BRENDA - Enzyme Database
show all sequences of 1.14.99.58

The mechanism of heme transfer from the cytoplasmic heme binding protein PhuS to the delta-regioselective heme oxygenase of Pseudomonas aeruginosa

Bhakta, M.N.; Wilks, A.; Biochemistry 45, 11642-11649 (2006)

Data extracted from this reference:

Engineering
Protein Variants
Commentary
Organism
G125V
single-phase kinetics of transfer of heme from heme-binding protein PhuS
Pseudomonas aeruginosa
N19K/F117Y
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics
Pseudomonas aeruginosa
N19K/F117Y/K132A
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics
Pseudomonas aeruginosa
N19K/F117Y/K34N
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics
Pseudomonas aeruginosa
Organism
Organism
UniProt
Commentary
Textmining
Pseudomonas aeruginosa
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Posttranslational Modification
Posttranslational Modification
Commentary
Organism
additional information
heme transfer to the enzyme is independent of heme affinity and is mediated via a specific protein-protein interaction. A spin transition is involved during the transfer process with spin-state crossover occuring in the heme binding protein PhuS prior to the heme transfer step or alternatively occuring within the enzyme. Activation energies at pH 7.5 for the heme transfer from PhuS to enzyme are about 12-14 kcal per mol
Pseudomonas aeruginosa
Engineering (protein specific)
Protein Variants
Commentary
Organism
G125V
single-phase kinetics of transfer of heme from heme-binding protein PhuS
Pseudomonas aeruginosa
N19K/F117Y
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics
Pseudomonas aeruginosa
N19K/F117Y/K132A
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics
Pseudomonas aeruginosa
N19K/F117Y/K34N
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics
Pseudomonas aeruginosa
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
additional information
heme transfer to the enzyme is independent of heme affinity and is mediated via a specific protein-protein interaction. A spin transition is involved during the transfer process with spin-state crossover occuring in the heme binding protein PhuS prior to the heme transfer step or alternatively occuring within the enzyme. Activation energies at pH 7.5 for the heme transfer from PhuS to enzyme are about 12-14 kcal per mol
Pseudomonas aeruginosa
Other publictions for EC 1.14.99.58
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
Synonyms
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)
742894
Mourino
Metabolite-driven regulation ...
Pseudomonas aeruginosa
J. Biol. Chem.
291
20503-20515
2016
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726833
Gisk
Variable composition of heme o ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa KT 2240, Pseudomonas fluorescens, Pseudomonas fluorescens Pf-5, Pseudomonas mendocina, Pseudomonas mendocina YMP, Pseudomonas putida, Pseudomonas putida KT 2240, Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. tomato DC3000
Arch. Microbiol.
194
597-606
2012
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5
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30
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16
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9
10
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30
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48
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6
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3
6
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742839
Barker
Metabolic flux of extracellul ...
Pseudomonas aeruginosa
J. Biol. Chem.
287
18342-18350
2012
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1
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692400
Barkovits
Expression of the phytochrome ...
Pseudomonas aeruginosa
FEMS Microbiol. Lett.
80
160-168
2008
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680357
Rodríguez
The hydrogen-bonding network i ...
Pseudomonas aeruginosa
J. Am. Chem. Soc.
129
11730-11742
2007
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1
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681311
Furci
Inhibition of the bacterial he ...
Pseudomonas aeruginosa
J. Med. Chem.
50
3804-3813
2007
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13
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678146
Bhakta
The mechanism of heme transfer ...
Pseudomonas aeruginosa
Biochemistry
45
11642-11649
2006
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4
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678184
Rodríguez
Backbone NMR assignments and H ...
Pseudomonas aeruginosa
Biochemistry
45
4578-4592
2006
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659407
Wegele
The heme oxygenase(s)-phytochr ...
Pseudomonas aeruginosa
J. Biol. Chem.
279
45791-45802
2004
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742737
Fujii
Essential amino acid residues ...
Pseudomonas aeruginosa
J. Am. Chem. Soc.
126
4466-4467
2004
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8
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661923
Caignan
Oxidation of heme to beta- and ...
Pseudomonas aeruginosa
J. Am. Chem. Soc.
124
14879-14892
2002
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742771
Ratliff
Homologues of neisserial heme ...
Pseudomonas aeruginosa
J. Bacteriol.
183
6394-6403
2001
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