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Information on EC 1.14.13.163 - 6-hydroxy-3-succinoylpyridine 3-monooxygenase
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1.14.13.163 6-hydroxy-3-succinoylpyridine 3-monooxygenaseIUBMB Comments
The enzyme catalyses a reaction in the nicotine degradation pathway of Pseudomonas species. One of the enzymes from the soil bacterium Pseudomonas putida S16 contains an FAD cofactor .
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Word Map
- 1.14.13.163
- pyrrolidine
- putida
- 2,5-dihydroxypyridine
- tumefaciens
-
agrobacterium
-
alkaloid
- arthrobacter
-
ochrobactrum
-
fad-binding
- flavoprotein
-
nicotine-degrading
- synthesis
- wastes
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
hsp hydroxylase, 6-hydroxy-3-succinoylpyridine hydroxylase, nicotine hydroxylase, nadh-dependent hsp hydroxylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-hydroxy-3-succinoyl-pyridine 3-monooxygenase
6-hydroxy-3-succinoylpyridine hydroxylase
AWN88_01205
Hsh
HSP 3-monooxygenase
HSP hydroxylase
hspB
HSPH
NADH-dependent HSP hydroxylase
NIC
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
catalytic mechanism, overview. In contrast to conclusions reported previously, the second product of the HspB reaction is shown to be succinate, with isotope labeling experiments providing direct evidence that the newly introduced oxygen atom of succinate is derived from H2O. Reduced HspB reacts with oxygen to form a C(4a)-(hydro)peroxyflavin intermediate before it is converted to the oxidized flavoenzyme species. The formed C(4a)-hydroperoxyflavin intermediate reacts with HSP to form an intermediate that is hydrolyzed to the products 2,5-dihydroxypyridine and succinate
-
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
catalytic mechanism, overview. In contrast to conclusions reported previously, the second product of the HspB reaction is shown to be succinate, with isotope labeling experiments providing direct evidence that the newly introduced oxygen atom of succinate is derived from H2O. Reduced HspB reacts with oxygen to form a C(4a)-(hydro)peroxyflavin intermediate before it is converted to the oxidized flavoenzyme species. The formed C(4a)-hydroperoxyflavin intermediate reacts with HSP to form an intermediate that is hydrolyzed to the products 2,5-dihydroxypyridine and succinate
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate,NADH:oxygen oxidoreductase (3-hydroxylating, succinate semialdehyde releasing)
The enzyme catalyses a reaction in the nicotine degradation pathway of Pseudomonas species. One of the enzymes from the soil bacterium Pseudomonas putida S16 contains an FAD cofactor [2].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
6-hydroxy-3-succinoylpyridine + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
oxidative decarboxylation of HSP to 2,5-dihydroxypyridine in presence of NADH and FAD
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
oxidative decarboxylation of HSP to 2,5-dihydroxypyridine in presence of NADH and FAD
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
the enzyme efficiently catalyzes the conversion of 6-hydroxy-3-succinoylpyridine (HSP) into 2,5-dihydroxypyridine (2,5-DHP) and succinic acid in the presence of NADH and FAD
-
?
6-hydroxy-3-succinoylpyridine + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
6-hydroxy-3-succinoylpyridine + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
additional information
?
-
no activity with p-nitrophenol or 6-hydroxynicotinate as substrates
-
?
additional information
?
-
no activity with p-nitrophenol or 6-hydroxynicotinate as substrates
-
?
additional information
?
-
-
no activity with p-nitrophenol or 6-hydroxynicotinate as substrates
-
?
additional information
?
-
-
mass spectrometric analysis of substrates and products, with recombinant enzyme
-
?
additional information
?
-
-
mass spectrometric analysis of substrates and products, with recombinant enzyme
-
?
additional information
?
-
-
assay method optimization, overview. Product identification by LC-MS
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme is not significantly affected by Ni2+, Ca2+, K+, and Na+ at 5 mM. The enzyme is no metalloenzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by Twen-20, Tween-40, and Tween-80 at 1% w/v
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-hydroxy-3-succinoylpyridine
acts as an initial effector and strongly stimulates NADH oxidation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
stopped-flow spectroscopy and kinetic analysis
-
0.173
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate
-
pH 8.0, 25°C, recombinant His-tagged enzyme
0.201
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate
pH 8.0, 25°C, recombinant His-tagged enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.74
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate
-
pH 8.0, 25°C, recombinant His-tagged enzyme
21.6
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate
pH 8.0, 25°C, recombinant His-tagged enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from soil samples obtained from a field under continuous tobacco cropping in Henan, P.R. China
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
strain SJY uses nicotine as a sole source of carbon, nitrogen, and energy
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
-
phylogenetic analysis reveals that HspB is the most closely related to two p-nitrophenol 4-monooxygenases, and the experimental results exhibit that p-nitrophenol is a substrate of HspB
evolution
sequence alignment and phylogenetic analysis suggests that the VPP pathway, which evolved independently from nicotinic acid degradation, might have a closer relationship with the pyrrolidine pathway
evolution
-
phylogenetic analysis reveals that HspB is the most closely related to two p-nitrophenol 4-monooxygenases, and the experimental results exhibit that p-nitrophenol is a substrate of HspB
metabolism
6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation. 6-Hydroxy-3-succinoylpyridine (HSP) is a key intermediate connecting the two pathways, pyridine pathway and pyrrolidine pathway, detailed overview
metabolism
6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation. 6-Hydroxy-3-succinoylpyridine (HSP) is a key intermediate connecting the two pathways, pyridine pathway and pyrrolidine pathway, overview
metabolism
strain SJY1 efficiently degrades nicotine via a variant of the pyridine and pyrrolidine pathways (the VPP pathway), highlighting bacterial metabolic diversity in relation to nicotine degradation, a 97-kbp DNA fragment containing six nicotine degradation-related genes is obtained by gap closing from the genome sequence of strain SJY1, gene vppD gene encodes an NADH-dependent flavin-containing monooxygenase, which catalyzes the hydroxylation of 6-hydroxy-3-succinoylpyridine to 2,5-dihydroxypyridine. Nicotine degradation pathway in strain SJY1, detailed overview
metabolism
-
6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation. 6-Hydroxy-3-succinoylpyridine (HSP) is a key intermediate connecting the two pathways, pyridine pathway and pyrrolidine pathway, detailed overview
metabolism
-
6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation. 6-Hydroxy-3-succinoylpyridine (HSP) is a key intermediate connecting the two pathways, pyridine pathway and pyrrolidine pathway, overview
physiological function
-
strain S33 can transform nicotine into renewable hydroxylated-pyridine intermediates by a special pathway, in which at least three intermediates, 6-hydroxy-L-nicotine, 6-hydroxy-3-succinoylpyridine, and 2,5-dihydroxypyridine, have potential to be further chemically modified into useful compounds. Strain S33 is able to transform nicotine to 6-hydroxy-pseudooxynicotine first via the pyridine pathway through 6-hydroxy-L-nicotine and 6-hydroxy-N-methylmyosmine, and then, it turns to the pyrrolidine pathway with the formation of 6-hydroxy-3-succinoylpyridine and 2,5-dihydroxypyridine
physiological function
-
6-hydroxy-3-succinoyl-pyridine (HSP) 3-monooxygenase (HspB) is a flavoprotein essential to the pyrrolidine pathway of nicotine degradation, it catalyzes pyridine-ring beta-hydroxylation, resulting in carbon-carbon cleavage and production of 2,5-dihydroxypyridine
physiological function
the key enzyme HSP hydroxylase is involved in the fused nicotine degradation pathway of the pyridine and pyrrolidine pathways
physiological function
-
strain S33 can transform nicotine into renewable hydroxylated-pyridine intermediates by a special pathway, in which at least three intermediates, 6-hydroxy-L-nicotine, 6-hydroxy-3-succinoylpyridine, and 2,5-dihydroxypyridine, have potential to be further chemically modified into useful compounds. Strain S33 is able to transform nicotine to 6-hydroxy-pseudooxynicotine first via the pyridine pathway through 6-hydroxy-L-nicotine and 6-hydroxy-N-methylmyosmine, and then, it turns to the pyrrolidine pathway with the formation of 6-hydroxy-3-succinoylpyridine and 2,5-dihydroxypyridine
physiological function
-
the key enzyme HSP hydroxylase is involved in the fused nicotine degradation pathway of the pyridine and pyrrolidine pathways
physiological function
-
6-hydroxy-3-succinoyl-pyridine (HSP) 3-monooxygenase (HspB) is a flavoprotein essential to the pyrrolidine pathway of nicotine degradation, it catalyzes pyridine-ring beta-hydroxylation, resulting in carbon-carbon cleavage and production of 2,5-dihydroxypyridine
additional information
-
free H2O2 does not catalyze the HspB enzyme reaction
additional information
the ativity of VppD is 10fold higher than the activity of the hydroxylase (HspB) from Pseudomonas putida strain S16
additional information
-
free H2O2 does not catalyze the HspB enzyme reaction
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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). A0A2S6T7D1_9PROT
399
1
45139
TrEMBL
-
A0A2S6UVF6_9PROT
401
1
45564
TrEMBL
-
A0A644V4Z8_9ZZZZ
206
0
23920
TrEMBL
other Location (Reliability: 1)
A0A5J4Q3J9_9ZZZZ
211
0
24661
TrEMBL
other Location (Reliability: 1)
A0A518JQ03_9BACT
404
0
43350
TrEMBL
-
A0A2S6T7D7_9PROT
145
0
16247
TrEMBL
-
A0A080M9Z4_9PROT
205
0
23456
TrEMBL
-
A0A011PHW2_9PROT
206
0
23724
TrEMBL
-
A0A2S6TBB9_9PROT
281
0
30825
TrEMBL
-
A0A5J4RB66_9ZZZZ
216
0
25121
TrEMBL
other Location (Reliability: 2)
A0A1J5QIF8_9ZZZZ
229
0
26298
TrEMBL
other Location (Reliability: 2)
A0A518CVL2_9BACT
425
0
45614
TrEMBL
-
A0A0P1GWL9_9RHOB
208
0
23549
TrEMBL
-
A0A5J4R3Q5_9ZZZZ
218
0
25169
TrEMBL
other Location (Reliability: 2)
A0A5J4Q8R6_9ZZZZ
55
0
6258
TrEMBL
other Location (Reliability: 3)
A0A5J4QAB2_9ZZZZ
212
0
24761
TrEMBL
other Location (Reliability: 2)
A0A2S6U000_9PROT
403
1
45432
TrEMBL
-
A0A0S4HUC5_9PSED
229
0
26210
TrEMBL
-
A0A2S6UK35_9PROT
86
0
9318
TrEMBL
-
A0A5J4PGN9_9ZZZZ
211
0
24611
TrEMBL
other Location (Reliability: 2)
A0A0S4HSX2_9PSED
317
0
36105
TrEMBL
-
A0A1Y2P0K7_STRFR
590
0
64999
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
deletion of a GADGA motif in the FAD binding-domain results in complete loss of activity in the mutant protein
additional information
-
deletion of a GADGA motif in the FAD binding-domain results in complete loss of activity in the mutant protein
additional information
-
deletion of a GADGA motif in the FAD binding-domain results in complete loss of activity in the mutant protein
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
7 - 9
-
purified enzyme, 30°C, 30 min, over 50% activity remaining within this range
744640
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified recombinant His-tagged enzyme HspB, as a frozen solution or dry powder, no change in activity for at least 3 months, pH 8.0
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 17.6fold to homogeneity by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, and gel filtration, recombinant His-tagged enzyme 6.2fold from Escherichia coli strain B21-Codon Plus(DE3)-RIL by nickel affinity chromatography and gel filtration
-
native enzyme 64.4fold from Agrobacterium tumefaciens strain S33 cells by ammonium sulfate fractionation, hydrophobic interaction chromatography, desalting gel filtration, and two different steps of anion exchange chromatography, followed by gel filtration. Recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, anion exchange chromatography, and ultrafiltration. During purification, all the buffers are supplemented with 0.005 mM FAD. When FAD is omitted, the purification yield is very low
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography. FAD is partly lost during the purification
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, RT-PCR expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene hspB, phylogenetic analysis and tree, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene vppD cloned from a 97-kbp DNA fragment containing six nicotine degradation-related genes which is obtained by gap closing from the genome sequence of strain SJY1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged enzyme in Escherichia coli strain B21-Codon Plus(DE3)-RIL
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
development of an efficient process to transform HSP into 2,5-dihydroxypyridine (2,5-DHP) with heterologously expressed HSP hydroxylase and NADH-regenerating system, because 2,5-DHP, the product of the reaction catalyzed by HSP hydroxylase, is a valuable precursor for the chemical synthesis of 5-aminolevulinic acid, which is applied as a plant growth hormone, a herbicide and in cancer therapy
synthesis
-
enzyme HSPHZZ can be used for the enzymatic production of 2,5-dihydroxypyridine in biotechnology applications. 85.3 mg/l 2,5-dihydroxypyridine is produced in 40 min with a conversion of 74.9% at 30°C, pH 8.5, 1.0 mM substrate concentration, and 0.001 mM enzyme concentration
synthesis
-
development of an efficient process to transform HSP into 2,5-dihydroxypyridine (2,5-DHP) with heterologously expressed HSP hydroxylase and NADH-regenerating system, because 2,5-DHP, the product of the reaction catalyzed by HSP hydroxylase, is a valuable precursor for the chemical synthesis of 5-aminolevulinic acid, which is applied as a plant growth hormone, a herbicide and in cancer therapy
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tang, H.; Wang, S.; Ma, L.; Meng, X.; Deng, Z.; Zhang, D.; Ma, C.; Xu, P.
A novel gene, encoding 6-hydroxy-3-succinoylpyridine hydroxylase, involved in nicotine degradation by Pseudomonas putida strain S16
Appl. Environ. Microbiol.
74
1567-1574
2008
Pseudomonas putida (B1N1A2), Pseudomonas putida S16 (B1N1A2), Pseudomonas putida S16
brenda
Wang, S.; Huang, H.; Xie, K.; Xu, P.
Identification of nicotine biotransformation intermediates by Agrobacterium tumefaciens strain S33 suggests a novel nicotine degradation pathway
Appl. Microbiol. Biotechnol.
95
1567-1578
2012
Agrobacterium tumefaciens, Agrobacterium tumefaciens S33
brenda
Tang, H.; Yao, Y.; Zhang, D.; Meng, X.; Wang, L.; Yu, H.; Ma, L.; Xu, P.
A novel NADH-dependent and FAD-containing hydroxylase is crucial for nicotine degradation by Pseudomonas putida
J. Biol. Chem.
286
39179-39187
2011
Pseudomonas putida (F8G0M4), Pseudomonas putida, Pseudomonas putida S16 (F8G0M4), Pseudomonas putida S16
brenda
Yu, H.; Tang, H.; Zhu, X.; Li, Y.; Xu, P.
Molecular mechanism of nicotine degradation by a newly isolated strain, Ochrobactrum sp. strain SJY1
Appl. Environ. Microbiol.
81
272-281
2015
Ochrobactrum sp. (A0A075XAG5)
brenda
Li, H.; Xie, K.; Yu, W.; Hu, L.; Huang, H.; Xie, H.; Wang, S.
Nicotine dehydrogenase complexed with 6-hydroxypseudooxynicotine oxidase involved in the hybrid nicotine-degrading pathway in Agrobacterium tumefaciens S33
Appl. Environ. Microbiol.
82
1745-1755
2016
Agrobacterium tumefaciens (W8E0Y0), Agrobacterium tumefaciens S33 (W8E0Y0)
brenda
Wei, T.; Zang, J.; Zheng, Y.; Tang, H.; Huang, S.; Mao, D.
Characterization of a novel nicotine hydroxylase from Pseudomonas sp. ZZ-5 that catalyzes the conversion of 6-hydroxy-3-succinoylpyridine into 2,5-dihydroxypyridine
Catalysts
7
272-281
2017
Pseudomonas sp. ZZ-5
brenda
Yu, H.; Hausinger, R.; Tang, H.; Xu, P.
Mechanism of the 6-hydroxy-3-succinoyl-pyridine 3-monooxygenase flavoprotein from Pseudomonas putida S16
J. Biol. Chem.
289
29158-29170
2014
Pseudomonas putida, Pseudomonas putida S16
brenda
Li, H.; Xie, K.; Huang, H.; Wang, S.
6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation in Agrobacterium tumefaciens S33
PLoS ONE
9
e103324
2014
Agrobacterium tumefaciens (W8E0Y0), Agrobacterium tumefaciens S33 (W8E0Y0), Agrobacterium tumefaciens S33
brenda
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