BRENDA - Enzyme Database show
show all sequences of 4.4.1.15

The interconversion of ACC deaminase and D-cysteine desulfhydrase by diected mutagenesis

Todorovic, B.; Glick, B.R.; Planta 229, 193-205 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
cloning into the pET30a (+) vector at the EcoRV/HindIII sites, all single and double mutants are constructed using a Phusion Site Directed Mutagenesis Kit.
Pseudomonas putida
Expression of all recombinant proteins and mutants is carried out in Escherichia coli BL21. Altering of only two amino acid residues within the predicted active site served to change the enzyme from D-cysteine desulfhydrase to ACC deaminase.
Solanum lycopersicum
Engineering
Amino acid exchange
Commentary
Organism
E295S
By site-directed mutagenesis. The Pseudomonas putida UW4 single mutant is constructed using pET30a (+) with the full-length ACC deaminase as the template
Pseudomonas putida
E295S/L322T
The double mutant is constructed using the E295S mutant as the template.
Pseudomonas putida
S358E
By site-directed mutagenesis. The single mutants of the tomato enzyme are constructed using pET30 Xa/LIC with the full-length putative ACC deaminase as the template
Solanum lycopersicum
S358E/T386L
The double mutant is constructed using an additional round of mutagenesis and with the S358E single mutant as the template
Solanum lycopersicum
Inhibitors
Inhibitors
Commentary
Organism
Structure
aminooxyacetic acid
0.005-1 mM, enzymatic activity is progressively inhibited as the aminooxyacetic acid concentration is increased
Pseudomonas putida
aminooxyacetic acid
0.005-1 mM, enzymatic activity is progressively inhibited as the aminooxyacetic acid concentration is increased
Solanum lycopersicum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.21
-
D-cysteine
pH 8.0 at 37°C
Solanum lycopersicum
0.34
-
D-cysteine
double mutant Pseudomonas putida E295S/L322T
Pseudomonas putida
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
51480
-
recombinant protein is determined by mass spectrometry
Solanum lycopersicum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-cysteine + H2O
Pseudomonas putida
-
sulfide + NH3 + pyruvate
-
-
?
D-cysteine + H2O
Solanum lycopersicum
-
sulfide + NH3 + pyruvate
-
-
?
D-cysteine + H2O
Pseudomonas putida UW4
-
sulfide + NH3 + pyruvate
-
-
?
additional information
Solanum lycopersicum
Site-directed mutagenesis shows that altering only two amino acid residues within the predicted active site served to change the enzyme from D-cysteine desulfhydrase to 1-aminocyclopropane-1-carboxylate deaminase.
?
-
-
-
additional information
Pseudomonas putida
Site-directed mutagenesis shows that altering two amino acid residues at the same positions within the active site of tive site served to change the enzyme from D-cysteine desulfhydrase to deaminase from Pseudomonas putida UW4 the enzyme is converted into D-cysteine desulfhydrase.
?
-
-
-
additional information
Pseudomonas putida UW4
Site-directed mutagenesis shows that altering two amino acid residues at the same positions within the active site of tive site served to change the enzyme from D-cysteine desulfhydrase to deaminase from Pseudomonas putida UW4 the enzyme is converted into D-cysteine desulfhydrase.
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
-
-
Pseudomonas putida UW4
-
-
-
Solanum lycopersicum
B2MWN0
bony best variety
-
Purification (Commentary)
Commentary
Organism
Recombinant protein expressed with an N-terminal 6xHis-tag is purified under native/non-denaturing conditions using Ni-NTA Superflow resin.
Pseudomonas putida
The recombinant protein expressed with an N-terminal 6xHis-tag is purified under native/non-denaturing conditions using Ni-NTA Superflow resin
Solanum lycopersicum
Source Tissue
Source Tissue
Commentary
Organism
Textmining
fruit
collected at the breaker stage, which is defined as the stage where first spot of pink/red color appears at the blossom end
Solanum lycopersicum
-
leaf
collected at the mature green stage
Solanum lycopersicum
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
activity below detection, D-cysteine desulfhydrase activity in double mutant S358E/T386L; activity below detection, D-cysteine desulfhydrase activity in mutant S358E. Serine at 358 residue is essential for D-cysteine desulfhydrase activity.
Solanum lycopersicum
0.001594
-
D-cysteine desulfhydrase activity in WT
Pseudomonas putida
0.0356
-
D-cysteine desulfhydrase activity in mutant E295S
Pseudomonas putida
0.1475
-
D-cysteine desulfhydrase activity in double mutant E295S/L322T
Pseudomonas putida
0.6653
-
D-cysteine desulfhydrase activity in mutant T386L. Changing the threonine 386 residue alone reduces the activity of the enzyme substantially of about 11.5% of the native recombinant enzyme, although it does not cause complete loss of activity.
Solanum lycopersicum
5.784
-
D-cysteine desulfhydrase activity in wild-type
Solanum lycopersicum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-cysteine + H2O
-
694780
Pseudomonas putida
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
-
694780
Solanum lycopersicum
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
-
694780
Pseudomonas putida UW4
sulfide + NH3 + pyruvate
-
-
-
?
additional information
Site-directed mutagenesis shows that altering only two amino acid residues within the predicted active site served to change the enzyme from D-cysteine desulfhydrase to 1-aminocyclopropane-1-carboxylate deaminase.
694780
Solanum lycopersicum
?
-
-
-
-
additional information
Site-directed mutagenesis shows that altering two amino acid residues at the same positions within the active site of tive site served to change the enzyme from D-cysteine desulfhydrase to deaminase from Pseudomonas putida UW4 the enzyme is converted into D-cysteine desulfhydrase.
694780
Pseudomonas putida
?
-
-
-
-
additional information
Site-directed mutagenesis shows that altering two amino acid residues at the same positions within the active site of tive site served to change the enzyme from D-cysteine desulfhydrase to deaminase from Pseudomonas putida UW4 the enzyme is converted into D-cysteine desulfhydrase.
694780
Pseudomonas putida UW4
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Solanum lycopersicum
37
-
assay at
Pseudomonas putida
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
The enzyme is found to be very stable with almost 80% of its activity still remaining at 50°C
Solanum lycopersicum
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
654
-
D-cysteine
double mutant Pseudomonas putida E295S+L322T
Pseudomonas putida
13800
-
D-cysteine
-
Solanum lycopersicum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
with estimated 6.7 (pKa1) and 8.9 (pKa2)
Solanum lycopersicum
8
-
assay at
Pseudomonas putida
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0033
-
aminooxyacetic acid
value bases on non-linear regression
Solanum lycopersicum
Cloned(Commentary) (protein specific)
Commentary
Organism
cloning into the pET30a (+) vector at the EcoRV/HindIII sites, all single and double mutants are constructed using a Phusion Site Directed Mutagenesis Kit.
Pseudomonas putida
Expression of all recombinant proteins and mutants is carried out in Escherichia coli BL21. Altering of only two amino acid residues within the predicted active site served to change the enzyme from D-cysteine desulfhydrase to ACC deaminase.
Solanum lycopersicum
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E295S
By site-directed mutagenesis. The Pseudomonas putida UW4 single mutant is constructed using pET30a (+) with the full-length ACC deaminase as the template
Pseudomonas putida
E295S/L322T
The double mutant is constructed using the E295S mutant as the template.
Pseudomonas putida
S358E
By site-directed mutagenesis. The single mutants of the tomato enzyme are constructed using pET30 Xa/LIC with the full-length putative ACC deaminase as the template
Solanum lycopersicum
S358E/T386L
The double mutant is constructed using an additional round of mutagenesis and with the S358E single mutant as the template
Solanum lycopersicum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
aminooxyacetic acid
0.005-1 mM, enzymatic activity is progressively inhibited as the aminooxyacetic acid concentration is increased
Pseudomonas putida
aminooxyacetic acid
0.005-1 mM, enzymatic activity is progressively inhibited as the aminooxyacetic acid concentration is increased
Solanum lycopersicum
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0033
-
aminooxyacetic acid
value bases on non-linear regression
Solanum lycopersicum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.21
-
D-cysteine
pH 8.0 at 37°C
Solanum lycopersicum
0.34
-
D-cysteine
double mutant Pseudomonas putida E295S/L322T
Pseudomonas putida
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
51480
-
recombinant protein is determined by mass spectrometry
Solanum lycopersicum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-cysteine + H2O
Pseudomonas putida
-
sulfide + NH3 + pyruvate
-
-
?
D-cysteine + H2O
Solanum lycopersicum
-
sulfide + NH3 + pyruvate
-
-
?
D-cysteine + H2O
Pseudomonas putida UW4
-
sulfide + NH3 + pyruvate
-
-
?
additional information
Solanum lycopersicum
Site-directed mutagenesis shows that altering only two amino acid residues within the predicted active site served to change the enzyme from D-cysteine desulfhydrase to 1-aminocyclopropane-1-carboxylate deaminase.
?
-
-
-
additional information
Pseudomonas putida
Site-directed mutagenesis shows that altering two amino acid residues at the same positions within the active site of tive site served to change the enzyme from D-cysteine desulfhydrase to deaminase from Pseudomonas putida UW4 the enzyme is converted into D-cysteine desulfhydrase.
?
-
-
-
additional information
Pseudomonas putida UW4
Site-directed mutagenesis shows that altering two amino acid residues at the same positions within the active site of tive site served to change the enzyme from D-cysteine desulfhydrase to deaminase from Pseudomonas putida UW4 the enzyme is converted into D-cysteine desulfhydrase.
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
Recombinant protein expressed with an N-terminal 6xHis-tag is purified under native/non-denaturing conditions using Ni-NTA Superflow resin.
Pseudomonas putida
The recombinant protein expressed with an N-terminal 6xHis-tag is purified under native/non-denaturing conditions using Ni-NTA Superflow resin
Solanum lycopersicum
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
fruit
collected at the breaker stage, which is defined as the stage where first spot of pink/red color appears at the blossom end
Solanum lycopersicum
-
leaf
collected at the mature green stage
Solanum lycopersicum
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
activity below detection, D-cysteine desulfhydrase activity in double mutant S358E/T386L; activity below detection, D-cysteine desulfhydrase activity in mutant S358E. Serine at 358 residue is essential for D-cysteine desulfhydrase activity.
Solanum lycopersicum
0.001594
-
D-cysteine desulfhydrase activity in WT
Pseudomonas putida
0.0356
-
D-cysteine desulfhydrase activity in mutant E295S
Pseudomonas putida
0.1475
-
D-cysteine desulfhydrase activity in double mutant E295S/L322T
Pseudomonas putida
0.6653
-
D-cysteine desulfhydrase activity in mutant T386L. Changing the threonine 386 residue alone reduces the activity of the enzyme substantially of about 11.5% of the native recombinant enzyme, although it does not cause complete loss of activity.
Solanum lycopersicum
5.784
-
D-cysteine desulfhydrase activity in wild-type
Solanum lycopersicum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-cysteine + H2O
-
694780
Pseudomonas putida
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
-
694780
Solanum lycopersicum
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
-
694780
Pseudomonas putida UW4
sulfide + NH3 + pyruvate
-
-
-
?
additional information
Site-directed mutagenesis shows that altering only two amino acid residues within the predicted active site served to change the enzyme from D-cysteine desulfhydrase to 1-aminocyclopropane-1-carboxylate deaminase.
694780
Solanum lycopersicum
?
-
-
-
-
additional information
Site-directed mutagenesis shows that altering two amino acid residues at the same positions within the active site of tive site served to change the enzyme from D-cysteine desulfhydrase to deaminase from Pseudomonas putida UW4 the enzyme is converted into D-cysteine desulfhydrase.
694780
Pseudomonas putida
?
-
-
-
-
additional information
Site-directed mutagenesis shows that altering two amino acid residues at the same positions within the active site of tive site served to change the enzyme from D-cysteine desulfhydrase to deaminase from Pseudomonas putida UW4 the enzyme is converted into D-cysteine desulfhydrase.
694780
Pseudomonas putida UW4
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Solanum lycopersicum
37
-
assay at
Pseudomonas putida
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
The enzyme is found to be very stable with almost 80% of its activity still remaining at 50°C
Solanum lycopersicum
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
654
-
D-cysteine
double mutant Pseudomonas putida E295S+L322T
Pseudomonas putida
13800
-
D-cysteine
-
Solanum lycopersicum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
with estimated 6.7 (pKa1) and 8.9 (pKa2)
Solanum lycopersicum
8
-
assay at
Pseudomonas putida
Other publictions for EC 4.4.1.15
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)
746770
Ekimova
Distribution of 1-aminocyclop ...
Methylorubrum extorquens, Methylorubrum extorquens DSM 1338
Antonie van Leeuwenhoek
111
1723-1734
2018
-
-
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1
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1
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4
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4
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1
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1
1
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1
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1
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4
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1
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1
1
-
-
-
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1
1
748473
Li
-
Identification of wheat D-cys ...
Triticum aestivum
J. Plant Growth Regul.
37
1175-1184
2018
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1
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1
1
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-
730698
Bharath
Structural and mutational stud ...
Salmonella enterica subsp. enterica serovar Typhimurium
PLoS ONE
7
e36267
2012
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1
1
7
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1
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1
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3
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1
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3
1
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1
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1
1
7
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1
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1
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3
1
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2
2
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729125
Jin
Hydrogen sulfide improves drou ...
Arabidopsis thaliana, Arabidopsis thaliana Col-0
Biochem. Biophys. Res. Commun.
414
481-486
2011
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-
1
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7
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7
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1
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1
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7
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2
2
2
2
-
-
694780
Todorovic
The interconversion of ACC dea ...
Pseudomonas putida, Pseudomonas putida UW4, Solanum lycopersicum
Planta
229
193-205
2008
-
-
2
-
4
-
2
2
-
-
1
6
-
7
-
-
2
-
-
2
6
-
6
-
2
-
1
2
2
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1
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2
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4
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2
1
2
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1
6
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2
-
2
6
-
6
-
2
-
1
2
2
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-
680893
Tarze
Extracellular production of hy ...
Escherichia coli
J. Biol. Chem.
282
8759-8767
2007
1
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1
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3
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1
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1
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1
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3
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680123
Jain
Catalytic and regulatory prope ...
Synechococcus elongatus
Indian J. Exp. Biol.
44
767-772
2006
-
-
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1
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1
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1
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8
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1
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1
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1
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8
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1
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664881
Riemenschneider
Isolation and characterization ...
Arabidopsis thaliana
FEBS J.
272
1291-1304
2005
-
-
1
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1
2
1
1
-
5
1
-
4
-
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1
-
-
-
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3
1
-
1
-
1
1
-
-
1
-
2
2
-
-
1
1
-
-
1
2
2
-
1
1
-
5
1
-
-
-
1
-
-
-
-
3
1
-
1
-
1
1
-
-
2
-
-
-
-
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-
648739
Soutourina
Role of D-cysteine desulfhydra ...
Escherichia coli
J. Biol. Chem.
276
40864-40872
2001
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1
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2
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2
1
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3
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1
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4
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2
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1
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1
1
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2
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2
1
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1
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4
-
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-
2
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645577
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Partial purification and regul ...
Phormidium uncinatum, Phormidium uncinatum CU 1462/7
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1997
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648737
Schuetz
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Thiol accumulation and cystein ...
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1991
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34752
Nagasawa
Physiological comparison of D- ...
Escherichia coli, Escherichia coli W3110 / ATCC 27325, Pseudomonas putida, Pseudomonas putida CR 1-1
Arch. Microbiol.
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1988
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12
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648734
Schmidt
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D-cysteine desulfhydrase from ...
Spinacia oleracea
Methods Enzymol.
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1987
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4
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5
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648735
Rennenberg
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Cysteine desulphydrase activit ...
Cucurbita pepo, Nicotiana tabacum
Phytochemistry
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1987
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648731
Nagasawa
D-Cysteine desulfhydrase of Es ...
Citrobacter freundii, Enterobacter cloacae, Escherichia coli, Escherichia coli W3110 / ATCC 27325, Klebsiella pneumoniae
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1985
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29
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648733
Schmidt
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A cysteine desulfhydrase speci ...
Chlorella fusca
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1983
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648732
Schmidt
A cysteine desulfhydrase from ...
Spinacia oleracea
Z. Pflanzenphysiol.
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1982
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