HOD-cofactorfree-dioxygenase

Relationship

Family: HOD-cofactorfree-dioxygenase

Block: X

Parent Family: Abhydrolase_6

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

Database

Interpro : No interpro

PIRSF : No PIRSF

Pdoc : No Pdoc

Pfam : PF12697 Abhydrolase_6

Prints : No Print

EC Number : No EC Number

Sequences

Peptide in Fasta
Nucleotide in Fasta
Alignment with Multalin Text only
Seed alignment with MAFFT No colour
Alignment with MAFFT No colour
Dendrogram The dnd file

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)

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
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
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
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
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 : 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