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show all sequences of 1.13.11.72

Water-dependent reaction pathways: an essential factor for the catalysis in HEPD enzyme

Du, L.; Gao, J.; Liu, Y.; Liu, C.; J. Phys. Chem. B 116, 11837-11844 (2012)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces viridochromogenes
Q5IW40
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-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-hydroxyethylphosphonate + O2
catalytic cycle is based on concatenated bifurcations. The first bifurcation is based on the abstraction of hydrogen atoms from the substrate, which leads to a distal or proximal hydroperoxo species Fe-OOH or Fe-(OH)O. The second and the third bifurcations refer to the carbon-carbon bond cleavage reaction achieved through a tridentate intermediate, or employing a proton-shuttle assisted mechanism, in which the residue Glu176 or the FeIV O group serves as a general base. The reaction directions seem to be tunable and show significant environment dependence
720308
Streptomyces viridochromogenes
hydroxymethylphosphonate + formate
-
-
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?
2-hydroxyethylphosphonate + O2
in the reaction mechanism water molecules serve as an oxygen source in the generation of mononuclear nonheme iron oxo complexes, taking part in the catalytic cycle before the carbon-carbon bond cleavage process. After the dioxygen is bound to the iron center, the dioxygen-bound species Fe-O2 is generated. The abstraction of hydrogen atom from the substrate leads to a distal or proximal hydroperoxo species Fe(III)-OOH. This is the rate-limiting step, which has an energy barrier of 21 and 18 kcal/mol for distal and proximal H-abstraction processes, respectively. The second step is the cleavage of the O-O bond, and the carbon-carbon bond is broken subsequently. In this step, a tridentate binding species and a Fe(IV) sigmaO species are important intermediates to break the carbon-carbon bond. In the third step, the formic acid and the intermediate CH2PO2(OH)- radical are generated. Finally, 2-hydroxyethylphosphonate is converted to hydroxymethylphosphonate, and the formate or formic acid is formed
720308
Streptomyces viridochromogenes
hydroxymethylphosphonate + formate
-
-
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?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-hydroxyethylphosphonate + O2
catalytic cycle is based on concatenated bifurcations. The first bifurcation is based on the abstraction of hydrogen atoms from the substrate, which leads to a distal or proximal hydroperoxo species Fe-OOH or Fe-(OH)O. The second and the third bifurcations refer to the carbon-carbon bond cleavage reaction achieved through a tridentate intermediate, or employing a proton-shuttle assisted mechanism, in which the residue Glu176 or the FeIV O group serves as a general base. The reaction directions seem to be tunable and show significant environment dependence
720308
Streptomyces viridochromogenes
hydroxymethylphosphonate + formate
-
-
-
?
2-hydroxyethylphosphonate + O2
in the reaction mechanism water molecules serve as an oxygen source in the generation of mononuclear nonheme iron oxo complexes, taking part in the catalytic cycle before the carbon-carbon bond cleavage process. After the dioxygen is bound to the iron center, the dioxygen-bound species Fe-O2 is generated. The abstraction of hydrogen atom from the substrate leads to a distal or proximal hydroperoxo species Fe(III)-OOH. This is the rate-limiting step, which has an energy barrier of 21 and 18 kcal/mol for distal and proximal H-abstraction processes, respectively. The second step is the cleavage of the O-O bond, and the carbon-carbon bond is broken subsequently. In this step, a tridentate binding species and a Fe(IV) sigmaO species are important intermediates to break the carbon-carbon bond. In the third step, the formic acid and the intermediate CH2PO2(OH)- radical are generated. Finally, 2-hydroxyethylphosphonate is converted to hydroxymethylphosphonate, and the formate or formic acid is formed
720308
Streptomyces viridochromogenes
hydroxymethylphosphonate + formate
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-
-
?
Other publictions for EC 1.13.11.72
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)
745178
Peck
O-H activation by an unexpect ...
Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736
J. Am. Chem. Soc.
139
2045-2052
2017
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745390
Peck
Go it alone four-electron oxi ...
Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736
J. Biol. Inorg. Chem.
22
381-394
2017
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745162
Peck
A common late-stage intermedi ...
Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736
J. Am. Chem. Soc.
137
3217-3220
2015
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720308
Du
Water-dependent reaction pathw ...
Streptomyces viridochromogenes
J. Phys. Chem. B
116
11837-11844
2012
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718907
Peck
Mechanism and substrate recogn ...
Streptomyces viridochromogenes
Biochemistry
50
6598-6605
2011
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719655
Whitteck
On the stereochemistry of 2-hy ...
Streptomyces viridochromogenes
J. Am. Chem. Soc.
133
4236-4239
2011
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719648
Hirao
Ferric superoxide and ferric h ...
Streptomyces viridochromogenes
J. Am. Chem. Soc.
132
17901-17909
2010
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719645
Whitteck
Hydroperoxylation by hydroxyet ...
Streptomyces viridochromogenes
J. Am. Chem. Soc.
131
16225-16232
2009
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720539
Cicchillo
An unusual carbon-carbon bond ...
Streptomyces viridochromogenes
Nature
459
871-874
2009
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