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Information on EC 1.13.11.38 - 1-hydroxy-2-naphthoate 1,2-dioxygenase
for references in articles please use BRENDA:EC1.13.11.38
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EC Tree 1 Oxidoreductases
1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
1.13.11 With incorporation of two atoms of oxygen
1.13.11.38 1-hydroxy-2-naphthoate 1,2-dioxygenase
IUBMB Comments
Requires Fe2+. Involved, with EC 4.1.2.34 4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase, in the metabolism of phenanthrene in bacteria.
The enzyme appears in viruses and cellular organisms
- 1.13.11.38
- nocardioides
- gentisate
- salicylate
- phenanthrene
-
ring-cleaving
- salicylatoxidans
-
pseudaminobacter
-
phenanthrene-degrading
- 2-carboxybenzaldehyde
- alcaligenes
- sphingomonas
-
unobserved
-
extradiol-type
showSynonyms
1-hydroxy-2-naphthoate dioxygenase, diox1, diox2, 1-hndo, 1-h2na dioxygenase, 1-hydroxy-2-naphthoic acid dioxygenase, 1h2ndo, 1-hydroxy-2-naphthoate 1,2-dioxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-H2NA dioxygenase
1-hydroxy-2-naphthoate 1,2-dioxygenase
1-hydroxy-2-naphthoate dioxygenase
1-hydroxy-2-naphthoate-degrading enzyme
-
-
-
-
1-hydroxy-2-naphthoic acid dioxygenase
1H2NDO
Diox1
Diox2
oxygenase, 1-hydroxy-2-naphthoate di-
-
-
-
-
Sphe3 1-H2NA dioxygenase
1-hydroxy-2-naphthoic acid dioxygenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-hydroxy-2-naphthoate + O2 = (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
1-hydroxy-2-naphthoate:oxygen 1,2-oxidoreductase (decyclizing)
Requires Fe2+. Involved, with EC 4.1.2.34 4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase, in the metabolism of phenanthrene in bacteria.
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CAS REGISTRY NUMBER
COMMENTARY
85941-64-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-hydroxy-2-naphthoic acid + O2
2-carboxybenzylpyruvic acid
-
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Gram-negative coccus
-
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Gram-negative coccus B156
-
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Substrates: -
Products: i.e. trans-2'-carboxybenzalpyruvate
Products: i.e. trans-2'-carboxybenzalpyruvate
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: -
Products: i.e. trans-2'-carboxybenzalpyruvate. The structure of the ring cleavage product is determined upon separation by high-performance liquid chromatography at pH 2.5 by using nuclear magnetic resonance and mass spectroscopic techniques
Products: i.e. trans-2'-carboxybenzalpyruvate. The structure of the ring cleavage product is determined upon separation by high-performance liquid chromatography at pH 2.5 by using nuclear magnetic resonance and mass spectroscopic techniques
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: enzyme is involved in degradation of phenanthrene
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Substrates: the enzyme is involved in degradation of phenanthrene
Products: i.e. trans-2'-carboxybenzalpyruvate
Products: i.e. trans-2'-carboxybenzalpyruvate
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: enzyme is involved in degradation of phenanthrene
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: -
Products: i.e. trans-2'-carboxybenzalpyruvate. The structure of the ring cleavage product is determined upon separation by high-performance liquid chromatography at pH 2.5 by using nuclear magnetic resonance and mass spectroscopic techniques
Products: i.e. trans-2'-carboxybenzalpyruvate. The structure of the ring cleavage product is determined upon separation by high-performance liquid chromatography at pH 2.5 by using nuclear magnetic resonance and mass spectroscopic techniques
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Substrates: -
Products: i.e. trans-2'-carboxybenzalpyruvate
Products: i.e. trans-2'-carboxybenzalpyruvate
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Substrates: the enzyme is involved in degradation of phenanthrene
Products: i.e. trans-2'-carboxybenzalpyruvate
Products: i.e. trans-2'-carboxybenzalpyruvate
?
1-hydroxy-2-naphthoate + O2
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: -
Products: -
Products: -
r
1-hydroxy-2-naphthoate + O2
?
-
Substrates: gentisate 1,2-dioxygenase with an extraordinary substrate range. Relative activities with salicylate, 5-aminosalicylate, 1-hydroxy-2-naphthoate, and gentisate with both preparations are about 1:10:40:120
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
?
-
Substrates: gentisate 1,2-dioxygenase with an extraordinary substrate range. Relative activities with salicylate, 5-aminosalicylate, 1-hydroxy-2-naphthoate, and gentisate with both preparations are about 1:10:40:120
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with: gentisate, 3-hydroxyanthranilate, 2-hydroxy-1-naphthoate, 3-hydroxy-2-naphthoate, salicylate, m-hydroxybenzoate, p-hydroxybenzoate, and protocatechuate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with: gentisate, 3-hydroxyanthranilate, 2-hydroxy-1-naphthoate, 3-hydroxy-2-naphthoate, salicylate, m-hydroxybenzoate, p-hydroxybenzoate, and protocatechuate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with 3-hydroxy-2-naphthoic acid
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with 3-hydroxy-2-naphthoic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 3-hydroxy-2-naphthoic acid
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with 3-hydroxy-2-naphthoic acid
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with 3-hydroxy-2-naphthoic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: 1-hydroxy-2-naphthoic acid dioxygenase shows no activity with gentisic acid, salicylic acid and other hydroxynaphthoic acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: Pseudomonas sp. strain PPD can metabolize phenanthrene as the sole source of carbon and energy via the phthalic acid route
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-hydroxy-2-naphthoic acid + O2
2-carboxybenzylpyruvic acid
-
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: enzyme is involved in degradation of phenanthrene
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Substrates: the enzyme is involved in degradation of phenanthrene
Products: i.e. trans-2'-carboxybenzalpyruvate
Products: i.e. trans-2'-carboxybenzalpyruvate
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: enzyme is involved in degradation of phenanthrene
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Substrates: the enzyme is involved in degradation of phenanthrene
Products: i.e. trans-2'-carboxybenzalpyruvate
Products: i.e. trans-2'-carboxybenzalpyruvate
?
1-hydroxy-2-naphthoate + O2
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-naphthoate + O2
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 1-hydroxy-2-naphthoic acid dioxygenase shows no activity with gentisic acid, salicylic acid and other hydroxynaphthoic acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: Pseudomonas sp. strain PPD can metabolize phenanthrene as the sole source of carbon and energy via the phthalic acid route
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
enzyme contains 1.15 mol of Fe(II)/mol of the subunit. Fe2+ is required for the enzyme to exhibit activity
Fe2+
-
salicylate 1,2-dioxygenase is an iron (II) class III ring cleaving dioxygenase
Fe2+
Sphe3 1-H2NA dioxygenase is iron-dependent
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition when the concentration of the substrate 1-hydroxy-2-naphthoate is 0.01 mM and that of the tested compounds is 0.1 or 1 mM: gentisate, 3-hydroxyanthranilate, 2-hydroxy-1-naphthoate, salicylate, m-hydroxybenzoate, p-hydroxybenzoate, and protocatechuate
-
o-phenanthroline
0.1 mM, reactivation by incubating with FeSO4 and ascorbic acid
o-phenanthroline
inhibits at 0.01 mM, addition of 0.1 mM FeSO4 restores the enzyme activity; inhibits at 0.01 mM, addition of 0.1 mM FeSO4 restores the enzyme activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.046
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, mutant M46V
0.08
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, mutant A85H
0.08
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, mutant L38Q
0.14
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme
0.144
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, mutant W104Y
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.2
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, mutant L38Q
3.31
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, mutant A85H
4.6
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, mutant W104Y
17
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, mutant M46V
24
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
27.5
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, mutant L38Q
32
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, mutant W104Y
41.4
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, mutant A85H
171
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme
369.6
1-hydroxy-2-naphthoate
-
pH 8.0, temperature not specified in the publication, mutant M46V
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
180
61.5
-
after all purification steps from Pseudomonas sp. PPD cells grown on phenanthrene
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Gram-negative coccus
isolated from soil and able to grow on phenanthrene as sole source of carbon and energy
-
-
brenda
Gram-negative coccus B156
isolated from soil and able to grow on phenanthrene as sole source of carbon and energy
-
-
brenda
gene diox1; sp. nov., isolated from a Greek creosote-oil-polluted site, gene diox1
UniProt
brenda
gene diox2; sp. nov., isolated from a Greek creosote-oil-polluted site, gene diox2
UniProt
brenda
gene diox1; sp. nov., isolated from a Greek creosote-oil-polluted site, gene diox1
UniProt
brenda
gene diox2; sp. nov., isolated from a Greek creosote-oil-polluted site, gene diox2
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
strain Sphe3 grows on 2-carboxybenzaldehyde, protocatechuate, and phthalate as sole carbon sources, all intermediates of phenanthrene degradation via the phthalate pathway, whereas no growth is observed on salicylic acid
brenda
additional information
strain Sphe3 grows on 2-carboxybenzaldehyde, protocatechuate, and phthalate as sole carbon sources, all intermediates of phenanthrene degradation via the phthalate pathway, whereas no growth is observed on salicylic acid
brenda
additional information
-
strain Sphe3 grows on 2-carboxybenzaldehyde, protocatechuate, and phthalate as sole carbon sources, all intermediates of phenanthrene degradation via the phthalate pathway, whereas no growth is observed on salicylic acid
brenda
additional information
-
strain Sphe3 grows on 2-carboxybenzaldehyde, protocatechuate, and phthalate as sole carbon sources, all intermediates of phenanthrene degradation via the phthalate pathway, whereas no growth is observed on salicylic acid
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
occurrence of two diox1 and diox2 homologues in the Sphe3 genome implies that a replicative transposition event has contributed to the evolution of 1-H2NA dioxygenase in Arthrobacter phenanthrenivorans
evolution
-
occurrence of two diox1 and diox2 homologues in the Sphe3 genome implies that a replicative transposition event has contributed to the evolution of 1-H2NA dioxygenase in Arthrobacter phenanthrenivorans
-
metabolism
-
metabolic pathway for degradation of phenanthrene in Pseudomonas sp. strain PPD
metabolism
the enzyme catalyzes a step in phenanthrene degradation, overview
metabolism
-
the enzyme catalyzes a step in phenanthrene degradation, overview
-
additional information
-
salicylate 1,2-dioxygenase shares with 1-hydroxy-2-naphthoate dioxygenase its unique ability to oxidatively cleave monohydroxylated aromatic compounds. Nevertheless salicylate 1,2-dioxygenase is more versatile with respect to 1-hydroxy-2-naphthoate dioxygenase and other known gentisate dioxygenases because it cleaves not only gentisate and1-hydroxy-2-naphthoate but also salicylate and substituted salicylates, cf. EC 1.13.11.4
additional information
-
salicylate 1,2-dioxygenase shares with 1-hydroxy-2-naphthoate dioxygenase its unique ability to oxidatively cleave monohydroxylated aromatic compounds. Nevertheless salicylate 1,2-dioxygenase is more versatile with respect to 1-hydroxy-2-naphthoate dioxygenase and other known gentisate dioxygenases because it cleaves not only gentisate and1-hydroxy-2-naphthoate but also salicylate and substituted salicylates, cf. EC 1.13.11.4
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A5Q5CDY5_MYCSJ
Mycobacterium sp. (strain JLS)
361
0
40508
TrEMBL
-
A0A2S6TBJ4_9PROT
319
0
36426
TrEMBL
-
E6TIQ7_MYCSR
Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
361
0
40568
TrEMBL
-
A1T2B5_MYCVP
Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1)
361
0
40625
TrEMBL
-
F0M3R4_PSEPM
Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG 23796 / Sphe3)
387
0
42933
TrEMBL
-
A0A2S6TZF3_9PROT
317
0
36072
TrEMBL
-
F0MC51_PSEPM
Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG 23796 / Sphe3)
387
0
42781
TrEMBL
-
A4T3D9_MYCGI
Mycolicibacterium gilvum (strain PYR-GCK)
361
0
40511
TrEMBL
-
A0A5Q5BHQ3_MYCSS
Mycobacterium sp. (strain MCS)
356
0
40048
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
-
Sephacryl S-200-HR gel-filtration chromatography; SDS-PAGE under denaturing conditions, homotetramer, subunit molecular mass of about 39000
270000
42000
45000
42000
x * 42000, recombinant Diox1, x * 45000, native enzyme, SDS-PAGE
42000
x * 42000, recombinant Diox2, x * 45000, native enzyme, SDS-PAGE
45000
x * 42000, recombinant Diox1, x * 45000, native enzyme, SDS-PAGE
45000
x * 42000, recombinant Diox2, x * 45000, native enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
tetramer
?
x * 42000, recombinant Diox1, x * 45000, native enzyme, SDS-PAGE
?
x * 42000, recombinant Diox2, x * 45000, native enzyme, SDS-PAGE
?
-
x * 42000, recombinant Diox1, x * 45000, native enzyme, SDS-PAGE
-
?
-
x * 42000, recombinant Diox2, x * 45000, native enzyme, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant A85H and W104Y variants and mutant W104Y with gentiate, sitting drop vapor diffusion method, 4°C, mixing of 0.001 ml of protein solution with 0.0008 ml of crystallization solution containing 8% PEG10000 and 0.1 M Tris-HCl pH 8.0, with 0.0002 ml of a 0.1 M calcium chloride solution, crystals quality is also improved using seeding techniques, X-ray diffraction structure determination and analysis at 2.5-2.7 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A85H
-
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate than the wild-type enzyme and no more activity with gentisate. substitution of Ala85 with a histidine residue caused significant changes in the orientation of the loop containing this residue which is involved in the active site closing upon substrate binding. In SDO A85H this specific loop shifts away from the active site and thus opens the cavity favoring the binding of bulkier substrates. Since this loop also interacts with the N-terminal residues of the vicinal subunit, the structure and packing of the holoenzyme might be also affected.
L38Q
-
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate than the wild-type enzyme
W104Y
-
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows increased catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate and to the wild-type enzyme. W104Y SDO mutant exhibits reduced reaction rates for all substrates
A85H
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site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate than the wild-type enzyme and no more activity with gentisate. substitution of Ala85 with a histidine residue caused significant changes in the orientation of the loop containing this residue which is involved in the active site closing upon substrate binding. In SDO A85H this specific loop shifts away from the active site and thus opens the cavity favoring the binding of bulkier substrates. Since this loop also interacts with the N-terminal residues of the vicinal subunit, the structure and packing of the holoenzyme might be also affected.
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L38Q
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site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate than the wild-type enzyme
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W104Y
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site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows increased catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate and to the wild-type enzyme. W104Y SDO mutant exhibits reduced reaction rates for all substrates
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additional information
additional information
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generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutation M46V of salicylate 1,2-dioxygenase, rational design of mutants, structure comparisons, overview
additional information
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generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutation M46V of salicylate 1,2-dioxygenase, rational design of mutants, structure comparisons, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE