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show all sequences of 1.13.11.50

Insight of the iron binding and transport in Dke1 - A molecular dynamics study

Brkic, H.; Croat. Chem. Acta 88, 297-306 (2015)
No PubMed abstract available

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
molecular dynamic simulations with wild-type and mutants E88Q, R80A, Y70A of the Fe2+ free protein, of the enzyme with Fe2+ bound in the active site, without and with applying random force, and of the proteins with the metal ion located at the entrance of the water tunnel
Acinetobacter johnsonii
Engineering
Amino acid exchange
Commentary
Organism
E98Q
an interplay of residues Glu98, His104, Glu11 (from the neighbor subunit), and Arg80 is the most important for the Fe2+ transport in and out of the protein
Acinetobacter johnsonii
R80A
mutation causes relocation of Glu11 from neighbor subunit closer to His104, enabling formation of the Glu11(OE1/2)-His104(NE2H/CD2H) H-bond
Acinetobacter johnsonii
Y70A
an interplay of residues Glu98, His104, Glu11 (from the neighbor subunit), and Arg80 is the most important for the Fe2+ transport in and out of the protein
Acinetobacter johnsonii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
an interplay of residues Glu98, His104, Glu11 (from the neighbor subunit), and Arg80 is the most important for the Fe2+ transport in and out of the protein. The Fe2+ ion when expelled from the binding site can be trapped at different locations within the enzyme. The neighborhood of residue Glu11 (form the neighbor subunit) is the second most favorable binding site for the Fe2+ ion after the active site
Acinetobacter johnsonii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Acinetobacter johnsonii
Q8GNT2
-
-
Crystallization (Commentary) (protein specific)
Crystallization
Organism
molecular dynamic simulations with wild-type and mutants E88Q, R80A, Y70A of the Fe2+ free protein, of the enzyme with Fe2+ bound in the active site, without and with applying random force, and of the proteins with the metal ion located at the entrance of the water tunnel
Acinetobacter johnsonii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E98Q
an interplay of residues Glu98, His104, Glu11 (from the neighbor subunit), and Arg80 is the most important for the Fe2+ transport in and out of the protein
Acinetobacter johnsonii
R80A
mutation causes relocation of Glu11 from neighbor subunit closer to His104, enabling formation of the Glu11(OE1/2)-His104(NE2H/CD2H) H-bond
Acinetobacter johnsonii
Y70A
an interplay of residues Glu98, His104, Glu11 (from the neighbor subunit), and Arg80 is the most important for the Fe2+ transport in and out of the protein
Acinetobacter johnsonii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
an interplay of residues Glu98, His104, Glu11 (from the neighbor subunit), and Arg80 is the most important for the Fe2+ transport in and out of the protein. The Fe2+ ion when expelled from the binding site can be trapped at different locations within the enzyme. The neighborhood of residue Glu11 (form the neighbor subunit) is the second most favorable binding site for the Fe2+ ion after the active site
Acinetobacter johnsonii
Other publictions for EC 1.13.11.50
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)
742322
Brkic
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Insight of the iron binding a ...
Acinetobacter johnsonii
Croat. Chem. Acta
88
297-306
2015
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725553
Brkic
Dke1--structure, dynamics, and ...
Acinetobacter johnsonii
J. Biol. Inorg. Chem.
17
801-815
2012
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725198
Diebold
Spectroscopic and computationa ...
Acinetobacter johnsonii
J. Am. Chem. Soc.
133
15979-15991
2011
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711258
Diebold
The three-his triad in Dke1: c ...
Acinetobacter johnsonii
Biochemistry
49
6945-6952
2010
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711267
Straganz
Kinetic and CD/MCD spectroscop ...
Acinetobacter johnsonii
Biochemistry
49
996-1004
2010
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696107
Leitgeb
Biochemical characterization a ...
Acinetobacter johnsonii
Biochem. J.
418
403-411
2009
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675466
Straganz
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Exploring the cupin-type metal ...
Acinetobacter johnsonii
J. Mol. Catal. B
39
171-178
2006
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657614
Hofer
Fast determination of operatio ...
Acinetobacter johnsonii
Appl. Microbiol. Biotechnol.
1
1-12
2005
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657866
Grogan
Emergent mechanistic diversity ...
Acinetobacter johnsonii
Biochem. J.
388
721-730
2005
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671683
Straganz
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Integrated approach for produc ...
Acinetobacter johnsonii
Biocatal. Biotransform.
23
261-269
2005
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674150
Straganz
Reaction coordinate analysis f ...
Acinetobacter johnsonii
J. Am. Chem. Soc.
127
12306-12314
2005
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636327
Straganz
Acetylacetone-cleaving enzyme ...
Acinetobacter johnsonii
Biochem. J.
369
573-581
2003
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636328
Straganz
A novel beta-diketone-cleaving ...
Acinetobacter johnsonii
Biochem. Biophys. Res. Commun.
297
232-236
2002
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