BRENDA - Enzyme Database
show all sequences of 3.13.1.1

Genetic rearrangement strategy for optimizing the dibenzothiophene biodesulfurization pathway in Rhodococcus erythropolis

Li, G.Q.; Li, S.S.; Zhang, M.L.; Wang, J.; Zhu, L.; Liang, F.L.; Liu, R.L.; Ma, T.; Appl. Environ. Microbiol. 74, 971-976 (2008)

Data extracted from this reference:

Application
Application
Commentary
Organism
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
Rhodococcus erythropolis
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
Rhodococcus erythropolis
Cloned(Commentary)
Commentary
Organism
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
Rhodococcus erythropolis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-hydroxybiphenyl + sulfite
Rhodococcus erythropolis
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'-hydroxybiphenyl-2-sulfinate + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodococcus erythropolis
-
strains DS-3, IGTS8, and KA 2-5-1, gene dszB
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-hydroxybiphenyl + sulfite
-
695760
Rhodococcus erythropolis
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
?
2-hydroxybiphenyl + sulfite
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
695760
Rhodococcus erythropolis
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
?
Application (protein specific)
Application
Commentary
Organism
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
Rhodococcus erythropolis
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
Rhodococcus erythropolis
Cloned(Commentary) (protein specific)
Commentary
Organism
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
Rhodococcus erythropolis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-hydroxybiphenyl + sulfite
Rhodococcus erythropolis
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'-hydroxybiphenyl-2-sulfinate + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-hydroxybiphenyl + sulfite
-
695760
Rhodococcus erythropolis
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
?
2-hydroxybiphenyl + sulfite
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
695760
Rhodococcus erythropolis
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
?
Other publictions for EC 3.13.1.1
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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Zolghadr
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Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
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451-467
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8
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4
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1
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726230
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An essential role for tomato s ...
Solanum lycopersicum
Plant Physiol.
161
148-164
2013
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1
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2
2
2
2
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720497
Meyer
Sulfoquinovose synthase - an i ...
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius MW001
Mol. Microbiol.
82
1150-1163
2011
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1
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1
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6
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2
2
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723680
Shimojima
Biosynthesis and functions of ...
Arabidopsis thaliana, Chlamydomonas reinhardtii, Rhodobacter sphaeroides, Spinacia oleracea
Prog. Lipid Res.
50
234-239
2011
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1
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3
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1
4
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8
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7
7
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695786
Calzada
Analysis of dibenzothiophene d ...
Pseudomonas putida, Pseudomonas putida CECT 5279
Appl. Environ. Microbiol.
75
875-877
2009
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2
1
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695760
Li
Genetic rearrangement strategy ...
Rhodococcus erythropolis
Appl. Environ. Microbiol.
74
971-976
2008
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2
1
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649481
Shimojima
Native uridine 5'-diphosphate- ...
Spinacia oleracea
Arch. Biochem. Biophys.
413
123-130
2003
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1
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1
1
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1
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3
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2
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668388
Sato
Identification of a gene for U ...
Chlamydomonas reinhardtii
DNA Res.
10
229-237
2003
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1
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393361
Sanda
Recombinant Arabidopsis SQD1 c ...
Arabidopsis sp., Arabidopsis thaliana
J. Biol. Chem.
276
3941-3946
2001
1
1
1
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3
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393362
Mulichak
Crystal structure of SQD1, an ...
Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
96
13097-13102
1999
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1
1
1
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3
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1
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393364
Essigmann
Prediction of the active-site ...
Arabidopsis thaliana
Arch. Biochem. Biophys.
369
30-41
1999
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2
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393363
Essigmann
Phosphate availability affects ...
Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
95
1950-1955
1998
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1
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3
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