psepu-QDO
Pseudomonas putida (Arthrobacter siderocapsulatus). 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase
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 mechanism.
Relationship
Molecular evidence
Sequence
Peptide
MQSLNVNGTL MTYSESGDPH APTLFLLSGW CQDHRLFKNL APLLARDFHV ICPDWRGHDA KQTDSGDFDS QTLAQDLLAF IDAKGIRDFQ MVSTSHGCWV NIDVCEQLGA ARLPKTIVID WLLQPHPGFW QQLAEGQHPT EYVAGRQSFF DEWAETTDNA DVLNHLRNEM PWFHGEMWQR ACREIEANYR TWGSPLDRME SLPQKPEICH IYSQPLSQDY RQLQLDFAAG HSWFHPRHIP GRTHFPSLEN PVAVAQAIRE FLQA
References
| 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 : Cloning, sequence analysis, and expression of the Pseudomonas putida 33\/1 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase gene, encoding a carbon monoxide forming dioxygenase - Max_1999_Biochim.Biophys.Acta_1431_547 |
| Author(s) : Max N , Betz A , Facey S , Lingens F , Hauer B , Fetzner S |
| Ref : Biochimica & Biophysica Acta , 1431 :547 , 1999 |
| Abstract : Max_1999_Biochim.Biophys.Acta_1431_547 |
| ESTHER : Max_1999_Biochim.Biophys.Acta_1431_547 |
| PubMedSearch : Max_1999_Biochim.Biophys.Acta_1431_547 |
| PubMedID: 10350631 |
| 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 |
| Title : Microbial metabolism of quinoline and related compounds. XIV. Purification and properties of 1H-3-hydroxy-4-oxoquinoline oxygenase, a new extradiol cleavage enzyme from Pseudomonas putida strain 33\/1 - Block_1992_Biol.Chem.Hoppe.Seyler_373_343 |
| Author(s) : Block DW , Lingens F |
| Ref : Biol Chem Hoppe Seyler , 373 :343 , 1992 |
| Abstract : Block_1992_Biol.Chem.Hoppe.Seyler_373_343 |
| ESTHER : Block_1992_Biol.Chem.Hoppe.Seyler_373_343 |
| PubMedSearch : Block_1992_Biol.Chem.Hoppe.Seyler_373_343 |
| PubMedID: 1515060 |
| Gene_locus related to this paper: psepu-QDO |