BRENDA - Enzyme Database
show all sequences of 1.8.2.6

Structural basis for the oxidation of protein-bound sulfur by the sulfur cycle molybdohemo-enzyme sulfane dehydrogenase SoxCD

Zander, U.; Faust, A.; Klink, B.U.; de Sanctis, D.; Panjikar, S.; Quentmeier, A.; Bardischewsky, F.; Friedrich, C.G.; Scheidig, A.J.; J. Biol. Chem. 286, 8349-8360 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Paracoccus pantotrophus
Crystallization (Commentary)
Crystallization
Organism
crystal structure of SoxCD1, solved at 1.33 A . SoxCD1 misses the heme-2 domain D2 and is catalytically as active as SoxCD.The substrate of SoxCD is the outer (sulfane) sulfur of Cys-110-persulfide located at the C-terminal peptide swinging arm of SoxY of the SoxYZ carrier complex. The oxidation reactions of the sulfane-sulfur are initiated by the nucleophilic attack of the persulfide anion on the molybdenum atom that is, in turn, reduced. The close proximity of heme-1 to the molybdopterin allows easy acceptance of the electrons
Paracoccus pantotrophus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Molybdenum
sulfite oxidase-type molybdenum cofactor in subunit SoxC, residue Arg114 involved in the first oxidation step is in close proximity to the molybdenum atiom
Paracoccus pantotrophus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Paracoccus pantotrophus
-
-
-
Subunits
Subunits
Commentary
Organism
heterotetramer
structure resembles a tight alpha2beta-complex with internal 2-fold symmetry, crystallization data
Paracoccus pantotrophus
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Paracoccus pantotrophus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure of SoxCD1, solved at 1.33 A . SoxCD1 misses the heme-2 domain D2 and is catalytically as active as SoxCD.The substrate of SoxCD is the outer (sulfane) sulfur of Cys-110-persulfide located at the C-terminal peptide swinging arm of SoxY of the SoxYZ carrier complex. The oxidation reactions of the sulfane-sulfur are initiated by the nucleophilic attack of the persulfide anion on the molybdenum atom that is, in turn, reduced. The close proximity of heme-1 to the molybdopterin allows easy acceptance of the electrons
Paracoccus pantotrophus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Molybdenum
sulfite oxidase-type molybdenum cofactor in subunit SoxC, residue Arg114 involved in the first oxidation step is in close proximity to the molybdenum atiom
Paracoccus pantotrophus
Subunits (protein specific)
Subunits
Commentary
Organism
heterotetramer
structure resembles a tight alpha2beta-complex with internal 2-fold symmetry, crystallization data
Paracoccus pantotrophus
Other publictions for EC 1.8.2.6
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)
745125
Ray
Insight into the conformation ...
Dechloromonas aromatica
Interdiscip. Sci.
9
309-321
2017
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745711
Ramadhani
Recombinant sox enzymes from ...
Paracoccus pantotrophus, Paracoccus pantotrophus GB17
Microbes Environ.
32
54-60
2017
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1
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11
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745066
Drew
Spectroscopic characterizatio ...
Paracoccus pantotrophus
Inorg. Chem.
50
409-411
2011
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745285
Zander
Structural basis for the oxid ...
Paracoccus pantotrophus
J. Biol. Chem.
286
8349-8360
2011
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744213
Bagchi
Structural insight into SoxC ...
Paracoccus pantotrophus
Biochem. Biophys. Res. Commun.
331
1107-1113
2005
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744303
Bardischewsky
Sulfur dehydrogenase of Parac ...
Paracoccus pantotrophus
Biochemistry
44
7024-7034
2005
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744086
Friedrich
Oxidation of reduced inorgani ...
Paracoccus pantotrophus
Appl. Environ. Microbiol.
67
2873-2882
2001
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745201
Rother
Novel genes of the sox gene c ...
Paracoccus pantotrophus, Paracoccus pantotrophus GB17
J. Bacteriol.
183
4499-4508
2001
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10
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