BRENDA - Enzyme Database
show all sequences of 1.13.11.54

Characterization of metal binding in the active sites of acireductone dioxygenase isoforms from Klebsiella ATCC 8724

Chai, S.C.; Ju, T.; Dang, M.; Beaulieu Goldsmith, R.; Maroney, M.J.; Pochapsky, T.C.; Biochemistry 47, 2428-2438 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Klebsiella oxytoca
Engineering
Amino acid exchange
Commentary
Organism
D101A
about 60% of wild-type activity
Klebsiella oxytoca
E100A
about 2% of wild-type activity. E100 is not essential for metal binding
Klebsiella oxytoca
E102A
no catalytic activity
Klebsiella oxytoca
E95A
about 4% of wild-type activity
Klebsiella oxytoca
H140A
no catalytic activity
Klebsiella oxytoca
H140F
no catalytic activity
Klebsiella oxytoca
H96A
no catalytic activity
Klebsiella oxytoca
H98A
no catalytic activity
Klebsiella oxytoca
H98S
no catalytic activity. Mutant exhibits little affinity for either Ni2+ or Fe2+, indicating that His 98 is likely involved in binding both metals
Klebsiella oxytoca
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
ligands are H96, H98, E102 and H140, the same as in the isoform requiring Ni2+, EC 1.13.11.54. Structural and functional differences between FeARD' and NiARD' forms are triggered by subtle differences in the local backbone. Both enzymes bind their respective metals with pseudo-octahedral geometry and both may lose a His ligand upon binding of substrate under anaerobic conditions
Klebsiella oxytoca
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Klebsiella oxytoca
Q9ZFE7
-
-
Klebsiella oxytoca ATCC 8724
Q9ZFE7
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Klebsiella oxytoca
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D101A
about 60% of wild-type activity
Klebsiella oxytoca
E100A
about 2% of wild-type activity. E100 is not essential for metal binding
Klebsiella oxytoca
E102A
no catalytic activity
Klebsiella oxytoca
E95A
about 4% of wild-type activity
Klebsiella oxytoca
H140A
no catalytic activity
Klebsiella oxytoca
H140F
no catalytic activity
Klebsiella oxytoca
H96A
no catalytic activity
Klebsiella oxytoca
H98A
no catalytic activity
Klebsiella oxytoca
H98S
no catalytic activity. Mutant exhibits little affinity for either Ni2+ or Fe2+, indicating that His 98 is likely involved in binding both metals
Klebsiella oxytoca
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
ligands are H96, H98, E102 and H140, the same as in the isoform requiring Ni2+, EC 1.13.11.54. Structural and functional differences between FeARD' and NiARD' forms are triggered by subtle differences in the local backbone. Both enzymes bind their respective metals with pseudo-octahedral geometry and both may lose a His ligand upon binding of substrate under anaerobic conditions
Klebsiella oxytoca
Other publictions for EC 1.13.11.54
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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742270
Valdez
-
Co2+ acireductone dioxygenase ...
Klebsiella oxytoca
Chem. Phys. Lett.
604
77-82
2014
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725214
Allpress
Regioselective aliphatic carbo ...
Klebsiella oxytoca
J. Am. Chem. Soc.
135
659-668
2013
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725438
Friedman
Acireductone dioxygenase 1 (AR ...
Arabidopsis thaliana, Arabidopsis thaliana Columbia-0
J. Biol. Chem.
286
30107-30118
2011
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685212
Chai
Characterization of metal bind ...
Klebsiella oxytoca, Klebsiella oxytoca ATCC 8724
Biochemistry
47
2428-2438
2008
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675408
Ju
One protein, two enzymes revis ...
Mus musculus
J. Mol. Biol.
363
823-834
2006
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663098
Sauter
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Oryza sativa
Plant J.
44
718-729
2005
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673849
Hirano
Membrane-type 1 matrix metallo ...
Homo sapiens, Saccharomyces cerevisiae, Saccharomyces cerevisiae Y700
Genes Cells
10
565-574
2005
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661058
Dai
Mechanistic studies of two dio ...
Klebsiella pneumoniae
Biochemistry
40
6379-6387
2001
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662101
Dai
One protein, two enzymes ...
Klebsiella oxytoca
J. Biol. Chem.
274
1193-1195
1999
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