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

Family : HOD-cofactorfree-dioxygenase

Block : X

Position in NCBI Life Tree : Pseudomonas putida

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)

> cellular organisms N E > Bacteria N E > Proteobacteria N E > Gammaproteobacteria N E > Pseudomonadales N E > Pseudomonadaceae N E > Pseudomonas N E > Pseudomonas putida group N E > Pseudomonas putida N E

Molecular evidence

No mutation

No kinetic

No disease

No inhibitor

Database

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 (7)

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
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
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
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
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
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
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
PubMedID: 1515060
Gene_locus related to this paper: psepu-QDO