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 E

Molecular evidence

No mutation

8A97 - Room temperature crystal structure of the cofactor-devoid 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) under xenon pressure (30 bar) 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) 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) 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) 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 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 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

No kinetic

No disease

No inhibitor

Database

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 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
PubMedID: 37799987
Gene_locus related to this paper: artsp-hod

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
PubMedID:
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
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
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 : 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
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
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
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
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
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
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
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
PubMedID: 8856057
Gene_locus related to this paper: artsp-hod , psepu-QDO