PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
3584076-2	1987	A strain of P. putida (NAH:Tn5/G67) defective in salicylate hydroxylase (nahG) was assessed for its ability to oxidize 1,4-dichloronaphthalene.	1,4-DICHLORONAPHTHALENE	119-142	salicylate hydroxylase	Pseudomonas putida	49-71
30703421-0	2019	Catalytic mechanism for the conversion of salicylate into catechol by the flavin-dependent monooxygenase salicylate hydroxylase.	Salicylates	42-52	salicylate hydroxylase	Pseudomonas putida	105-127
7213760-1	1981	Salicylate hydroxylase (salicylate, NADH: oxygen oxidoreductase (1-hydroxylating, decarboxylating), EC 1.14.13.1) in Pseudomonas putida catalyzed hydroxylation of the substrate analogue, salicylaldehyde, to form catechol and formate with stoichiometric consumption of NADH and O2.	salicylaldehyde	187-202	salicylate hydroxylase	Pseudomonas putida	0-22
7213760-1	1981	Salicylate hydroxylase (salicylate, NADH: oxygen oxidoreductase (1-hydroxylating, decarboxylating), EC 1.14.13.1) in Pseudomonas putida catalyzed hydroxylation of the substrate analogue, salicylaldehyde, to form catechol and formate with stoichiometric consumption of NADH and O2.	catechol	212-220	salicylate hydroxylase	Pseudomonas putida	0-22
7213760-1	1981	Salicylate hydroxylase (salicylate, NADH: oxygen oxidoreductase (1-hydroxylating, decarboxylating), EC 1.14.13.1) in Pseudomonas putida catalyzed hydroxylation of the substrate analogue, salicylaldehyde, to form catechol and formate with stoichiometric consumption of NADH and O2.	formic acid	225-232	salicylate hydroxylase	Pseudomonas putida	0-22
7213760-1	1981	Salicylate hydroxylase (salicylate, NADH: oxygen oxidoreductase (1-hydroxylating, decarboxylating), EC 1.14.13.1) in Pseudomonas putida catalyzed hydroxylation of the substrate analogue, salicylaldehyde, to form catechol and formate with stoichiometric consumption of NADH and O2.	NAD	36-40	salicylate hydroxylase	Pseudomonas putida	0-22
7213760-1	1981	Salicylate hydroxylase (salicylate, NADH: oxygen oxidoreductase (1-hydroxylating, decarboxylating), EC 1.14.13.1) in Pseudomonas putida catalyzed hydroxylation of the substrate analogue, salicylaldehyde, to form catechol and formate with stoichiometric consumption of NADH and O2.	Oxygen	277-279	salicylate hydroxylase	Pseudomonas putida	0-22
32582120-7	2020	Previously, this strain was shown to contain genes encoding the key enzymes for naphthalene catabolism: naphthalene 1,2-dioxygenase, salicylate hydroxylase, catechol 2,3-dioxygenase, and catechol 1,2-dioxygenase.	naphthalene	80-91	salicylate hydroxylase	Pseudomonas putida	133-155
30703421-0	2019	Catalytic mechanism for the conversion of salicylate into catechol by the flavin-dependent monooxygenase salicylate hydroxylase.	catechol	58-66	salicylate hydroxylase	Pseudomonas putida	105-127
30703421-1	2019	Salicylate hydroxylase (NahG) is a flavin-dependent monooxygenase that catalyzes the decarboxylative hydroxylation of salicylate into catechol in the naphthalene degradation pathway in Pseudomonas putida G7.	Salicylates	118-128	salicylate hydroxylase	Pseudomonas putida	0-22
30703421-1	2019	Salicylate hydroxylase (NahG) is a flavin-dependent monooxygenase that catalyzes the decarboxylative hydroxylation of salicylate into catechol in the naphthalene degradation pathway in Pseudomonas putida G7.	catechol	134-142	salicylate hydroxylase	Pseudomonas putida	0-22
30703421-1	2019	Salicylate hydroxylase (NahG) is a flavin-dependent monooxygenase that catalyzes the decarboxylative hydroxylation of salicylate into catechol in the naphthalene degradation pathway in Pseudomonas putida G7.	naphthalene	150-161	salicylate hydroxylase	Pseudomonas putida	0-22
1917904-1	1991	Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzes the hydroxylation of salicylate, and also o-aminophenol, o-nitrophenol, and o-halogenophenols, to catechol.	2-nitrophenol	129-142	salicylate hydroxylase	Pseudomonas putida	0-22
10920265-0	2000	Overexpression of salicylate hydroxylase and the crucial role of lys(163) as its NADH binding site.	NAD	81-85	salicylate hydroxylase	Pseudomonas putida	18-40
10920265-2	2000	By cultivation of Escherichia coli BL21 (DE3)/pSAH8 in LB medium at 37 degrees C with isopropyl-b-D-thiogalactopyranoside as the inducer, salicylate hydroxylase was overexpressed mainly in the form of inclusion bodies.	lb medium	55-64	salicylate hydroxylase	Pseudomonas putida	138-160
10920265-2	2000	By cultivation of Escherichia coli BL21 (DE3)/pSAH8 in LB medium at 37 degrees C with isopropyl-b-D-thiogalactopyranoside as the inducer, salicylate hydroxylase was overexpressed mainly in the form of inclusion bodies.	isopropyl-b-d-thiogalactopyranoside	86-121	salicylate hydroxylase	Pseudomonas putida	138-160
10920265-6	2000	Based on chemical modification of the salicylate hydroxylase from P. putida, Lys163 was previously proposed to be the NADH binding site.	NAD	118-122	salicylate hydroxylase	Pseudomonas putida	38-60
8561793-1	1996	The salicylate hydroxylase, a flavoprotein monooxygenase, catalyzes the decarboxylative hydroxylation of salicylate to form catechol.	catechol	124-132	salicylate hydroxylase	Pseudomonas putida	4-26
7794247-1	1995	The salicylate hydroxylase can convert the salicylate to catechol, and catechol 2,3-dioxygenase catalizes the conversion of catechol to 2-hydroxymuconic semialdehyde.	catechol	57-65	salicylate hydroxylase	Pseudomonas putida	4-26
7794247-1	1995	The salicylate hydroxylase can convert the salicylate to catechol, and catechol 2,3-dioxygenase catalizes the conversion of catechol to 2-hydroxymuconic semialdehyde.	catechol	71-79	salicylate hydroxylase	Pseudomonas putida	4-26
1917904-1	1991	Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzes the hydroxylation of salicylate, and also o-aminophenol, o-nitrophenol, and o-halogenophenols, to catechol.	o-halogenophenols	148-165	salicylate hydroxylase	Pseudomonas putida	0-22
1917904-1	1991	Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzes the hydroxylation of salicylate, and also o-aminophenol, o-nitrophenol, and o-halogenophenols, to catechol.	catechol	170-178	salicylate hydroxylase	Pseudomonas putida	0-22
1993181-1	1991	Gene nahG of naphthalene/salicylate catabolic plasmid NAH7 encodes a protein of molecular weight 45,000, salicylate hydroxylase.	naphthalene	13-24	salicylate hydroxylase	Pseudomonas putida	5-9
1993181-1	1991	Gene nahG of naphthalene/salicylate catabolic plasmid NAH7 encodes a protein of molecular weight 45,000, salicylate hydroxylase.	naphthalene	13-24	salicylate hydroxylase	Pseudomonas putida	105-127
1993181-1	1991	Gene nahG of naphthalene/salicylate catabolic plasmid NAH7 encodes a protein of molecular weight 45,000, salicylate hydroxylase.	Salicylates	25-35	salicylate hydroxylase	Pseudomonas putida	5-9
1993181-1	1991	Gene nahG of naphthalene/salicylate catabolic plasmid NAH7 encodes a protein of molecular weight 45,000, salicylate hydroxylase.	Salicylates	25-35	salicylate hydroxylase	Pseudomonas putida	105-127
1993181-9	1991	The amino acid sequence between positions 8 and 37 of salicylate hydroxylase shows homology with known ADP binding sites of other FAD-containing oxidoreductases, thus confirming its biochemical function.	Adenosine Diphosphate	103-106	salicylate hydroxylase	Pseudomonas putida	54-76
1993181-11	1991	A small DNA segment (831 base pairs) disrupts the continuity of the known gene order nahG and nahH, the latter encoding catechol 2,3-dioxygenase.	nahh	94-98	salicylate hydroxylase	Pseudomonas putida	85-89
1993181-11	1991	A small DNA segment (831 base pairs) disrupts the continuity of the known gene order nahG and nahH, the latter encoding catechol 2,3-dioxygenase.	catechol	120-128	salicylate hydroxylase	Pseudomonas putida	85-89
1864847-0	1991	Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase.	o-halogenophenol	17-33	salicylate hydroxylase	Pseudomonas putida	55-77
1864847-0	1991	Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase.	2-nitrophenol	38-51	salicylate hydroxylase	Pseudomonas putida	55-77
1864847-1	1991	Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzed the formation of catechol from substrate analogues such as o-nitro-, o-amino-, o-iodo-, o-bromo-, and o-chloro-phenol by removing the ortho-substituted groups.	catechol	89-97	salicylate hydroxylase	Pseudomonas putida	0-22
1864847-1	1991	Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzed the formation of catechol from substrate analogues such as o-nitro-, o-amino-, o-iodo-, o-bromo-, and o-chloro-phenol by removing the ortho-substituted groups.	o-nitro-	131-139	salicylate hydroxylase	Pseudomonas putida	0-22
1864847-1	1991	Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzed the formation of catechol from substrate analogues such as o-nitro-, o-amino-, o-iodo-, o-bromo-, and o-chloro-phenol by removing the ortho-substituted groups.	o-amino-, o-iodo-, o-bromo-, and o-chloro-phenol	141-189	salicylate hydroxylase	Pseudomonas putida	0-22
1864847-6	1991	Like salicylate, these substrates perturb the absorption spectrum of salicylate hydroxylase in the visible region, indicating the formation of enzyme.substrate complexes.	Salicylates	5-15	salicylate hydroxylase	Pseudomonas putida	69-91
1864847-10	1991	It is concluded that salicylate hydroxylase cleaves the C-N and C-X bonds of ortho-substituted phenols.	Phenols	95-102	salicylate hydroxylase	Pseudomonas putida	21-43
2223838-0	1990	Functional modification of an arginine residue on salicylate hydroxylase.	Arginine	30-38	salicylate hydroxylase	Pseudomonas putida	50-72
2223838-1	1990	Salicylate hydroxylase from Pseudomonas putida (EC 1.14.13.1, salicylate, NADH:oxygen oxidoreductase) is an FAD-containing monooxygenase, which catalyzes decarboxylative hydroxylation of salicylate to produce catechol in the presence of NADH and O2.	Salicylates	62-72	salicylate hydroxylase	Pseudomonas putida	0-22
2223838-1	1990	Salicylate hydroxylase from Pseudomonas putida (EC 1.14.13.1, salicylate, NADH:oxygen oxidoreductase) is an FAD-containing monooxygenase, which catalyzes decarboxylative hydroxylation of salicylate to produce catechol in the presence of NADH and O2.	Salicylates	187-197	salicylate hydroxylase	Pseudomonas putida	0-22
2223838-1	1990	Salicylate hydroxylase from Pseudomonas putida (EC 1.14.13.1, salicylate, NADH:oxygen oxidoreductase) is an FAD-containing monooxygenase, which catalyzes decarboxylative hydroxylation of salicylate to produce catechol in the presence of NADH and O2.	catechol	209-217	salicylate hydroxylase	Pseudomonas putida	0-22
2223838-1	1990	Salicylate hydroxylase from Pseudomonas putida (EC 1.14.13.1, salicylate, NADH:oxygen oxidoreductase) is an FAD-containing monooxygenase, which catalyzes decarboxylative hydroxylation of salicylate to produce catechol in the presence of NADH and O2.	NAD	74-78	salicylate hydroxylase	Pseudomonas putida	0-22
2223838-1	1990	Salicylate hydroxylase from Pseudomonas putida (EC 1.14.13.1, salicylate, NADH:oxygen oxidoreductase) is an FAD-containing monooxygenase, which catalyzes decarboxylative hydroxylation of salicylate to produce catechol in the presence of NADH and O2.	Oxygen	246-248	salicylate hydroxylase	Pseudomonas putida	0-22
1917904-0	1991	Intermediate and mechanism of hydroxylation of o-iodophenol by salicylate hydroxylase.	2-iodophenol	47-59	salicylate hydroxylase	Pseudomonas putida	63-85
1917904-1	1991	Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzes the hydroxylation of salicylate, and also o-aminophenol, o-nitrophenol, and o-halogenophenols, to catechol.	Salicylates	93-103	salicylate hydroxylase	Pseudomonas putida	0-22
1917904-1	1991	Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzes the hydroxylation of salicylate, and also o-aminophenol, o-nitrophenol, and o-halogenophenols, to catechol.	2-aminophenol	114-127	salicylate hydroxylase	Pseudomonas putida	0-22