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2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
2-(2'-hydroxyphenyl)ethene-1-sulfinate + H2O
o-hydroxystyrene + sulfite
2-(2-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
2-phenylbenzenesulfinate + H2O
biphenyl + sulfite
additional information
?
-
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
?
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
-
?
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
?
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
?
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
-
highly specific for
-
?
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
the enzyme is involved in biodesulfurization, an option for enzymatically removing sulfur from the recalcitrant thiophenic derivatives that comprise the majority of organosulfur compounds remaining in hydrotreated petroleum products
-
-
?
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
electrophilic aromatic substitution mechanism. The catalytic cysteine in the enzyme DszB (C27) acts as a proton donor. The nascent ionized C27 at the transition state is stabilized by H60, whose charge is modulated by hydrogen bond interaction with S25
-
-
?
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
?
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
?
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
?
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
-
highly specific for
-
?
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
ir
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
final step of the desulfurozation of dibenzothiophene
-
ir
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
ir
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
final step of the desulfurozation of dibenzothiophene
-
ir
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
specific for
-
?
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
final step of the desulfurozation of dibenzothiophene
-
?
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
specific for
-
?
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
final step of the desulfurozation of dibenzothiophene
-
?
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
?
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
?
2-(2'-hydroxyphenyl)ethene-1-sulfinate + H2O
o-hydroxystyrene + sulfite
-
-
-
?
2-(2'-hydroxyphenyl)ethene-1-sulfinate + H2O
o-hydroxystyrene + sulfite
-
-
-
?
2-(2-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
-
?
2-(2-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
the microbial conversion of DBT into 2-HBP is accomplished by the 4S pathway, consisting of two monooxygenases, DszC and DszA, and one desulfinase, DszB, which are encoded by the dsz operon
-
-
?
2-phenylbenzenesulfinate + H2O
biphenyl + sulfite
-
-
-
?
2-phenylbenzenesulfinate + H2O
biphenyl + sulfite
-
-
-
?
additional information
?
-
-
no activity with xanthene, 2-hydroxydiphenylmetane, 2-methoxybiphenyl, phenylhydroquinone, 2-biphenyl carboxylic acid, 2-amino-4-phenylphenol
-
?
additional information
?
-
-
no activity with xanthene, 2-hydroxydiphenylmetane, 2-methoxybiphenyl, phenylhydroquinone, 2-biphenyl carboxylic acid, 2-amino-4-phenylphenol
-
?
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2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
?
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
the enzyme is involved in biodesulfurization, an option for enzymatically removing sulfur from the recalcitrant thiophenic derivatives that comprise the majority of organosulfur compounds remaining in hydrotreated petroleum products
-
-
?
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
?
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
final step of the desulfurozation of dibenzothiophene
-
ir
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
final step of the desulfurozation of dibenzothiophene
-
ir
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
final step of the desulfurozation of dibenzothiophene
-
?
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
final step of the desulfurozation of dibenzothiophene
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
the microbial conversion of DBT into 2-HBP is accomplished by the 4S pathway, consisting of two monooxygenases, DszC and DszA, and one desulfinase, DszB, which are encoded by the dsz operon
-
-
?
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2,2'-Dihydroxybiphenyl
-
competitive
2,3-Dihydroxybiphenyl
-
competitive
Ag+
-
strong inhibition at 1 mM
Co2+
-
18% inhibition at 0.1 mM
Hg2+
-
strong inhibition at 1 mM
iodoacetic acid
-
95% inhibition at 1 mM
Mn2+
-
71% inhibition at 1 mM
N-bromosuccimide
-
complete inhibition at 0.01 mM after 10 min
Ni2+
-
24% inhibition at 1 mM
o-hydroxystyrene
-
product inhibition, 80% inhibition at 5 mM, the OH-group is important for the inhibitory effect
phenylglyoxal hydrate
-
19% inhibition at 0.01 mM after 10 min
pyridoxal-5-phosphate
-
38% inhibition at 0.01 mM after 10 min
Tetranitromethane
-
complete inhibition at 0.01 mM after 10 min
2-Hydroxybiphenyl
-
30% inhibition at 5 mM, the OH-group is important for the inhibitory effect
2-Hydroxybiphenyl
-
competitive, product inhibition
Cu2+
-
67% inhibition at 1 mM
Cu2+
-
95% inhibition at 0.1 mM
Cu2+
-
strong inhibition at 1 mM
DTNB
-
86% inhibition at 0.1 mM
DTNB
-
complete inhibition at 0.01 mM after 10 min
DTNB
-
strong inhibition at 1 mM
Fe2+
-
44% inhibition at 1 mM
Fe2+
-
11% inhibition at 0.1 mM
N-ethylmaleimide
-
complete inhibition at 1 mM
N-ethylmaleimide
-
strong inhibition at 1 mM
p-chloromercuribenzoate
-
92% inhibition at 0.1 mM
p-chloromercuribenzoate
-
strong inhibition at 1 mM
Zn2+
-
98% inhibition at 1 mM
Zn2+
-
50% inhibition at 0.1 mM
additional information
-
no inhibition by 1,10-phenanthroline and EDTA, no inhibition by Co2+, Ca2+, and Mg2+, no inhibition by biphenyl, 2-methylbiphenyl, and 2-methoxybiphenyl
-
additional information
-
no product inhibition, no inhibition by Mn2+, Mg2+, and Ca2
-
additional information
-
no inhibition by product sulfite, no inhibition by chelating agents EDTA, 1,10-phenanthroline, and 8-hydroxyquinone
-
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C26S
-
site-directed mutagenesis of the only cysteine residue results in an completely inactive mutant
H60Q
-
mutation causes an 17fold reduction in the specific activity
Q65H
increase in thermostability, decrease in catalytic activity
R70I
-
inactive mutant mostly exists in the insoluble fraction of the cell extract
R70K
-
inactive mutant mostly exists in the insoluble fraction of the cell extract
Y63A
increase in catalytic activity
Y63F
increase in catalytic activity, similar thermostability as wild-type
Y63F/Q65H
increase in thermostability without loss of catalytic activity or affinity for substrate
Y63K
decrease in activity
Y63S
affinity for the substrate is about 7-fold lower than that of the wild-type enzyme
Y63W
activity similar to wild-type
Q65H
-
increase in thermostability, decrease in catalytic activity
-
Y63A
-
increase in catalytic activity
-
Y63F
-
increase in catalytic activity, similar thermostability as wild-type
-
Y63S
-
affinity for the substrate is about 7-fold lower than that of the wild-type enzyme
-
Y63W
-
activity similar to wild-type
-
C26S
-
site-directed mutagenesis of the only cysteine residue results in an completely inactive mutant
-
C17S
-
site-directed mutagenesis of the only cysteine residue results in an completely inactive mutant
C17S
-
site-directed mutagenesis of the only cysteine residue results in an completely inactive mutant
-
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energy production
-
the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels
energy production
-
the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels
energy production
-
the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels
-
additional information
-
environmental protection, the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels
additional information
-
environmental protection, the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels
additional information
-
environmental protection, the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels
-
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Oldfield, C.; Pogrebinsky, O.; Simmonds, J.; Olson, E.S.; Kulpa, C.F.
Elucidation of the metabolic pathway for dibenzothiophene desulphurization by Rhodococcus sp. strain IGTS8 (ATCC 53968)
Microbiology
143
2961-2973
1997
Rhodococcus rhodochrous, Rhodococcus rhodochrous IGTS8 / ATCC 53968
brenda
Konishi, J.; Maruhashi, K.
2-(2'-Hydroxyphenyl)benzene sulfinate desulfinase from the thermophilic desulfurizing bacterium Paenibacillus sp. strain A11-2: purification and characterization
Appl. Microbiol. Biotechnol.
62
356-361
2003
Paenibacillus sp., Paenibacillus sp. A11-2
brenda
Watkins, L.M.; Rodriguez, R.; Schneider, D.; Broderick, R.; Cruz, M.; Chambers, R.; Ruckman, E.; Cody, M.; Mrachko, G.T.
Purification and characterization of the aromatic desulfinase, 2-(2'-hydroxyphenyl)benzenesulfinate desulfinase
Arch. Biochem. Biophys.
415
14-23
2003
Rhodococcus erythropolis, Rhodococcus erythropolis IGTS8 / ATCC 53968
brenda
Nakayama, N.; Matsubara, T.; Ohshiro, T.; Moroto, Y.; Kawata, Y.; Koizumi, K.; Hirakawa, Y.; Suzuki, M.; Maruhashi, K.; Izumi, Y.; Kurane, R.
A novel enzyme, 2'-hydroxybiphenyl-2-sulfinate desulfinase (DszB), from a dibenzothiophene-desulfurizing bacterium Rhodococcus erythropolis KA2-5-1: gene overexpression and enzyme characterization
Biochim. Biophys. Acta
1598
122-130
2002
Rhodococcus erythropolis, Rhodococcus erythropolis KA2-5-1
brenda
Lee, W.C.; Ohshiro, T.; Matsubara, T.; Izumi, Y.; Tanokura, M.
Crystallization and preliminary x-ray analyses of desulfurization enzyme DszB and its C27S mutant complexed with biphenyl-2-sulfinic acid
Acta Crystallogr. Sect. D
D60
1636-1638
2004
Rhodococcus sp., Rhodococcus sp. IGTS8
brenda
Lee, W.C.; Ohshiro, T.; Matsubara, T.; Izumi, Y.; Tanokura, M.
Crystal structure and desulfurization mechanism of 2'-hydroxybiphenyl-2-sulfinic acid desulfinase
J. Biol. Chem.
281
32534-32539
2006
Rhodococcus erythropolis
brenda
Ohshiro, T.; Ohkita, R.; Takikawa, T.; Manabe, M.; Lee, W.C.; Tanokura, M.; Izumi, Y.
Improvement of 2-hydroxybiphenyl-2-sulfinate desulfinase, an enzyme involved in the dibenzothiophene desulfurization pathway, from Rhodococcus erythropolis KA2-5-1 by site-directed mutagenesis
Biosci. Biotechnol. Biochem.
71
2815-2821
2007
Rhodococcus erythropolis (P54997), Rhodococcus erythropolis IGTS8 / ATCC 53968 (P54997)
brenda
Li, G.Q.; Li, S.S.; Zhang, M.L.; Wang, J.; Zhu, L.; Liang, F.L.; Liu, R.L.; Ma, T.
Genetic rearrangement strategy for optimizing the dibenzothiophene biodesulfurization pathway in Rhodococcus erythropolis
Appl. Environ. Microbiol.
74
971-976
2008
Rhodococcus erythropolis
brenda
Calzada, J.; Zamarro, M.T.; Alcon, A.; Santos, V.E.; Diaz, E.; Garcia, J.L.; Garcia-Ochoa, F.
Analysis of dibenzothiophene desulfurization in a recombinant Pseudomonas putida strain
Appl. Environ. Microbiol.
75
875-877
2009
Pseudomonas putida, Pseudomonas putida CECT 5279
brenda
Geronimo, I.; Nigam, S.R.; Payne, C.M.
Desulfination by 2-hydroxybiphenyl-2-sulfinate desulfinase proceeds via electrophilic aromatic substitution by the cysteine-27 proton
Chem. Sci.
8
5078-5086
2017
Rhodococcus erythropolis (Q6WE14), Rhodococcus erythropolis
brenda
Yu, Y.; Mills, L.C.; Englert, D.L.; Payne, C.M.
Inhibition mechanisms of Rhodococcus erythropolis 2-hydroxybiphenyl-2-sulfinate desulfinase (DszB)
J. Phys. Chem. B
123
9054-9065
2019
Rhodococcus erythropolis (Q6WE14), Rhodococcus erythropolis, Rhodococcus erythropolis IGTS8 (Q6WE14), Rhodococcus erythropolis IGTS8
brenda