'''
**[[3dhg]], [[3i5j]], [[2inc]] – PmTMO α+β+γ subunits + Fe – ''Pseudomonas mendocina''<br />
**[[2ind]] – PmTMO α+β+γ subunits + Mn <br />
**[[3rng]], [[3rnf]], [[3rne]], [[3rnc]], [[3rnb]], [[3rna]], [[3rn9]], [[3n20]], [[3n1z]], [[3n1y]], [[3n1x]], [[2rdb]] – PmTMO α+β+γ subunits (mutant) + Fe <br />
**[[1sjg]] – PmTMO protein C + Fe <br />
**[[1vm9]] – PmTMO protein C (mutant) + Fe <br />
**[[2bf5]], [[2bf3]], [[2bf2]] – PmTMO protein D <br />
**[[4wqm]] – PmTMO (mutant) + Ni <br />
**[[4p1c]], [[4p1b]] – PmTMO protein A+B+E+ferredoxin (mutant) + Fe <br />
**[[2q3w]] – PmTMO ferredoxin subunit (mutant) + Fe <br />
*TMO complexes
**[[3dhh]], [[3q3n]], [[3q3o]] – PmTMO α+β+γ subunits + Fe + phenol derivative + TMO system effector protein<br />
**[[3rmk]], [[1t0s]], [[1t0q]]  – 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 />
**[[5tdv]] – PmTMO protein A+B+D+E + Fe + peroxide<br />
**[[5tdu]] – PmTMO protein A+B+D+E + Fe + cresol<br />
**[[5tdt]] – PmTMO protein A+B+D+E + Fe + peroxide + toluene<br />
**[[5tds]] – PmTMO protein A+B+D+E + Fe + toluene<br />
**[[1t0r]] – PsTMO + Fe + OH – ''Pseudomonas stutzeri''<br />
*'''Heme-degrading monooxygenase (IsdI)'''
**[[2zdp]] – SaIsdI + heme-Co – ''Staphylococcus aureus''<br />
**[[3lgm]], [[2zdo]] – 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 />
**[[4nl5]] – MtMO + heme + CN – ''Mycobacterium tuberculosis''<br />
**[[4oz5]] – MO + heme – ''Bacillus subtilis''<br />
*'''Kynurenine 3-monooxygenase (KMO)'''
**[[5x68]] – hKMO + FAD - human<br />
**[[4j2w]], [[4j31]], [[4j33]], [[4j34]] – yKMO + FAD – yeast<br />
**[[4j36]], [[5x64]] – yKMO + FAD + inhibitor<br />
**[[5x6q]] – yKMO (mutant) + FAD + inhibitor<br />
**[[5na5]], [[5x6p]] – PfKMO (mutant) + FAD – ''Pseudomonas fluorescens''<br />
**[[5y7a]], [[5y77]], [[6fox]] – PfKMO + FAD + kynurenine <br />
**[[5nak]] – PfKMO (mutant) + FAD + kynurenine <br />
**[[5y66]] – PfKMO + FAD + kynurenine + inhibitor<br />
**[[6fph]], [[6fp1]], [[6fp0]], [[6foz]], [[6foy]] – PfKMO + FAD + inhibitor<br />
**[[5nah]], [[5nag]], [[5nae]], [[5nab]], [[5n7t]], [[5mzk]], [[5mzi]], [[5mzc]], [[5fn0]] – PfKMO (mutant) + FAD + inhibitor<br />
*'''Phenol 2-monooxygenase (PMO)'''
**[[1foh]] – TcPMO + FAD – ''Trichosporon cutaneum''<br />
**[[1pn0]] – TcPMO + FAD + phenol<br />
*'''Phenylalanine 2-monooxygenase'''
**[[5pah]], [[6pah]] – hFMO catalytic domain + inhibitor <br />
*Phenylalanine 4-monooxygenase or phenylalanine-4-hydroxylase
See [[Hydroxylase]]
*'''ActVA-Orf6 monooxygenase (AOMO)'''
**[[1lq9]] – ScAOMO – ''Streptomyces coelicolor''<br />
**[[1n5q]] – ScAOMO + sancycline <br />
**[[1n5s]], [[1n5t]] – ScAOMO + acetyl dithranol<br />
**[[1n5v]] – ScAOMO + nanaomycine <br />
*Baeyer-Villiger monooxygenase (BVMO)
**[[6jdk]] – BVMO – ''Parvibaculum lavamentivorans''<br />
*'''Flavin-containing monooxygenase'''
**[[2gv8]] – fyMO + FAD + NADP – fission yeast<br />
**[[2gvc]] – fyMO + FAD + NADP + methimazole<br />
**[[4a9w]] – SmMO + FAD – ''Stenotrophomonas maltophilia''<br />
**[[4c5o]] – SmMO (mutant) + FAD <br />
**[[5wan]] – EcMO + FMN + uracil – Escherichia coli<br />
**[[5iq4]], [[5iq1]], [[5ipy]] – RnMO (mutant) + FAD + NAP – ''Roseovarius nubinhibens'' <br />
**[[5gsn]] – RnMO (mutant) + FAD + NAP + methimazole <br />
**[[4usr]] – PsMO + FAD <br />
**[[3rp6]] – KpMO + FAD – ''Klebsiella pneumoniae''<br />
**[[3rp8]] – KpMO (mutant) + FAD <br />
**[[3rp7]] – KpMO + FAD + uric acid<br />
**[[3c96]], [[2rgj]] – PaMO + FAD – ''Pseudomonas aeruginosa''<br />
**[[2xvf]], [[2xve]] – MaMO + FAD – ''Methylophaga aminisulfidivorans'' <br />
**[[2xvj]] – MaMO (mutant) + FAD + indole <br />
**[[2xvi]] – MaMO (mutant) + FAD + O2<br />
**[[2vqb]] – MaMO (mutant) + FAD + NADP + O2<br />
**[[2xvh]], [[2xlu]], [[2xlt]] – MaMO + FAD + NADP derivative<br />
**[[2xls]], [[2xlr]], [[2xlp]], [[2vq7]] – MaMO (mutant) + FAD + NADP <br />
**[[5nmw]] – ZvMO + FAD – ''Zonocerus variegatus''<br />
**[[5nmx]] – ZvMO + FAD + NADP <br />
*2,4,6-trichlorophenol 4-monooxygenase
**[[4g5e]] – MO – ''Cupriavidus necator''<br />
*Chlorophenol 4-monooxygenase
**[[4oo2]] – MO – ''Streptomyces globisporus''<br />
**[[3k86]], [[3hwc]] – BcMO – ''Burkholderia cepacia'' <br />
**[[3k87]] – BcMO + FAD  <br />
**[[3k88]] – BcMO + FAD + NAD  <br />
*Phenylacetone monooxygenase
**[[4ovi]], [[4c74]] – TfMO + FAD + APADP – ''Thermobifida fusca''<br />
**[[1w4x]] – TfMO + FAD<br />
**[[2ylt]], [[2yls]], [[2ylr]] – TfMO + FAD + NADP <br />
**[[2ylz]] – TfMO (mutant) + FAD  <br />
**[[4c77]] – TfMO (mutant) + FAD + APADP <br />
**[[4d04]] – TfMO (mutant) + FAD + NAP <br />
**[[4d03]], [[2ym2]], [[2ylx]], [[2ylw]] – TfMO (mutant) + FAD + NADP <br />
**[[2ym1]] – TfMO (mutant) + FAD + NADP + O2<br />
*6-hydroxynicotinate 3-monooxygenase
**[[5eow]] – PpMO + FAD – ''Pseudomonas putida''<br />
*Styrene monooxygenase
**[[3ihm]] – PpMO  <br />
**[[4f07]] – PpMO (mutant) + FAD <br />
*Tryptophan 2-monooxygenase
**[[4iv9]] – MO + FAD – ''Pseudomonas savastanoi''<br />
*Tryptophan 5-monooxygenase
**[[1mlw]] – hMO + Fe + dihydrobiopterin <br />
*Tyrosine 3-monooxygenase
**[[2xsn]] – hMO + Zn<br />
**[[2toh]] – rMO + Fe + dihydrobiopterin + tyrosine - rat<br />
**[[2mda]] – rMO regulatory domain <br />
*Nitronate monooxygenase
**[[4q4k]] – PaMO + FMN <br />
**[[6e2a]] – PaMO + FMN + NAD<br />
**[[5lsm]] – MO + FMN – ''Shewanella oneidensis''<br />
**[[6bka]] – MO + FMN – ''Cyberlyndnera mrakii''<br />
*2-hydroxbiphenyl 3-monooxygenase
**[[4z2r]] – PnMO + FAD – ''Pseudomonas nitroreducens''<br />
**[[4cy6]] – PnMO (mutant)  <br />
**[[4z2u]], [[4z2t]], [[4cy8]] – PnMO (mutant) + FAD <br />
**[[5brt]] – PnMO + FAD + hydroxybephenyl <br />
*4-hydroxyphenylacetate 3-monooxygenase
**[[4ira]] – BmMO + FAD – ''Brucella melitensis''<br />
**[[3cb0]] – BmMO + FMN<br />
**[[6eb0]] – EcMO oxygenase subunit<br />
**[[6b1b]] – EcMO oxygenase subunit (mutant)<br />
*Ornithine N(5)-monooxygenase
**[[5cku]] – MO + FAD + NADP + ornithine – ''Neosartorya fumigata''<br />
**[[4nzh]], [[4b69]] – AfMO + FAD + ornithine – ''Aspergillus fumigatus''<br />
**[[4b65]] – AfMO + FAD + NADP  <br />
**[[4b68]], [[4b66]] – AfMO + FAD + NAP + arginine <br />
**[[4b67]], [[4b63]] – AfMO + FAD + NADP + ornithine <br />
**[[4b64]] – AfMO + FAD + NADP + lysine <br />
**[[3s61]] – PaMO + FAD + NADP + ornithine derivative<br />
*Steroid monooxygenase
**[[4ap1]], [[4aos]] – RrMO + FAD + NADP – ''Rhodococcus rhodochrous''<br />
**[[4aox]] – RrMO (mutant) + FAD <br />
**[[4ap3]] – RrMO (mutant) + FAD + NADP <br />
*Cyclohexanone monooxygenase
**[[5m10]] – TmMO + FAD + NAP + nicotinamide – ''Thermocripsum municipale''<br />
**[[5m0z]] – TmMO + FAD + NADP derivative <br />
**[[6gqi]] – TmMO + FAD + NADP + hexanic acid <br />
**[[6era]], [[6er9]] – RhMO + FAD + NADP – ''Rhodococcus''<br />
**[[4rg4]], [[4rg3]], [[3gwf]], [[3gwd]] – RhMO + FAD + NAP + caprolactone <br />
**[[3ucl]] – RhMO + FAD + NADP + cyclohexanone <br />
*Lysine 6-monooxygenase
**[[5cqf]] – MO – ''Pseudomonas syringae''<br />
**[[4d7e]] – NfMO (mutant) + FAD – ''Nocardia farcinica''<br />
**[[5o8p]] – EaMO + FAD – ''Erwinia amylovora''<br />
**[[5o8r]] – EaMO + FAD + NADP <br />
*EDTA monooxygenase
**[[5dqp]] – MO – ''Chelativorans''<br />
*Rifampicin monooxygenase or Pentachlorophenol 4-monooxygenase
**[[5vqb]] – SvMO + FAD – ''Sterptomyces venezuelae''<br />
**[[6brd]] – SvMO (mutant) + FAD + rifampicin <br />
**[[5kow]] – NfMO + FAD <br />
**[[5kox]] – NfMO + FAD + rifampicin <br />
*3,6-diketocamphane 1,6 monooxygenase
**[[5aec]] – PpMO <br />
**[[4uwm]] – PpMO + FMN<br />
*Lytic polysaccharide monooxygenase
**[[5tki]], [[5foh]], [[4qi8]] – NcMO-2 + Cu – ''Neurospora crassa''''Italic text''<br />
**[[5tkh]], [[5tkg]], [[5tkf]], [[4eir]] – NcMO-2 + Cu + O2 <br />
**[[4eis]] – NcMO-3 + Cu + peroxide <br />
**[[5iju]] – MO + Cu – ''Bacillus amyloliquefaciens''<br />
**[[5acj]], [[5aci]], [[5ach]], [[5acg]], [[5acf]] – MO + Cu – ''Lentinus similis''<br />
**[[4mai]] – moMO + Cu – mold<br />
**[[4mah]] – moMO + Zn<br />
**[[5no7]] – MO – ''Pycnoporus cinnabarinus''<br />
*Peptidyl-glycine alpha-amidating monooxygenase
**[[5mw0]], [[5wkw]] – rMO <br />
**[[1yjl]] – rMO (mutant)<br />
**[[3mib]], [[3mic]], [[3mid]], [[3mie]], [[3mif]], [[3mig]], [[3mih]], [[3mlj]], [[3mlk]], [[3mll]], [[1opm]] – rMO + Cu + Ni <br />
**[[6ao6]], [[5wja]] – rMO (mutant) + Cu + Ni<br />
**[[1sdw]] – rMO + Cu + Ni + O2 + threonine derivative<br />
**[[1yjk]], [[1yip]], [[1phm]] – rMO + Cu<br />
**[[1yi9]], [[6ay0]], [[6an3]], [[6amp]], [[6alv]], [[6ala]] – rMO (mutant) + Cu<br />
**[[3fw0]] – rMO + Hg<br />
**[[3fvz]] – rMO + Zn + Fe<br />
*Antibiotic biosynthesis monooxygenase
**[[4hl9]] – MO – ''Rhodospirillum rubrum''<br />
**[[4dn9]] – MO – ''Chloroflexus aurantiacus''<br />
**[[2ril]] – MO – ''Shewanella loihica''<br />
*Monooxygenase
**[[2i7g]] – MO – ''Agrobacterium tumefaciens''<br />
**[[5uq4]] – MtMO <br />
**[[5f5l]] – MiMO – ''Micromonospora'' <br />
**[[5f5n]] – MiMO + NAD + substrate  <br />
*Monooxygenase TROPB
**[[6nes]] – TsMO + FAD – ''Talaromyces stipitatus''<br />
**[[6nev]], [[6neu]] – TsMO (mutant) + FAD <br />
**[[6net]] – TsMO + FAD + dihydroxy dimethylbenzaldehyde<br />
*Lactate 2-monooxygenase or lactate oxydase
**[[6dvi]] – MsLMO + FMN – ''Mycobacterium smegmatis''<br />
**[[6dvh]] – MsLMO (mutant) + FMN <br />
*Squalene monooxygenase or squalene epoxidase
**[[6c6r]], [[6c6p]], [[6c6n]] – hSMO + FAD + inhibitor<br />
*Dimethyl-sulfide monooxygenase
**[[6ak1]] – DMOA – ''Hyphomicrobium sulfonivorans''<br />
*Salicylate 1-monooxygenase or salicylate hydroxylase
See [[Hydroxylase]]
'''Methane monooxygenase''' See [[Methane monooxygenase]]
'''Camphor 5-monooxygenase''' See [[Cytochrome P450]]
'''Luciferin 4-monooxygenase and Alkanal monooxygenase''' See [[Luciferase]]
}}


== References ==
== References ==

Revision as of 14:17, 3 November 2019

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.

Peptidylglycine α-Hydroxylating Monooxygenase (PHM)-coordination of peroxide to CuM center. Structural and computational study [1]

In recent years there has been a significant interest in describing the interactions of copper-containing enzymes with O2/H2O2-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 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.

Structural and other studies showed that peptidylglycine α-hydroxylating monooxygenase (PHM) contains . 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, . The Å. This Cu(II)-bound , forming . 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


Glycosylated lytic polysaccharide monooxygenase complex with Cu(II) (orange) and peroxide (PDB code 5tkh)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Rudzka K, Moreno DM, Eipper B, Mains R, Estrin DA, Amzel LM. Coordination of peroxide to the Cu(M) center of peptidylglycine alpha-hydroxylating monooxygenase (PHM): structural and computational study. J Biol Inorg Chem. 2012 Dec 18. PMID:23247335 doi:10.1007/s00775-012-0967-z

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