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Information on EC 3.13.1.3 - 2'-hydroxybiphenyl-2-sulfinate desulfinase
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3.13.1.3 2'-hydroxybiphenyl-2-sulfinate desulfinaseIUBMB Comments
The enzyme from Rhodococcus sp. strain IGTS8 is encoded by the plasmid-encoded dibenzothiophene-desulfurization (dsz) operon. The enzyme has a narrow substrate specificity with biphenyl-2-sulfinate being the only other substrate known to date .
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Word Map
- 3.13.1.3
-
desulfurization
- dibenzothiophene
- rhodococcus
- 2-hydroxybiphenyl
- erythropolis
-
petroleum
- sulfur
- sulfite
-
carbon-sulfur
-
biodesulfurization
-
thiophenic
- sulfonate
-
organosulfur
- energy production
The enzyme appears in viruses and cellular organisms
Synonyms
2'-hydroxybiphenyl-2-sulfinate desulfinase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2'-hydroxybiphenyl-2-sulfinate desulfinase
2-(2'-hydroxyphenyl)benzene sulfinate desulfinase
2-(2'-hydroxyphenyl)benzene sulfinate hydrolase
-
-
-
-
2-(2'-hydroxyphenyl)benzenesulfinate desulfinase
2-(2-hydroxyphenyl)benzenesulfinate:H2O hydrolase
-
-
-
-
Desulfinase
DszB
EC 3.1.2.24
-
-
formerly
-
gene dszB-encoded hydrolase
-
-
-
-
hydrolase, 2,(2'-hydroxyphenyl)benzene sulfinate
-
-
-
-
TdsB
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2'-hydroxybiphenyl-2-sulfinate + H2O = 2-hydroxybiphenyl + sulfite
-
-
-
-
2'-hydroxybiphenyl-2-sulfinate + H2O = 2-hydroxybiphenyl + sulfite
Cys26 is essential for activity
-
2'-hydroxybiphenyl-2-sulfinate + H2O = 2-hydroxybiphenyl + sulfite
Cys26 is essential for activity
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
desulfination
oxidation
-
-
-
-
reduction
-
-
-
-
desulfination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
2'-hydroxybiphenyl-2-sulfinate sulfohydrolase
The enzyme from Rhodococcus sp. strain IGTS8 is encoded by the plasmid-encoded dibenzothiophene-desulfurization (dsz) operon. The enzyme has a narrow substrate specificity with biphenyl-2-sulfinate being the only other substrate known to date [2].
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CAS REGISTRY NUMBER
COMMENTARY
198154-06-2
-
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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
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
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
-
-
?
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
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
specific for
-
?
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
final step of the desulfurozation of dibenzothiophene
-
?
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
-
-
-
?
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
Rhodococcus rhodochrous IGTS8 / ATCC 53968
-
-
-
?
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
-
-
-
?
additional information
?
-
-
no activity with xanthene, 2-hydroxydiphenylmetane, 2-methoxybiphenyl, phenylhydroquinone, 2-biphenyl carboxylic acid, 2-amino-4-phenylphenol
-
?
additional information
?
-
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
no activity with xanthene, 2-hydroxydiphenylmetane, 2-methoxybiphenyl, phenylhydroquinone, 2-biphenyl carboxylic acid, 2-amino-4-phenylphenol
-
?
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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
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
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
o-hydroxystyrene
-
product inhibition, 80% inhibition at 5 mM, the OH-group is important for the inhibitory effect
2-Hydroxybiphenyl
-
30% inhibition at 5 mM, the OH-group is important for the inhibitory effect
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0056
2'-hydroxybiphenyl-2-sulfinate
mutant Y63F, pH 7.0, 28°C
0.0082
2'-hydroxybiphenyl-2-sulfinate
wild-type, pH 7.0, 28°C
0.0098
2'-hydroxybiphenyl-2-sulfinate
mutant Y63F/Q65H, pH 7.0, 28°C
0.0556
2'-hydroxybiphenyl-2-sulfinate
mutant Y63S, pH 7.0, 28°C
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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
additional information
-
desulfurization activity in strain CECT5279 over time in vivo
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.4
-
activity decreases sigificantly below pH 6.0 and above pH 8.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 50
-
rapid loss of activity at temperatures higher or lower than the optimum
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Rhodococcus erythropolis IGTS8 / ATCC 53968
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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
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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). DSZB_RHOSG
Rhodococcus sp. (strain ATCC 53968 / IGTS8)
365
0
39045
Swiss-Prot
-
DSZB_RHOSH
Rhodococcus erythropolis (strain XP)
365
0
39045
Swiss-Prot
-
A0A1V5CI50_9DELT
375
0
40991
TrEMBL
-
A0A1S1HCW9_9SPHN
352
0
38987
TrEMBL
-
A0A841CDR3_9PSEU
341
0
36618
TrEMBL
-
A0A8B4DKM1_9MYCO
360
0
38806
TrEMBL
-
A0A0H3A3M7_MYCA1
Mycobacterium avium (strain 104)
317
0
34103
TrEMBL
-
X8DU08_9MYCO
356
0
38140
TrEMBL
-
Q6FC44_ACIAD
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
350
0
39223
TrEMBL
-
A0A1N5THK5_9MYCO
356
0
38140
TrEMBL
-
A0A1U2FDN8_9MYCO
283
0
30612
TrEMBL
-
A0A1S1HAW3_9SPHN
374
0
40972
TrEMBL
-
W0VB21_9BURK
360
0
38890
TrEMBL
-
A0A1N5ZID8_9MYCO
283
0
30612
TrEMBL
-
Q93D18_ACIAD
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
352
0
39625
TrEMBL
-
A0A1S1HCJ4_9SPHN
359
0
39189
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of DszB and an inactive mutant of DszB in complex with substrate at resolution of 1.8 A or better
-
DszB and DszB C27S mutant complexed with biphenyl-2-sulfinic acid are crystallized. The crystals of DszB belong to the orthorhombic P2(1)2(1)2(1) space group, with unit-cell parameters a = 36.7 A, b = 82.6 A, c = 139.6 A, and contain one molecule of DszB in the asymmetric unit. Crystals of DszB C27S complexed with biphenyl-2-sulfinic acid belong to space group C2 with unit-cell parameters a = 153.4 A, b = 45.9 A, c = 112.9 A, beta = 115.93°
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C17S
C26S
-
site-directed mutagenesis of the only cysteine residue results in an completely inactive mutant
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
Y63F
increase in catalytic activity, similar thermostability as wild-type
Y63F/Q65H
increase in thermostability without loss of catalytic activity or affinity for substrate
Y63S
affinity for the substrate is about 7-fold lower than that of the wild-type enzyme
Q65H
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
increase in thermostability, decrease in catalytic activity
-
Y63F
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
increase in catalytic activity, similar thermostability as wild-type
-
Y63S
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
affinity for the substrate is about 7-fold lower than that of the wild-type enzyme
-
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
recombinant enzyme, rapid loss of activity above, inactivation after 4 h
35
30 min, wild-type, almost complete loss of activity, mutant Y63F/Q65H, 90% residual activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant 7.8fold from Escherichia coli, and native from strain KA2-5-1 160fold, to homogeneity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21, activity of recombinant DszB was comparable to the natively expressed enzyme
gene dszB, DszB expression pattern in Pseudomonas putida strain CECT5279
-
gene dszB, organized in the dsz operon, DNA and amino acid sequence determination and analysis, genetic organization and expression analysis, recombinant expression in recombinant Rhodococcus erythropolis strain CGMCC 4.1491, that is dsz-deficient
-
gene dszZ, DNA sequence determination, cooverexpression in Escherichia coli with chaperonin genes groEL and groES at 25°C
-
gene tdsB, DNA sequence determination, overexpression in Escherichia coli BL21 (DE3)
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
energy production
additional information
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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Release 2023.1 (January 2023)
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