HOD-cofactorfree-dioxygenase
Relationship
Comment
1h-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) Oxygenases without requirement for cofactors or metal ions, catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Composed of a classical alpha/beta-hydrolase fold core domain with a cap domain. Organic substrates undergo selective deprotonation of their hydroxyl group by a His/Asp charge-relay system affording the generation of electron-donating species. The oxyanion hole of the alpha/beta-hydrolase fold, is utilized here to host and control oxygen chemistry involving a peroxide anion intermediate. Product release occurs by proton back transfer from the catalytic histidine.It is a non-nucleophilic general-base mechanismDatabase
Interpro : No interpro
PIRSF : No PIRSF
Pdoc : No Pdoc
Pfam : PF12697 Abhydrolase_6
Prints : No Print
EC Number : No EC Number
References (8)
| Title : Definition of an alpha\/beta-hydrolase fold subfamily comprising Pseudomonas quinolone signal cleaving dioxygenases - Wullich_2020_Appl.Environ.Microbiol__ |
| Author(s) : Wullich SC , Arranz San Martin A , Fetzner S |
| Ref : Applied Environmental Microbiology , : , 2020 |
| Abstract : Wullich_2020_Appl.Environ.Microbiol__ |
| ESTHER : Wullich_2020_Appl.Environ.Microbiol__ |
| PubMedSearch : Wullich_2020_Appl.Environ.Microbiol__ |
| PubMedID: 32086305 |
| Title : Structural basis for recognition and ring-cleavage of the Pseudomonas quinolone signal (PQS) by AqdC, a mycobacterial dioxygenase of the alpha\/beta-hydrolase fold family - Wullich_2019_J.Struct.Biol_207_287 |
| Author(s) : Wullich SC , Kobus S , Wienhold M , Hennecke U , Smits SHJ , Fetzner S |
| Ref : J Struct Biol , 207 :287 , 2019 |
| Abstract : Wullich_2019_J.Struct.Biol_207_287 |
| ESTHER : Wullich_2019_J.Struct.Biol_207_287 |
| PubMedSearch : Wullich_2019_J.Struct.Biol_207_287 |
| PubMedID: 31228546 |
| Gene_locus related to this paper: mycab-x8en65 |
| Title : Origin of the proton-transfer step in the cofactor-free (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase: effect of the basicity of an active site His residue - Hernandez-Ortega_2014_J.Biol.Chem_289_8620 |
| Author(s) : Hernandez-Ortega A , Quesne MG , Bui S , Heuts DP , Steiner RA , Heyes DJ , de Visser SP , Scrutton NS |
| Ref : Journal of Biological Chemistry , 289 :8620 , 2014 |
| Abstract : Hernandez-Ortega_2014_J.Biol.Chem_289_8620 |
| ESTHER : Hernandez-Ortega_2014_J.Biol.Chem_289_8620 |
| PubMedSearch : Hernandez-Ortega_2014_J.Biol.Chem_289_8620 |
| PubMedID: 24482238 |
| Gene_locus related to this paper: artsp-hod |
| Title : Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha\/beta-hydrolase fold - Steiner_2010_Proc.Natl.Acad.Sci.U.S.A_107_657 |
| Author(s) : Steiner RA , Janssen HJ , Roversi P , Oakley AJ , Fetzner S |
| Ref : Proc Natl Acad Sci U S A , 107 :657 , 2010 |
| Abstract : Steiner_2010_Proc.Natl.Acad.Sci.U.S.A_107_657 |
| ESTHER : Steiner_2010_Proc.Natl.Acad.Sci.U.S.A_107_657 |
| PubMedSearch : Steiner_2010_Proc.Natl.Acad.Sci.U.S.A_107_657 |
| PubMedID: 20080731 |
| Gene_locus related to this paper: artsp-hod , psepu-QDO |
| Title : Oxygenases without requirement for cofactors or metal ions - Fetzner_2002_Appl.Microbiol.Biotechnol_60_243 |
| Author(s) : Fetzner S |
| Ref : Applied Microbiology & Biotechnology , 60 :243 , 2002 |
| Abstract : Fetzner_2002_Appl.Microbiol.Biotechnol_60_243 |
| ESTHER : Fetzner_2002_Appl.Microbiol.Biotechnol_60_243 |
| PubMedSearch : Fetzner_2002_Appl.Microbiol.Biotechnol_60_243 |
| PubMedID: 12436305 |
| Gene_locus related to this paper: artsp-hod , psepu-QDO |
| Title : Site-directed mutagenesis of potential catalytic residues in 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase, and hypothesis on the catalytic mechanism of 2,4-dioxygenolytic ring cleavage - Fischer_2000_FEMS.Microbiol.Lett_190_21 |
| Author(s) : Fischer F , Fetzner S |
| Ref : FEMS Microbiology Letters , 190 :21 , 2000 |
| Abstract : Fischer_2000_FEMS.Microbiol.Lett_190_21 |
| ESTHER : Fischer_2000_FEMS.Microbiol.Lett_190_21 |
| PubMedSearch : Fischer_2000_FEMS.Microbiol.Lett_190_21 |
| PubMedID: 10981684 |
| Gene_locus related to this paper: psepu-QDO |
| Title : Bacterial 2,4-dioxygenases: new members of the alpha\/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases - Fischer_1999_J.Bacteriol_181_5725 |
| Author(s) : Fischer F , Kunne S , Fetzner S |
| Ref : Journal of Bacteriology , 181 :5725 , 1999 |
| Abstract : Fischer_1999_J.Bacteriol_181_5725 |
| ESTHER : Fischer_1999_J.Bacteriol_181_5725 |
| PubMedSearch : Fischer_1999_J.Bacteriol_181_5725 |
| PubMedID: 10482514 |
| Gene_locus related to this paper: psepu-QDO |
| Title : 2,4-dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33\/1 - Bauer_1996_Eur.J.Biochem_240_576 |
| Author(s) : Bauer I , Max N , Fetzner S , Lingens F |
| Ref : European Journal of Biochemistry , 240 :576 , 1996 |
| Abstract : Bauer_1996_Eur.J.Biochem_240_576 |
| ESTHER : Bauer_1996_Eur.J.Biochem_240_576 |
| PubMedSearch : Bauer_1996_Eur.J.Biochem_240_576 |
| PubMedID: 8856057 |
| Gene_locus related to this paper: artsp-hod , psepu-QDO |
Structures (15)
Genes Proteins in HOD-cofactorfree-dioxygenase family (37)
No fragment of genes
Structures in HOD-cofactorfree-dioxygenase family (15)Substrates in HOD-cofactorfree-dioxygenase family (6)
Inhibitors in HOD-cofactorfree-dioxygenase family (1)