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Literature summary for 1.14.13.163 extracted from

  • Yu, H.; Hausinger, R.; Tang, H.; Xu, P.
    Mechanism of the 6-hydroxy-3-succinoyl-pyridine 3-monooxygenase flavoprotein from Pseudomonas putida S16 (2014), J. Biol. Chem., 289, 29158-29170 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene hspB, phylogenetic analysis and tree, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas putida

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information stopped-flow spectroscopy and kinetic analysis Pseudomonas putida
0.173
-
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate pH 8.0, 25°C, recombinant His-tagged enzyme Pseudomonas putida
0.0294
-
NADH pH 8.0, 25°C, recombinant His-tagged enzyme Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 Pseudomonas putida
-
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 Pseudomonas putida S16
-
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-
Pseudomonas putida S16
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Pseudomonas putida

Storage Stability

Storage Stability Organism
-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 Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information mass spectrometric analysis of substrates and products, with recombinant enzyme Pseudomonas putida ?
-
?
additional information mass spectrometric analysis of substrates and products, with recombinant enzyme Pseudomonas putida S16 ?
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
-
Pseudomonas putida 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
-
Pseudomonas putida S16 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
?

Synonyms

Synonyms Comment Organism
hspB
-
Pseudomonas putida
6-hydroxy-3-succinoyl-pyridine 3-monooxygenase
-
Pseudomonas putida
HSP 3-monooxygenase
-
Pseudomonas putida

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Pseudomonas putida

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.49
-
NADH pH 8.0, 25°C, recombinant His-tagged enzyme Pseudomonas putida
7.74
-
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate pH 8.0, 25°C, recombinant His-tagged enzyme Pseudomonas putida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
NADH
-
Pseudomonas putida
FAD
-
Pseudomonas putida

General Information

General Information Comment Organism
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 Pseudomonas putida
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 Pseudomonas putida
additional information free H2O2 does not catalyze the HspB enzyme reaction Pseudomonas putida