Information on EC 1.14.13.1 - salicylate 1-monooxygenase:
   PRINT
Please wait a moment until all data are loaded. This message will disappear when all data are loaded.
Mark a special word or phrase in this record:  
Select one or more organisms in this record:

Show additional data Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

Please login to have access to the AMENDA and FRENDA data

EC NUMBERCOMMENTARY
1.14.13.1-

RECOMMENDED NAMEGeneOntology No.
salicylate 1-monooxygenaseGO:0018658

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
salicylate + NADH + 2 H+ + O2 = catechol + NAD+ + H2O + CO2
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
oxidation----
oxidative decarboxylation----
redox reaction----
reduction----

PATHWAYKEGG LinkMetaCyc Link
chlorosalicylate degradation-PWY-6107
methylsalicylate degradation-PWY-6184
salicylate degradation I-PWY-6183

SYSTEMATIC NAMEIUBMB Comments
salicylate,NADH:oxygen oxidoreductase (1-hydroxylating, decarboxylating)A flavoprotein (FAD).

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
NahGPseudomonas sp.--675817
NahGNicotiana tabacum--676519
NahGLotus japonicus, Medicago truncatula--676603
NahGPseudomonas putida--689421, 713130
NahUPseudomonas sp.--675817
oxygenase, salicylate 1-mono-----
salicylate 1-hydroxylase----
salicylate 1-hydroxylasePseudomonas reinekei--651730, 680483, 701143
salicylate 1-hydroxylaseSphingomonas sp.--684569
salicylate hydroxylasePseudomonas reinekeiQ0VH44-651730, 680483
salicylate hydroxylaseFusarium sp.--671441
salicylate hydroxylasePseudomonas sp.--671724, 675817, 710856
salicylate hydroxylaseNicotiana tabacum--676519
salicylate hydroxylaseLotus japonicus, Medicago truncatula--676603
salicylate hydroxylasePseudomonas stutzeri--698002
salicylate hydroxylasePseudomonas putida--700067, 700069, 713130
salicylate hydroxylasePseudomonas fluorescens--700067
salicylate hydroxylaseAlcaligenes sp.--712039
salicylate hydroxylase (decarboxylating)----
salicylate monooxygenase----
salicylate-1-hydroxylaseAlcaligenes sp.--712039
salicylic hydroxylase----
SalOHPseudomonas reinekeiQ0VH44-651730, 680483
SHLPseudomonas sp.--690072, 710856

CAS REGISTRY NUMBERCOMMENTARY
9059-28-3-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Alcaligenes sp.phenanthrene-degrading712039--Manually annotated by BRENDA team
Burkholderia cepacia-390011--Manually annotated by BRENDA team
Emericella nidulans-657557Q9HFQ8SwissProtManually annotated by BRENDA team
Fusarium sp.strain BI671441--Manually annotated by BRENDA team
Fusarium sp. BIstrain BI671441--Manually annotated by BRENDA team
Lotus japonicus-676603--Manually annotated by BRENDA team
Medicago truncatula-676603--Manually annotated by BRENDA team
Nicotiana tabacum-676519--Manually annotated by BRENDA team
Pseudomonas fluorescens-700067--Manually annotated by BRENDA team
Pseudomonas putida-389997, 389998, 390001, 390002, 390003, 390004, 390006, 390007, 390009, 390010, 390013, 390014, 390015, 689421, 700067--Manually annotated by BRENDA team
Pseudomonas putidagene nahG713130--Manually annotated by BRENDA team
Pseudomonas putidastrain BS202-P1, grown on phenanthrene390017--Manually annotated by BRENDA team
Pseudomonas putidastrain ND6700069--Manually annotated by BRENDA team
Pseudomonas putidaUUC-1, strain is capable of utilizing salicylate at high concentrations390016--Manually annotated by BRENDA team
Pseudomonas putida BS202-P1strain BS202-P1, grown on phenanthrene390017--Manually annotated by BRENDA team
Pseudomonas putida ND6strain ND6675817, 700069--Manually annotated by BRENDA team
Pseudomonas reinekeigene salA651730, 680483Q0VH44UniProtManually annotated by BRENDA team
Pseudomonas reinekeistrain MT1701143--Manually annotated by BRENDA team
Pseudomonas reinekei MT1gene salA651730Q0VH44UniProtManually annotated by BRENDA team
Pseudomonas sp.-389999, 390000, 390005, 671724, 686457, 690072, 710856--Manually annotated by BRENDA team
Pseudomonas sp.ATCC 29351390008--Manually annotated by BRENDA team
Pseudomonas sp.ATCC 29352657599--Manually annotated by BRENDA team
Pseudomonas sp.strain ND6675817--Manually annotated by BRENDA team
Pseudomonas stutzeristrain AN10698002--Manually annotated by BRENDA team
Pseudomonas stutzeri AN10strain AN10698002--Manually annotated by BRENDA team
Sphingobium sp.strain P2657732--Manually annotated by BRENDA team
Sphingomonas sp.strain CHY-1684569--Manually annotated by BRENDA team
Sphingomonas sp. CHY-1strain CHY-1684569--Manually annotated by BRENDA team
Trichosporon cutaneum-439423--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
metabolismPseudomonas reinekei-strain MT1 is capable of degrading 4- and 5-chlorosalicylates via 4-chlorocatechol, 3-chloromuconate, and maleylacetate by the chlorocatechol pathway, overview651730
metabolismPseudomonas reinekei-salicylate 1-hydroxylase is not clustered with the meta cleavage pathway680483
metabolismPseudomonas stutzeri-naphthalene degradation698002

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
1-hydroxy-2-naphthoate + NADH + 2 H+ + O2?
show the reaction diagram		Sphingomonas sp.-137% of the activity with salicylate684569--?
1-hydroxy-2-naphthoate + NADH + O21,2-dihydroxynaphthalene + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas putida--390017--?
2,3-dihydroxybenzoate + NADH + O2pyrogallol + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas sp.--389999-389999?
2,3-dihydroxybenzoate + NADH + O2pyrogallol + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas sp.--390000, 390005--?
2,3-dihydroxybenzoate + NADH + O2pyrogallol + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas putida--389997, 390017--?
2,3-dihydroxybenzoate + NADH + O2pyrogallol + CO2 + H2O + NAD+
show the reaction diagram		Trichosporon cutaneum--439423-439423?
2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane + NADHNO2- + N2O + formate + NH4+
show the reaction diagram		Pseudomonas sp.-the enzyme catalyzes two oxygen-sensitive single-electron transfer steps necessary to release two nitrite ions from 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane and this is followed by the secondary decomposition of this energetic chemical657599N2O is abiotically produced from NO2-NH2-?
2,4-dihydroxybenzoate + NAD(P)H + O2benzene-1,2,4-triol + CO2 + H2O + NAD(P)+
show the reaction diagram		Trichosporon cutaneum--439423-439423?
2,4-dihydroxybenzoate + NADH + 2 H+ + O21,2,4-trihydroxybenzene + NAD+ + H2O + CO2
show the reaction diagram		Sphingomonas sp.-91% of the activity with salicylate684569--?
2,5-dihydroxybenzoate + NADH + O2benzene-1,2,5-triol + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas sp.--390000, 390005--?
2,5-dihydroxybenzoate + NADH + O2benzene-1,2,5-triol + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas putida--389997, 390017--?
2,5-dihydroxybenzoate + NADH + O2benzene-1,2,5-triol + CO2 + H2O + NAD+
show the reaction diagram		Trichosporon cutaneum-or NADPH439423-439423?
2,6-dihydroxybenzoate + NADH + 2 H+ + O21,2,3-trihydroxybenzene + NAD+ + H2O + CO2
show the reaction diagram		Sphingomonas sp.-70% of the activity with salicylate684569--?
2,6-dihydroxybenzoate + NADH + O2pyrogallol + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas sp.--389999-389999?
2,6-dihydroxybenzoate + NADH + O2pyrogallol + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas sp.--390000, 390005--?
2,6-dihydroxybenzoate + NADH + O2pyrogallol + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas putida--389997, 390017--?
2,6-dihydroxybenzoate + NADH + O2pyrogallol + CO2 + H2O + NAD+
show the reaction diagram		Trichosporon cutaneum--439423-439423?
2-hydroxy-2-naphthoate + NADH + 2 H+ + O2?
show the reaction diagram		Sphingomonas sp.-160% of the activity with salicylate684569--?
3,5-dinitrosalicylate + NADH + O2? + NAD+ + H2O + CO2
show the reaction diagram		Pseudomonas sp.--675817--?
3-chlorosalicylate + NADH + H+ + O23-chlorocatechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekeiQ0VH44-651730--?
3-chlorosalicylate + NADH + H+ + O23-chlorocatechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekei--680483--?
3-methylsalicylate + NADH + 2 H+ + O23-methylcatechol + NAD+ + H2O + CO2
show the reaction diagram		Sphingomonas sp.-76% of the activity with salicylate684569--?
3-methylsalicylate + NADH + H+ + O23-methylcatechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekei--680483--?
3-methylsalicylate + NADH + O21,2-dihydroxy-3-methylbenzene + CO2 + NAD+ + H2O
show the reaction diagram		Sphingobium sp.--657732--?
3-methylsalicylate + NADH + O21,2-dihydroxy-3-methylbenzene + NAD+ + H2O + CO2
show the reaction diagram		Pseudomonas sp.--675817--?
4-(3-benzothiazol-2-yl-4-cyano-2-oxo-2H-chromen-7-yloxymethyl)-2-hydroxy-benzoic acid + O2 + NADH + 2 H+?
show the reaction diagram		Pseudomonas sp.-i.e. SHLF, two-step synthesis of a long-wavelength latent fluorogenic substrate SHLF. In the presence of NADH and under aerobic conditions, SHL catalyzes the decarboxylative hydroxylation of SHLF followed by a quinonemethide-type rearrangement reaction concomitant with the ejection of a fluorescence coumarin 2, which is spontaneous and irreversible at physiological temperatures in aqueous media. The fluorescence signal generated by this process is specific and, in the near red spectral region with an emission maximum at 595 nm, is suppressed by salicylic acid710856--?
4-aminosalicylate + NADH + O24-aminocatechol + CO2 + NAD+ + H2O
show the reaction diagram		Pseudomonas putida--390017--?
4-aminosalicylate + NADH + O24-aminocatechol + CO2 + NAD+ + H2O
show the reaction diagram		Trichosporon cutaneum--439423--?
4-chlorosalicylate + NADH + H+ + O24-chlorocatechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekeiQ0VH44-651730--?
4-chlorosalicylate + NADH + H+ + O24-chlorocatechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekei--680483--?
4-chlorosalicylate + NADH + O21,2-dihydroxy-4-chlorobenzene + CO2 + NAD+ + H2O
show the reaction diagram		Pseudomonas putida--390017--?
4-chlorosalicylate + NADH + O21,2-dihydroxy-4-chlorobenzene + CO2 + NAD+ + H2O
show the reaction diagram		Trichosporon cutaneum--439423--?
4-chlorosalicylate + NADH + O21,2-dihydroxy-4-chlorobenzene + CO2 + NAD+ + H2O
show the reaction diagram		Sphingobium sp.--657732--?
4-chlorosalicylate + NADH + O24-chlorocatechol + NAD+ + H2O + CO2
show the reaction diagram		Pseudomonas reinekei--701143--?
4-methylsalicylate + NADH + 2 H+ + O24-methylcatechol + NAD+ + H2O + CO2
show the reaction diagram		Sphingomonas sp.-108% of the activity with salicylate684569--?
4-methylsalicylate + NADH + H+ + O24-methylcatechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekei--680483--?
4-methylsalicylate + NADH + O21,2-dihydroxy-4-methylbenzene + CO2 + NAD+ + H2O
show the reaction diagram		Sphingobium sp.--657732--?
5-aminosalicylate + NADH + O25-aminocatechol + CO2 + NAD+ + H2O
show the reaction diagram		Trichosporon cutaneum--439423--?
5-chlorosalicylate + NADH + 2 H+ + O24-chlorocatechol + NAD+ + H2O + CO2
show the reaction diagram		Sphingomonas sp.-46% of the activity with salicylate684569--?
5-chlorosalicylate + NADH + H+ + O25-chlorocatechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekeiQ0VH44-651730--?
5-chlorosalicylate + NADH + H+ + O25-chlorocatechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekei--680483--?
5-chlorosalicylate + NADH + O21,2-dihydroxy-5-chlorobenzene + CO2 + NAD+ + H2O
show the reaction diagram		Trichosporon cutaneum--439423--?
5-chlorosalicylate + NADH + O21,2-dihydroxy-5-chlorobenzene + CO2 + NAD+ + H2O
show the reaction diagram		Sphingobium sp.--657732--?
5-chlorosalicylate + NADH + O21,2-dihydroxy-5-chlorobenzene + NAD+ + H2O + CO2
show the reaction diagram		Pseudomonas sp.--675817--?
5-fluorosalicylate + NADH + O21,2-dihydroxy-5-fluorobenzene + CO2 + NAD+ + H2O
show the reaction diagram		Trichosporon cutaneum--439423--?
5-methoxysalicylate + NADH + O21,2-dihydroxy-5-methoxybenzene + CO2 + NAD+ + H2O
show the reaction diagram		Trichosporon cutaneum--439423--?
5-methylsalicylate + NADH + 2 H+ + O24-methylcatechol + NAD+ + H2O + CO2
show the reaction diagram		Sphingomonas sp.-68.5% of the activity with salicylate684569--?
5-methylsalicylate + NADH + H+ + O25-methylcatechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekei--680483--?
5-methylsalicylate + NADH + O21,2-dihydroxy-5-methylbenzene + CO2 + NAD+ + H2O
show the reaction diagram		Pseudomonas putida--390017--?
5-methylsalicylate + NADH + O21,2-dihydroxy-5-methylbenzene + CO2 + NAD+ + H2O
show the reaction diagram		Trichosporon cutaneum--439423--?
5-methylsalicylate + NADH + O21,2-dihydroxy-5-methylbenzene + CO2 + NAD+ + H2O
show the reaction diagram		Sphingobium sp.--657732--?
5-methylsalicylate + NADH + O21,2-dihydroxy-5-methoxybenzene + NAD+ + H2O + CO2
show the reaction diagram		Pseudomonas sp.--675817--?
5-nitrosalicylate + NADH + 2 H+ + O24-nitrocatechol + NAD+ + H2O + CO2
show the reaction diagram		Sphingomonas sp.-32% of the activity with salicylate684569--?
anthranilate + NADH + 2 H+ + O22-aminophenol + NAD+ + H2O + CO2
show the reaction diagram		Sphingomonas sp.-67% of the activity with salicylate684569--?
aspirin + NADH + O2? + NAD+ + H2O + CO2
show the reaction diagram		Pseudomonas sp.--675817--?
gentisate + NADH + 2 H+ + O2?
show the reaction diagram		Sphingomonas sp.-99% of the activity with salicylate684569--?
o-iodophenol + NADH + O2catechol + iodide + NAD+
show the reaction diagram		Pseudomonas putida--390001, 390002--?
o-nitrophenol + NADH + O2catechol + nitrite + NAD+
show the reaction diagram		Pseudomonas sp.--390000---
o-nitrophenol + NADH + O2catechol + nitrite + NAD+
show the reaction diagram		Pseudomonas putida--390002--?
p-aminosalicylate + NADH + O21,2-dihydroxy-4-aminobenzene + NAD+ + CO2 + H2O
show the reaction diagram		Pseudomonas sp.--390000, 390005--?
p-aminosalicylate + NADH + O21,2-dihydroxy-4-aminobenzene + NAD+ + CO2 + H2O
show the reaction diagram		Pseudomonas putida--389997--?
salicylaldehyde + NADH + O2catechol + formate + NAD+
show the reaction diagram		Pseudomonas putida-mechanism390006--?
salicylate + NADH + 2 H+ + O2catechol + NAD+ + H2O + CO2
show the reaction diagram		Sphingomonas sp.--684569--?
salicylate + NADH + H+ + O2catechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekeiQ0VH44-651730--?
salicylate + NADH + H+ + O2catechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekei--680483--?
salicylate + NADH + O2catechol + NAD+ + H2O + CO2
show the reaction diagram		Nicotiana tabacum--676519--?
salicylate + NADH + O2catechol + NAD+ + H2O + CO2
show the reaction diagram		Pseudomonas sp.--389999, 390000, 390005, 390008, 657599, 671724, 675817--?
salicylate + NADH + O2catechol + NAD+ + H2O + CO2
show the reaction diagram		Pseudomonas putida--389997, 389998, 390001, 390002, 390003, 390004, 390006, 390007, 390009, 390010, 390013, 390014, 390015, 390016, 390017--?
salicylate + NADH + O2catechol + NAD+ + H2O + CO2
show the reaction diagram		Lotus japonicus--676603--?
salicylate + NADH + O2catechol + NAD+ + H2O + CO2
show the reaction diagram		Burkholderia cepacia--390011--?
salicylate + NADH + O2catechol + NAD+ + H2O + CO2
show the reaction diagram		Trichosporon cutaneum--439423--?
salicylate + NADH + O2catechol + NAD+ + H2O + CO2
show the reaction diagram		Medicago truncatula--676603--?
salicylate + NADH + O2catechol + NAD+ + H2O + CO2
show the reaction diagram		Fusarium sp.-bismuth salt of salicylate671441--?
salicylate + NADH + O2catechol + NAD+ + O2
show the reaction diagram		Sphingobium sp.--657732--?
salicylate + O2 + NADH + 2 H+catechol + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas sp.--710856--?
salicylate + O2 + NADH + 2 H+catechol + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas putida--713130--?
salicylate + O2 + NADH + 2 H+catechol + CO2 + H2O + NAD+
show the reaction diagram		Alcaligenes sp.--712039--?
salicylate + O2 + NADPH + 2 H+catechol + CO2 + H2O + NADP+
show the reaction diagram		Pseudomonas sp.--390000---
salicylate + O2 + NADPH + 2 H+catechol + CO2 + H2O + NADP+
show the reaction diagram		Pseudomonas sp.--710856--?
salicylate + O2 + NADPH + 2 H+catechol + CO2 + H2O + NADP+
show the reaction diagram		Alcaligenes sp.--712039--?
sulfosalicylate + NADH + O2? + NAD+ + H2O + CO2
show the reaction diagram		Pseudomonas sp.--675817--?
m-hydroxybenzoate + NADH + O21,3-dihydroxybenzene + CO2 + NAD+ + H2O
show the reaction diagram		Pseudomonas sp.-6% of the reaction with salicylate390000, 390005--?
additional information?-Pseudomonas sp.-mechanism390000---
additional information?-Pseudomonas putida-mechanism389997, 389998, 390001, 390003, 390004---
additional information?-Pseudomonas putida-enzyme catalyzes formation of catechol from substrate analogues such as o-nitro-, o-amino-, o-iodo-, o-bromo- and o-chlorophenol by removing the ortho substituted groups390002---
additional information?-Burkholderia cepacia-apoenzyme-flavin interaction390011---
additional information?-Pseudomonas putida-enzyme catalyses hydroxylation and dehalogenation of o-halogenophenols and also denitrification of o-nitrophenol with unusual stoichiometry390002---
additional information?-Pseudomonas putida-by chemical treatment of the enzyme with dicarbonyl reagents, such as glyoxal, the original oxygenase activity is converted to the salicylate-dependent NADH-dehydrogenase activity with free FAD as electron acceptor390010---
additional information?-Pseudomonas putida-o-fluorophenol is not converted to catechol, though NADH oxidation is observed390002---
additional information?-Emericella nidulansQ9HFQ8terbinafine resistance mediated by salicylate 1-monooxygenase. Terbinafine, which has a naphthalene nucleus in its chemical structure, may be a substrate for a salicylate-like part of an aromatic compound degradation pathway in Aspergillus nidulans657557---
additional information?-Sphingomonas sp.-1-hydroxy-2-naphthoate, which is an intermediate in phenanthrene degradation, is not hydroxylated by PhnII, but it induces a high rate of uncoupled oxidation of NADH684569---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
4-methylsalicylate + NADH + H+ + O24-methylcatechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekei--680483--
salicylate + O2 + NADH + 2 H+catechol + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas sp.--710856--
salicylate + O2 + NADH + 2 H+catechol + CO2 + H2O + NAD+
show the reaction diagram		Pseudomonas putida--713130--
salicylate + O2 + NADH + 2 H+catechol + CO2 + H2O + NAD+
show the reaction diagram		Alcaligenes sp.--712039--
salicylate + O2 + NADPH + 2 H+catechol + CO2 + H2O + NADP+
show the reaction diagram		Pseudomonas sp.--710856--
salicylate + O2 + NADPH + 2 H+catechol + CO2 + H2O + NADP+
show the reaction diagram		Alcaligenes sp.--712039--
5-methylsalicylate + NADH + H+ + O25-methylcatechol + NAD+ H2O
show the reaction diagram		Pseudomonas reinekei--680483--
additional information?-Emericella nidulansQ9HFQ8terbinafine resistance mediated by salicylate 1-monooxygenase. Terbinafine, which has a naphthalene nucleus in its chemical structure, may be a substrate for a salicylate-like part of an aromatic compound degradation pathway in Aspergillus nidulans657557--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
FADPseudomonas putida-flavoprotein389997, 389998, 390009 2D-image
FADPseudomonas sp.-1 mol of FAD loosly bound to 1 mol of enzyme, MW 57000; flavoprotein389999 2D-image
FADPseudomonas sp.-2 FAD per enzyme molecule, 2 subunits, total MW 91000; flavoprotein390000 2D-image
FADPseudomonas sp.-flavoprotein390005 2D-image
FADPseudomonas putida-13C-NMR, 15N-NMR and 31P-NMR investigation of interaction between FAD and the apoprotein; flavoprotein390007 2D-image
FADBurkholderia cepacia-enzyme with dimeric structure binds 1 FAD per monomer; flavoprotein; nature of flavin binding390011 2D-image
FADPseudomonas putida--390017 2D-image
FADTrichosporon cutaneum-flavoprotein439423 2D-image
FADPseudomonas sp.-the FAD-site of the enzyme is involved in the biotransformation of 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane657599 2D-image
FADPseudomonas sp.-0.9 molecules of FAD bound to one molecule of enzyme671724 2D-image
FADPseudomonas sp.--675817 2D-image
FADAlcaligenes sp.--712039 2D-image
NADHPseudomonas putida--389997, 389998, 390001, 390002, 390003, 390004, 390006, 390007, 390009, 390010, 390017 2D-image
NADHPseudomonas sp.--389999, 390000, 390005, 390008, 657599, 671724, 675817, 710856 2D-image
NADHBurkholderia cepacia--390011 2D-image
NADHTrichosporon cutaneum--439423 2D-image
NADHPseudomonas reinekeiQ0VH44-651730, 680483 2D-image
NADHFusarium sp.--671441 2D-image
NADHLotus japonicus, Medicago truncatula--676603 2D-image
NADHAlcaligenes sp.--712039 2D-image
NADPHPseudomonas putida-1% of the activity with NADH389997 2D-image
NADPHPseudomonas sp.--390000, 710856 2D-image
NADPHPseudomonas putida-50% of the activity with NADH390017 2D-image
NADPHTrichosporon cutaneum-60% of the activity with NADH439423 2D-image
NADPHAlcaligenes sp.--712039 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
IronSphingomonas sp.-three-component Fe-S protein complex: the oxygenase component, designated PhnII, exhibits an alpha3beta3 heterohexameric structure and contains one Rieske-type [2Fe-2S] cluster and one mononuclear iron per alpha subunit684569
additional informationTrichosporon cutaneum-no metal ion requirement439423

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1,10-phenanthrolinePseudomonas sp.--389999 2D-image
1-Hydroxy-2-naphthoateSphingomonas sp.-strong competitive inhibition of salicylate hydroxylation684569 2D-image
ascorbic acidPseudomonas sp.-slight389999 2D-image
BenzoatePseudomonas sp.-competitive inhibitor390005 2D-image
Br-Pseudomonas sp.--390005 2D-image
Cl-Pseudomonas sp.--390000, 390005 2D-image
Cl-Trichosporon cutaneum--439423 2D-image
CuSO4Pseudomonas sp.--389999 2D-image
F-Pseudomonas sp.--390000, 390005 2D-image
Na2MoO4Pseudomonas sp.-slight389999 2D-image
NO3-Pseudomonas sp.--390005 2D-image
O2Pseudomonas sp.-inhibits biotransformation of 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane657599 2D-image
p-chloromercuribenzoatePseudomonas sp.--389999, 390005 2D-image
SCN-Pseudomonas sp.--390000, 390005 2D-image
Trinitrobenzenesulfonic acidPseudomonas putida-irreversible inactivation, modification of a lysine residue results in loss of NADH-dehydrogenase activity suggesting its role in the NADH-binding site of the enzyme390013 2D-image
I-Pseudomonas sp.--390000, 390005 2D-image
additional informationPseudomonas putida-chemical modification of one arginine residue with glyoxal causes the enzyme to act as dehydrogenase, but not as oxygenase390010-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
Flavin 1,N6-ethenoadenine dinucleotideBurkholderia cepacia-weaker binding to the apoenzyme than FAD390011 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.004-1-Hydroxy-2-naphthoatePseudomonas putida--390017 2D-image
0.028-2,3-DihydroxybenzoatePseudomonas sp.-cosubstrate NADH390000 2D-image
0.028-2,3-DihydroxybenzoatePseudomonas sp.--390005 2D-image
0.143-2,4-DihydroxybenzoatePseudomonas sp.-cosubstrate NADH390000 2D-image
0.065-2,5-DihydroxybenzoatePseudomonas sp.-cosubstrate NADH390000 2D-image
0.065-2,5-DihydroxybenzoatePseudomonas sp.--390005 2D-image
0.011-2,6-DihydroxybenzoatePseudomonas sp.-cosubstrate NADH390000 2D-image
0.011-2,6-DihydroxybenzoatePseudomonas sp.--390005 2D-image
0.0038-3-chlorosalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
0.0127-3-methylsalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
0.0042-4-(3-benzothiazol-2-yl-4-cyano-2-oxo-2H-chromen-7-yloxymethyl)-2-hydroxy-benzoic acidPseudomonas sp.-pH 8.0, 37°C710856 2D-image
0.0028-4-chlorosalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
0.0158-4-methylsalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
0.0006-5-chlorosalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
0.0024-5-MethylsalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
0.0026-NADHPseudomonas sp.--389999 2D-image
0.0037-NADHPseudomonas putida-native enzyme390013 2D-image
0.0158-NADHPseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
0.0167-NADHPseudomonas sp.--390005 2D-image
0.017-NADHPseudomonas sp.-cosubstrate salicylate390000 2D-image
0.017-NADHPseudomonas sp.--390005 2D-image
0.02326-NADHPseudomonas sp.-enzyme form NahG675817 2D-image
0.044-NADHPseudomonas sp.-cosubstrate p-aminosalicylate390000 2D-image
0.049-NADHPseudomonas putida-modified enzyme390013 2D-image
0.07974-NADHPseudomonas sp.-enzyme form NahU675817 2D-image
0.091-NADHPseudomonas sp.-cosubstrate 2,3-dihydroxybenzoate390000 2D-image
0.118-NADHPseudomonas putida-cosubstrate salicylaldehyde390006 2D-image
0.14-NADHPseudomonas sp.-cosubstrate 2,4-dihydroxybenzoate390000 2D-image
0.23-NADHPseudomonas sp.-cosubstrate 2,5-dihydroxybenzoate or 2,6-dihydroxybenzoate390000 2D-image
0.1-NADPHPseudomonas sp.-cosubstrate salicylate390000 2D-image
0.1-NADPHPseudomonas putida-cosubstrates O2 and salicylate390002 2D-image
0.034-o-NitrophenolPseudomonas sp.-cosubstrate NADH390000 2D-image
0.034-o-NitrophenolPseudomonas putida--390002 2D-image
0.13-O2Pseudomonas putida-cosubstrate o-nitrophenol390002 2D-image
0.196-O2Pseudomonas putida-cosubstrates salicylate and NADH390006 2D-image
0.015-p-AminosalicylatePseudomonas sp.-cosubstrate NADH390000 2D-image
0.015-p-AminosalicylatePseudomonas sp.--390005 2D-image
0.087-SalicylaldehydePseudomonas putida--390006 2D-image
0.0005-salicylatePseudomonas sp.-enzyme form NahG675817 2D-image
0.0011-salicylateSphingomonas sp.-30°C, pH 7.0684569 2D-image
0.0016-salicylatePseudomonas putida-cosubstrate NADH390002 2D-image
0.0016-salicylatePseudomonas putida-native enzyme390013 2D-image
0.0016-salicylatePseudomonas sp.-pH 8.0, 37°C710856 2D-image
0.0018-salicylatePseudomonas putida-modified enzyme390013 2D-image
0.0019-salicylatePseudomonas sp.--389999 2D-image
0.0027-salicylatePseudomonas sp.-cosubstrate NADH390000 2D-image
0.0027-salicylatePseudomonas sp.--390005 2D-image
0.00494-salicylatePseudomonas sp.-enzyme form NahU675817 2D-image
0.0096-salicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
0.028-anthranilateSphingomonas sp.-30°C, pH 7.0684569 2D-image
additional information-additional informationPseudomonas putida--390002, 390004-
additional information-additional informationPseudomonas sp.--390005-
additional information-additional informationPseudomonas putida--390006-
additional information-additional informationPseudomonas putida-FAD, salicylate and NADH, comparison of wild-type, recombinant and mutant enzyme390014-
additional information-additional informationTrichosporon cutaneum--439423-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1.3-3-chlorosalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
2.2-3-methylsalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
0.00075-4-(3-benzothiazol-2-yl-4-cyano-2-oxo-2H-chromen-7-yloxymethyl)-2-hydroxy-benzoic acidPseudomonas sp.-pH 8.0, 37°C710856 2D-image
2.9-4-chlorosalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
6.4-4-methylsalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
1.6-5-chlorosalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
7.8-5-MethylsalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
5.4-NADHPseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image
4.6-salicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
340-3-chlorosalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483282839
170-3-methylsalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483218795
1000-4-chlorosalicylatePseudomonas reinekei-pH not specified in the publication, 25°C6804834446
410-4-methylsalicylatePseudomonas reinekei-pH not specified in the publication, 25°C680483218815
2700-5-chlorosalicylatePseudomonas reinekei-pH not specified in the publication, 25°C6804835177
3300-5-MethylsalicylatePseudomonas reinekei-pH not specified in the publication, 25°C6804835386
340-NADHPseudomonas reinekei-pH not specified in the publication, 25°C68048314331
480-salicylatePseudomonas reinekei-pH not specified in the publication, 25°C68048316463

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.00068-1-Hydroxy-2-naphthoateSphingomonas sp.-30°C, pH 7.0684569 2D-image
3.1-BenzoatePseudomonas sp.--390005 2D-image
60-Cl-Pseudomonas sp.--390000, 390005 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.000256-Pseudomonas sp.-biotransformation of 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane657599
0.0017-Alcaligenes sp.-salicylate-grown cells, pH 7.5, 30°C712039
0.0127-Alcaligenes sp.-phenanthrene-grown cells, pH 7.5, 30°C712039
0.58-Pseudomonas sp.-reaction with salicylate657599
1.27-Pseudomonas sp.-enzyme form NahG, using 3,5-dinitrosalicylate as substrate, at 20°C675817
1.53-Pseudomonas sp.-enzyme form NahU, using sulfosalicylate as substrate, at 20°C675817
3.17-Pseudomonas sp.-enzyme form NahG, using salicylate as substrate, at 20°C675817
3.63-Pseudomonas sp.-enzyme form NahG, using 5-chlorosalicylate as substrate, at 20°C675817
3.91-Pseudomonas sp.-enzyme form NahG, using 5-methylsalicylate as substrate, at 20°C675817
4.04-Pseudomonas sp.-enzyme form NahG, using 3-methylsalicylate as substrate, at 20°C675817
4.12-Pseudomonas sp.-enzyme form NahG, using aspirin as substrate, at 20°C675817
4.24-Pseudomonas sp.-enzyme form NahG, using sulfosalicylate as substrate, at 20°C675817
5-Pseudomonas putida--390017
5.25-Pseudomonas sp.-enzyme form NahU, using 5-chlorosalicylate as substrate, at 20°C675817
10.57-Pseudomonas sp.--390000, 390005
10.59-Pseudomonas sp.-enzyme form NahU, using 3-methylsalicylate as substrate, at 20°C675817
13.5-Pseudomonas sp.--389999
18.79-Pseudomonas sp.-enzyme form NahU, using 5-methylsalicylate as substrate, at 20°C675817
23.44-Pseudomonas sp.-enzyme form NahU, using salicylate as substrate, at 20°C675817
25.64-Pseudomonas sp.-enzyme form NahU, using aspirin as substrate, at 20°C675817
37-Trichosporon cutaneum--439423
85-Pseudomonas reinekei-purified enzyme from 4-methylsalicylate-grown cells, pH not specified in the publication, 25°C, substrate salicylate680483
90-Pseudomonas reinekei-purified enzyme from 5-methylsalicylate-grown cells, pH not specified in the publication, 25°C, substrate salicylate680483
120-Pseudomonas reinekei-purified enzyme from 5-chlorosalicylate-grown cells, pH not specified in the publication, 25°C, substrate 3-chlorosalicylate; purified enzyme from salicylate-grown cells, pH not specified in the publication, 25°C, substrate salicylate651730
120-Pseudomonas reinekei-purified enzyme from salicylate-grown cells, pH not specified in the publication, 25°C, substrate salicylate680483
190-Pseudomonas reinekei-purified enzyme from 5-chlorosalicylate-grown cells, pH not specified in the publication, 25°C, substrate 5-chlorosalicylate651730
240-Pseudomonas reinekei-purified enzyme from 5-chlorosalicylate-grown cells, pH not specified in the publication, 25°C, substrate 4-chlorosalicylate651730
460-Pseudomonas reinekei-purified enzyme from 5-chlorosalicylate-grown cells, pH not specified in the publication, 25°C, substrate salicylate651730
additional information-Pseudomonas putida--389998
additional information-Pseudomonas sp.--390008
additional information-Pseudomonas putida--390009
additional information-Pseudomonas sp.-no activity of enzyme form NahU when using 3,5-dinitrosalicylate as substrate675817

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
77.5Pseudomonas putida--390017
78.5Pseudomonas sp.--390005
7.58Pseudomonas sp.--389999
7.5-Trichosporon cutaneum--439423
7.5-Alcaligenes sp.-assay at712039
7.8-Pseudomonas putida-substrate salicylaldehyde390006
8-Pseudomonas putida-substrate o-iodophenol390002
8-Pseudomonas sp.-assay at710856

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
610Pseudomonas sp.-about 50% of activity maximum at pH 6 and 10389999
68Pseudomonas putida-65% of maximal activity at pH 6, 96% of maximal activity at pH 8390017
6.58.5Trichosporon cutaneum-about 75% of activity maximum at pH 6.5 and 8.5439423

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
20-Pseudomonas sp.-assay at389999
2527Pseudomonas sp.-assay at390000
25-Pseudomonas reinekei-assay at651730, 680483
30-Pseudomonas putida--390017
30-Alcaligenes sp.-assay at712039
37-Pseudomonas sp.-assay at710856

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
2050Pseudomonas putida-62% of maximal activity at 20°C, 70% of maximal activity at 50°C, no activity at 55°C390017

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
commercial preparationPseudomonas sp.--710856Manually annotated by BRENDA team
culture condition:4-methylsalicylate-grown cellPseudomonas reinekei--680483Manually annotated by BRENDA team
culture condition:5-chlorosalicylate-grown cellPseudomonas reinekeiQ0VH44-651730, 680483Manually annotated by BRENDA team
culture condition:5-methylsalicylate-grown cellPseudomonas reinekei--680483Manually annotated by BRENDA team
culture condition:phenanthrene-grown cellAlcaligenes sp.--712039Manually annotated by BRENDA team
culture condition:salicylate-grown cellPseudomonas reinekeiQ0VH44-651730, 680483Manually annotated by BRENDA team
culture condition:salicylate-grown cellAlcaligenes sp.--712039Manually annotated by BRENDA team
leafNicotiana tabacum--676519Manually annotated by BRENDA team
rootLotus japonicus, Medicago truncatula--676603Manually annotated by BRENDA team
leafLotus japonicus, Medicago truncatula--676603Manually annotated by BRENDA team
additional informationPseudomonas reinekei-very low activity in succinate-grown cells651730Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
4300048700Pseudomonas sp.-gel filtration, sedimentation equilibrium, calculation of MW per flavin390000, 390005
43000-Pseudomonas putida-SDS-PAGE390016
4340045300Trichosporon cutaneum-gel filtration, SDS-PAGE439423
45000-Pseudomonas putida-SDS-PAGE,gel filtration390009
45000-Pseudomonas putida-recombinant native and mutant protein, expressed in E. coli, SDS-PAGE390014
45000-Pseudomonas putida-SDS-PAGE390017
47000-Pseudomonas sp.-SDS-PAGE675817
57000-Pseudomonas sp.-SDS-PAGE671724
57200-Pseudomonas sp.-calculation from diffusion and sedimentation data389999

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Pseudomonas reinekei-x * 50712, sequence calculation, x * 48000, SalD, SDS-PAGE680483
dimerPseudomonas sp.-2 * 43000-48700, sedimentation equilibrium390000, 390005
monomerPseudomonas putida-1 * 52000, SDS-PAGE under dissociating conditions390003
monomerPseudomonas putida-1 * 45000, SDS-PAGE390009
monomerTrichosporon cutaneum-1 * 45300 SDS-PAGE439423
additional informationSphingomonas sp.-three-component Fe-S protein complex: the oxygenase component, designated PhnII, exhibits an alpha3beta3 heterohexameric structure and contains one Rieske-type [2Fe-2S] cluster and one mononuclear iron per alpha subunit. In the presence of purified reductase (PhnA4) and ferredoxin (PhnA3) components, PhnII catalyzes the hydroxylation of salicylate to catechol684569

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Pseudomonas putida-389998
apoenzyme is crystallized by dialysis method, using ammonium sulfate as the precipitantPseudomonas putida-390014

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
8-Pseudomonas sp.-highest stability389999

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
25-Pseudomonas sp.-apoenzyme unstable above389999
38-Pseudomonas sp.-2 h, 10% loss of activity in the presence of FAD; 30 min, complete inactivation in absence of FAD389999
60-Alcaligenes sp.-5 min, cell-free extract, in presence of 1-hydroxy-2-naphthoic acid, inactivation712039

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
glycerol, 10%, stabilizesPseudomonas putida-390009
loses its activity after ammonium sulfate fractionation and dialysis, and its full activity is restored by the addition of a heat-stable factor of rat liverPseudomonas sp.-671724
dithiothreitol, 0.5 mM, stabilizesTrichosporon cutaneum-439423

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-20°C, 20 mM KH2PO4 buffer pH 7.5Pseudomonas putida-390017
-20°C, stable for a few weeksPseudomonas putida-389998
4°C, 0.5 mM dithiothreitol, 10% loss of activity after 1 weekTrichosporon cutaneum-439423

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Pseudomonas putida-389998, 390009
cells grown on 1-hydroxy-2-naphthoatePseudomonas putida-390017
native enzyme from 5-chlorosalicylate-grown cells by anion exchange chromatography and gel filtrationPseudomonas reinekei-680483
-Pseudomonas sp.-389999, 390000, 390005
affinity chromatographyPseudomonas sp.-390008
Ni-NTA His Bind resin column chromatographyPseudomonas sp.-675817
oxygenase component PhnIISphingomonas sp.-684569
-Trichosporon cutaneum-439423

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression in Escherichia coliPseudomonas putida-390014
transgenic Populus tremula x Populus alba hybrid expressing the nahG transgene. Expression of nahG decreases quinic acid conjugates and increased catechol glucoside, while exerting little effect on levels of salicylic acid and catechol, the substrate and product, respectively, of the nahG enzymePseudomonas putida-689421
gene salA, DNA and amino acid sequence determination and analysis, phylogenetic analysisPseudomonas reinekei-680483
expressed in Escherichia coli strain BL21(DE3)Pseudomonas sp.-675817
biotransformation experiments with resting cells of Escherichia coli JM109 harboring recombinant ahd genes reveal that AhdA2cA1c, AhdA1dA2d, and AhdA1eA2e can function as a salicylate 1-hydroxylaseSphingobium sp.-657732

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
in mixed Pseudomonas reinekei MT1 with Achromobacter xylosoxidans MT3 cultures, analyzed by 2-D electrophoresisPseudomonas reinekei-701143
5-chlorosalicylate induces the enzymePseudomonas reinekei-680483

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
K163EPseudomonas putida-site directed mutagenesis, Lys163 is involved in the NADH-binding site390014
K163GPseudomonas putida-site directed mutagenesis, Lys163 is involved in the NADH-binding site390014
K163RPseudomonas putida-site directed mutagenesis, Lys163 is involved in the NADH-binding site390014
additional informationPseudomonas putida-construction of transgenic plants, using wild-type Columbia(0) plants and sid2 mutant plants, overexpressing the bacterial NahG, germination of NahG transgenic plants is influenced to a lesser degree by high salinity. Catechol accumulates in the transgenic plants and acts as an antioxidant that compromises the inhibitory effects of high salinity. Salicylic acid promotes seed germination under high salinity by modulating antioxidant activity in transgenic Arabidopsis thaliana, detailed overview713130

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
analysisPseudomonas putida-biosensor system for determining salicylate in body fluids390016
analysisPseudomonas sp.-an amperometric biosensor is developed for the interference-free determination of L-glutamate with a bienzyme-based Clark electrode. This sensor is based on the specific dehydrogenation by L-glutamate dehydrogenase (EC 1.4.1.3) in combination with salicylate hydroxylase (EC 1.14.13.1). The enzymes are entrapped by a poly(carbamoyl) sulfonate (PCS) hydrogel on a Teflon membrane686457
analysisPseudomonas sp.-two types of amperometric ATP biosensors are developed by using the coimmobilization of salicylate hydroxylase (SHL, EC 1.14.13.1), glucose-6-phosphate dehydrogenase (G6PDH, EC 1.1.1.49), and hexokinase (HEX, EC 2.7.1.1) on a Clark-type oxygen electrode and on a screenprinted electrode. The principles of the determination schemes are as follows: HEX transfers the phosphate group from ATP to glucose to form glucose-6-phosphate. G6PDH catalyzes the specific dehydrogenation of glucose-6-phosphate by consuming NAD+. The product, NADH initiates the irreversible decarboxylation and hydroxylation of salicylate by SHL to consume dissolved oxygen and generate catechol. This results in a detectable signal on a Clark-type electrode due to the SHL-enzymatic consumption of oxygen, or a detectable signal on a screen-printed electrode due to the SHL-enzymatic generation of catechol in the measurement of ATP. Both sensors show high performance characteristics with broad detection ranges, short measuring times, and good specificities690072
analysisPseudomonas sp.-usage of the enzyme in a fluorescence assay that detects 3-hydroxybutyrate and cholesterol in the nanomolar range and is more sensitive than the current SHL-dehydrogenase amperometric sensors, making it applicable to the construction of a fiber-optic fluorescence biosensor for clinical diagnostic uses710856
diagnosticsPseudomonas sp.-usage of the enzyme in a fluorescence assay that detects 3-hydroxybutyrate and cholesterol in the nanomolar range and is more sensitive than the current SHL-dehydrogenase amperometric sensors, making it applicable to the construction of a fiber-optic fluorescence biosensor for clinical diagnostic uses710856

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
389997Suzuki, K.; Takemori, S.; Katagiri, M.Mechanism of the salicylate hydroxylase reaction. IV. Fluorometric analysis of the complex formationBiochim. Biophys. Acta19177-851969Pseudomonas putida PubMed
389998Takemori, S.; Yasuda, H.; Mihara, K.; Suzuki, K.; Katagiri, M.Mechanism of the salicylate hydroxylase reaction. II. The enzyme-substrate complexBiochim. Biophys. Acta19158-681969Pseudomonas putida PubMed
389999Yamamoto, S.; Katagiri, M.; Maeno, H.; Hayaishi, O.Salicylate hydroxylase, a monooxygenase requiring flavin adenine dinucleotideJ. Biol. Chem.2403408-34131965Pseudomonas sp. PubMed
390000Kamin, H.; White-Stevens, R.H.; Presswood, R.P.Salicylate hydroxylaseMethods Enzymol.53527-5431978Pseudomonas sp. PubMed
390001Suzuki, K.; Gomi, T.; Itagaki, E.Intermediate and mechanism of hydroxylation of o-iodophenol by salicylate hydroxylaseJ. Biochem.109791-7971991Pseudomonas putida PubMed
390002Suzuki, K.; Gomi, T.; Kaidoh, T.; Itagaki, E.Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylaseJ. Biochem.109348-3531991Pseudomonas putida PubMed
390003Takemori, S.; Hon-Nami, K.; Kawahara, F.; Katagiri, M.Mechanism of the salicylate 1-monooxygenase reaction. VI. The monomeric nature of the enzymeBiochim. Biophys. Acta342137-1441974Pseudomonas putida PubMed
390004Takemori, S.; Nakamura, M.; Suzuki, K.; Katagiri, M.; Nakamura, T.Mechanism of the salicylate hydroxylase reaction. V. Kinetic analysesBiochim. Biophys. Acta284382-3931972Pseudomonas putida PubMed
390005White-Stevens, R.H.; Kamin, H.Studies of a flavoprotein, salicylate hydroxylase. I. Preparation, properties, and the uncoupling of oxygen reduction from hydroxylationJ. Biol. Chem.2472358-23701972Pseudomonas sp. PubMed
390006Suzuki, K.; Katagiri, M.Mechanism of salicylate hydroxylase-catalyzed decarboxylationBiochim. Biophys. Acta657530-5341981Pseudomonas putida PubMed
390007Vervoort, J.; Van Berkel, W.J.H.; Muller, F.; Moonen, C.T.W.NMR studies on p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens and salicylate hydroxylase from Pseudomonas putidaEur. J. Biochem.200731-7381991Pseudomonas putida PubMed
390008You, K.S.; Roe, C.R.Affinity chromatography of Pseudomonas salicylate hydroxylaseAnal. Biochem.114177-1851981Pseudomonas sp. PubMed
390009You, I.S.; Murray, R.I.; Jollie, D.; Gunsalus, I.C.Purification and characterization of salicylate hydroxylase from Pseudomonas putida PpG7Biochem. Biophys. Res. Commun.1691049-10541990Pseudomonas putida PubMed
390010Suzuki, K.; Ohnishi, K.Functional modification of an arginine residue on salicylate hydroxylaseBiochim. Biophys. Acta1040327-3361990Pseudomonas putida PubMed
390011Wang, L.H.; Tu, S.C.; Lusk, R.C.Apoenzyme of Pseudomonas cepacia salicylate hydroxylase. Preparation, fluorescence property, and nature of flavin bindingJ. Biol. Chem.2591136-11421984Burkholderia cepacia PubMed
390013Suzuki, K.; Mizuguchi, M.; Gomi, T.; Itagaki, E.Identification of a lysine residue in the NADH-binding site of salicylate hydroxylase from Pseudomonas putida S-1J. Biochem.117579-5851995Pseudomonas putida PubMed
390014Suzuki, K.; Asao, E.; Nakamura, Y.; Nakamura, M.; Ohnishi, K.; Fukuda, S.Overexpression of salicylate hydroxylase and the crucial role of Lys163 as its NADH binding siteJ. Biochem.128293-2992000Pseudomonas putida PubMed
390015Yabuuchi, T.; Suzuki, K.; Sato, T.; Ohnishi, K.; Itagaki, E.; Morimoto, Y.Crystallization and preliminary X-ray analysis of salicylate hydroxylase from Pseudomonas putida S-1J. Biochem.119829-8311996Pseudomonas putida PubMed
390016Banat, I.M.; Marchant, A.; Nigam, P.; Gaston, S.J.S.; Kelly, B.A.; Marchant, R.Production, partial characterization, and potential diagnostic use of salicylate hydroxylase from Pseudomonas putida UUC-1Enzyme Microb. Technol.16665-6701994Pseudomonas putida PubMed
390017Balashova, N.V.; Stolz, A.; Knackmuss, H.J.; Kosheleva, I.A.; Naumov, A.V.; Boronin, A.M.Purification and characterization of a salicylate hydroxylase involved in 1-hydroxy-2-naphthoic acid hydroxylation from the naphthalene and phenanthrene-degrading bacterial strain Pseudomonas putida BS202-P1Biodegradation12179-1882001Pseudomonas putida PubMed
439423Sze, I.S.Y.; Dagley, S.Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneumJ. Bacteriol.159353-3591984Trichosporon cutaneum PubMed
651730Nikodem, P.; Hecht, V.; Schlomann, M.; Pieper, D.H.New bacterial pathway for 4- and 5-chlorosalicylate degradation via 4-chlorocatechol and maleylacetate in Pseudomonas sp. strain MT1J. Bacteriol.1856790-68002003Pseudomonas reinekei PubMed
657557Graminha, M.A.; Rocha, E.M.; Prade, R.A.; Martinez-Rossi, N.M.Terbinafine resistance mediated by salicylate 1-monooxygenase in Aspergillus nidulansAntimicrob. Agents Chemother.483530-35352004Emericella nidulans PubMed
657599Bhushan, B.; Halasz, A.; Spain, J.C.; Hawari, J.Initial reaction(s) in biotransformation of CL-20 is catalyzed by salicylate 1-monooxygenase from Pseudomonas sp. strain ATCC 29352Appl. Environ. Microbiol.704040-40472004Pseudomonas sp. PubMed
657732Pinyakong, O.; Habe, H.; Yoshida, T.; Nojiri, H.; Omori, T.Identification of three novel salicylate 1-hydroxylases involved in the phenanthrene degradation of Sphingobium sp. strain P2Biochem. Biophys. Res. Commun.301350-3572003Sphingobium sp. PubMed
671441Dodge, A.G.; Wackett, L.P.Metabolism of bismuth subsalicylate and intracellular accumulation of bismuth by Fusarium sp. strain BIAppl. Environ. Microbiol.71876-8822005Fusarium sp. PubMed
671724Katagiri, M.Early years of oxygenase research in Bethesda, Osaka, Urbana, and KanazawaBiochem. Biophys. Res. Commun.338285-2892005Pseudomonas sp. PubMed
675817Zhao, H.; Chen, D.; Li, Y.; Cai, B.Overexpression, purification and characterization of a new salicylate hydroxylase from naphthalene-degrading Pseudomonas sp. strain ND6Microbiol. Res.160307-3132005Pseudomonas sp. PubMed
676519Alamillo, J.M.; Saenz, P.; Garcia, J.A.Salicylic acid-mediated and RNA-silencing defense mechanisms cooperate in the restriction of systemic spread of plum pox virus in tobaccoPlant J.48217-2272006Nicotiana tabacum PubMed
676603Stacey, G.; McAlvin, C.B.; Kim, S.Y.; Olivares, J.; Soto, M.J.Effects of endogenous salicylic acid on nodulation in the model legumes Lotus japonicus and Medicago truncatulaPlant Physiol.1411473-14812006Lotus japonicus, Medicago truncatula PubMed
680483Camara, B.; Bielecki, P.; Kaminski, F.; dos Santos, V.M.; Plumeier, I.; Nikodem, P.; Pieper, D.H.A gene cluster involved in degradation of substituted salicylates via ortho cleavage in Pseudomonas sp. strain MT1 encodes enzymes specifically adapted for transformation of 4-methylcatechol and 3-methylmuconateJ. Bacteriol.1891664-16742007Pseudomonas reinekei PubMed
684569Jouanneau, Y.; Micoud, J.; Meyer, C.Purification and characterization of a three-component salicylate 1-hydroxylase from Sphingomonas sp. strain CHY-1Appl. Environ. Microbiol.737515-75212007Sphingomonas sp. PubMed
686457Cui, Y.; Barford, J.P.; Renneberg, R.Development of an interference-free biosensor for L-glutamate using a bienzyme salicylate hydroxylase/L-glutamate dehydrogenase systemEnzyme Microb. Technol.41689-6932007Pseudomonas sp.-
689421Morse, A.M.; Tschaplinski, T.J.; Dervinis, C.; Pijut, P.M.; Schmelz, E.A.; Day, W.; Davis, J.M.Salicylate and catechol levels are maintained in nahG transgenic poplarPhytochemistry682043-20522007Pseudomonas putida PubMed
690072Cui, Y.; Barford, J.P.; Renneberg, R.Amperometric trienzyme ATP biosensors based on the coimmobilization of salicylate hydroxylase, glucose-6-phosphate dehydrogenase, and hexokinaseSens. Actuators B Chem.B1321-42008Pseudomonas sp.-
698002Lanfranconi, M.; Christie-Oleza, J.; Martin-Cardona, C.; Suarez-Suarez, L.; Lalucat, J.; Nogales, B.; Bosch, R.Physiological role of NahW, the additional salicylate hydroxylase found in Pseudomonas stutzeri AN10FEMS Microbiol. Lett.300265-2722009Pseudomonas stutzeri-
700067Akhmetov, L.; Filonov, A.; Puntus, I.; Kosheleva, I.; Nechaeva, I.; Yonge, D.; Petersen, J.; Boronin, A.Horizontal transfer of catabolic plasmids in the process of naphthalene biodegradation in model soil systemsMicrobiology7723-322008Pseudomonas fluorescens, Pseudomonas putida-
700069Sazonova, O.; Izmalkova, T.; Kosheleva, I.; Boronin, A.Salicylate degradation by Pseudomonas putida strains not involving the 'classical' nah2 operonMicrobiology77710-7162008Pseudomonas putida-
701143Bobadilla Fazzini, R.A.; Bielecka, A.; Quintas, A.K.; Golyshin, P.N.; Preto, M.J.; Timmis, K.N.; dos Santos, V.A.Bacterial consortium proteomics under 4-chlorosalicylate carbon-limiting conditionsProteomics92273-22852009Pseudomonas reinekei PubMed
710856Huang, S.T.; Teng, C.J.; Lee, Y.H.; Wu, J.Y.; Wang, K.L.; Lin, C.M.Design and synthesis of a long-wavelength latent fluorogenic substrate for salicylate hydroxylase: a useful fluorimetric indicator for analyte determination by dehydrogenase-coupled biosensorsAnal. Chem.827329-73342010Pseudomonas sp. PubMed
712039Deveryshetty, J.; Phale, P.S.Biodegradation of phenanthrene by Alcaligenes sp. strain PPH: partial purification and characterization of 1-hydroxy-2-naphthoic acid hydroxylaseFEMS Microbiol. Lett.31193-1012010Alcaligenes sp. PubMed
713130Lee, S.; Kim, S.G.; Park, C.M.Salicylic acid promotes seed germination under high salinity by modulating antioxidant activity in ArabidopsisNew Phytol.188626-6372010Pseudomonas putida PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.1)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)