artsp-hod
Arthrobacter sp. Arthrobacter ilicis Arthrobacter nitroguajacolicus RU61A, Paenarthrobacter nitroguajacolicus hod gene 1h-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) HodC
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. Other strains: Arthrobacter sp. Arthrobacter ilicis Arthrobacter nitroguajacolicus RU61A
Relationship
Family : HOD-cofactorfree-dioxygenase
Block : X
Position in NCBI Life Tree : Arthrobacter sp.
(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 > Terrabacteria group N E > Actinobacteria [phylum] N E > Actinobacteria [class] N E > Micrococcales N E > Micrococcaceae N E > Arthrobacter N E > Arthrobacter sp. N EMolecular evidence
No mutation
2WJ3 - Crystal structure of the cofactor-devoid 1-H-3-hydroxy-4- oxoquinaldine 2,4-dioxygenase (HOD) from Arthrobacter nitroguajacolicus RU61A
2WJ4 - Crystal structure of the cofactor-devoid 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) from Arthrobacter nitroguajacolicus RU61A anaerobically complexed with its natural substrate 1-H-3-hydroxy-4-oxoquinaldine
2WJ6 - Crystal structure of the cofactor-devoid 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) from Arthrobacter nitroguajacolicus RU61A anaerobically complexed with its natural substrate N-acetylanthranilate
2WM2 - Crystal structure of the cofactor-devoid 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) from Arthrobacter nitroguajacolicus RU61A anaerobically complexed with its chloride
4CFS - Crystal structure of the cofactor-devoid 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) catalytically inactive H251A variant complexed with its natural substrate 1-H-3-hydroxy-4-oxoquinaldine
7OJM - Crystal structure of the cofactor-devoid 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) catalytically inactive H251A variant complexed with 2-methyl-quinolin-4(1H)-one under normoxic conditions
7OKZ - Crystal structure of the cofactor-devoid 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) catalytically inactive H251A variant complexed with 2-methyl-quinolin-4(1H)-one under hyperoxic conditions
8A97 - Room temperature crystal structure of the cofactor-devoid 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) under xenon pressure (30 bar)
8ORO - Crystal structure of the cofactor-devoid 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) catalytically inactive S101A variant complexed with 2-methyl-quinolin-4(1H)-one (40 bar O2)
8OXN - Crystal structure of the cofactor-devoid 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) catalytically inactive S101A variant complexed with 2-methyl-quinolin-4(1H)-one (air)
8OXT - Crystal structure of the cofactor-devoid 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) catalytically inactive H251A variant complexed with NAA (40 bar O2 \/ QND turnover)
No kinetic
No disease
No inhibitor
Sequence
Peptide
MTDTYLHETL VFDNKLSYID NQRDTDGPAI LLLPGWCHDH RVYKYLIQEL DADFRVIVPN WRGHGLSPCE VPDFGYQEQV KDALEILDQL GVETFLPVSH SHGGWVLVEL LEQAGPERAP RGIIMDWLMW APKPDFAKSL TLLKDPERWR EGTHGLFDVW LDGHDEKRVR HHLLEEMADY GYDCWGRSGR VIEDAYGRNG SPMQMMANLT KTRPIRHIFS QPTEPEYEKI NSDFAEQHPW FSYAKLGGPT HFPAIDVPDR AAVHIREFAT AIRQGQ
References (13)
| Title : Evolutionary adaptation from hydrolytic to oxygenolytic catalysis - Bui_2023_bioRxiv__ |
| Author(s) : Bui S , Gil-Guerrero S , van der Linden P , Carpentier P , Ceccarelli M , Jambrina PG , Steiner RA |
| Ref : Biorxiv , : , 2023 |
| Abstract : |
| PubMedSearch : Bui_2023_bioRxiv__ |
| PubMedID: |
| Gene_locus related to this paper: artsp-hod |
| Title : Evolutionary adaptation from hydrolytic to oxygenolytic catalysis at the alpha\/beta fold - Bui_2023_Chem.Sci_14_10547 |
| Author(s) : Bui S , Gil-Guerrero S , van der Linden P , Carpentier P , Ceccarelli M , Jambrina PG , Steiner RA |
| Ref : Chem Sci , 14 :10547 , 2023 |
| Abstract : |
| PubMedSearch : Bui_2023_Chem.Sci_14_10547 |
| PubMedID: 37799987 |
| Gene_locus related to this paper: artsp-hod |
| Title : Enzyme-Mediated Quenching of the Pseudomonas Quinolone Signal (PQS): A Comparison between Naturally Occurring and Engineered PQS-Cleaving Dioxygenases - Arranz San Martin_2022_Biomolecules_12_170 |
| Author(s) : Arranz San Martin A , Vogel J , Wullich SC , Quax WJ , Fetzner S |
| Ref : Biomolecules , 12 :170 , 2021 |
| Abstract : |
| PubMedSearch : Arranz San Martin_2022_Biomolecules_12_170 |
| PubMedID: |
| Gene_locus related to this paper: artsp-hod , strbb-d7bw96 , mycab-x8en65 , nocfa-q5yp20 |
| 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 : |
| 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 : |
| 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 : Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha\/beta-hydrolase-fold superfamily - Steiner_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_382 |
| Author(s) : Steiner RA , Frerichs-Deeken U , Fetzner S |
| Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 63 :382 , 2007 |
| Abstract : |
| PubMedSearch : Steiner_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_382 |
| PubMedID: 17565176 |
| Gene_locus related to this paper: artsp-hod |
| Title : Complete nucleotide sequence of the 113-kilobase linear catabolic plasmid pAL1 of Arthrobacter nitroguajacolicus Ru61a and transcriptional analysis of genes involved in quinaldine degradation - Parschat_2007_J.Bacteriol_189_3855 |
| Author(s) : Parschat K , Overhage J , Strittmatter AW , Henne A , Gottschalk G , Fetzner S |
| Ref : Journal of Bacteriology , 189 :3855 , 2007 |
| Abstract : |
| PubMedSearch : Parschat_2007_J.Bacteriol_189_3855 |
| PubMedID: 17337569 |
| Gene_locus related to this paper: artsp-hod |
| Title : Dioxygenases without requirement for cofactors: identification of amino acid residues involved in substrate binding and catalysis, and testing for rate-limiting steps in the reaction of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase - Frerichs-Deeken_2005_Curr.Microbiol_51_344 |
| Author(s) : Frerichs-Deeken U , Fetzner S |
| Ref : Curr Microbiol , 51 :344 , 2005 |
| Abstract : |
| PubMedSearch : Frerichs-Deeken_2005_Curr.Microbiol_51_344 |
| PubMedID: 16187153 |
| Gene_locus related to this paper: artsp-hod |
| Title : Dioxygenases without requirement for cofactors and their chemical model reaction: compulsory order ternary complex mechanism of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion - Frerichs-Deeken_2004_Biochemistry_43_14485 |
| Author(s) : Frerichs-Deeken U , Ranguelova K , Kappl R , Huttermann J , Fetzner S |
| Ref : Biochemistry , 43 :14485 , 2004 |
| Abstract : |
| PubMedSearch : Frerichs-Deeken_2004_Biochemistry_43_14485 |
| PubMedID: 15533053 |
| Gene_locus related to this paper: artsp-hod |
| Title : Gene cluster of Arthrobacter ilicis Ru61a involved in the degradation of quinaldine to anthranilate: characterization and functional expression of the quinaldine 4-oxidase qoxLMS genes - Parschat_2003_J.Biol.Chem_278_27483 |
| Author(s) : Parschat K , Hauer B , Kappl R , Kraft R , Huttermann J , Fetzner S |
| Ref : Journal of Biological Chemistry , 278 :27483 , 2003 |
| Abstract : |
| PubMedSearch : Parschat_2003_J.Biol.Chem_278_27483 |
| PubMedID: 12730200 |
| Gene_locus related to this paper: artsp-hod |
| 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 : |
| PubMedSearch : Fetzner_2002_Appl.Microbiol.Biotechnol_60_243 |
| PubMedID: 12436305 |
| Gene_locus related to this paper: artsp-hod , psepu-QDO |
| Title : Molecular cloning, sequencing, expression, and site-directed mutagenesis of the 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase gene from Arthrobacter spec. Ru61a - Betz_2000_J.Basic.Microbiol_40_7 |
| Author(s) : Betz A , Facey SJ , Hauer B , Tshisuaka B , Lingens F |
| Ref : J Basic Microbiol , 40 :7 , 2000 |
| Abstract : |
| PubMedSearch : Betz_2000_J.Basic.Microbiol_40_7 |
| PubMedID: 10746195 |
| Gene_locus related to this paper: artsp-hod |
| 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 : |
| PubMedSearch : Bauer_1996_Eur.J.Biochem_240_576 |
| PubMedID: 8856057 |
| Gene_locus related to this paper: artsp-hod , psepu-QDO |