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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
d-cysteine desulfhydrase, d-cdes,
more
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cysteine desulfhydrase
-
CD
cysteine desulfhydrase
-
CD
-
D-cysteine desulfhydrase
-
-
D-cysteine desulfhydrase
-
-
D-cysteine desulfhydrase
-
-
D-cysteine desulfhydrase
-
-
-
D-cysteine desulfhydrase
-
D-cysteine desulfhydrase
-
-
D-cysteine desulfhydrase
-
-
-
DCD
-
DCyD
-
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D-cysteine + H2O = sulfide + NH3 + pyruvate
-
-
-
-
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elimination of H2S or RSH
C-S-bond cleavage
-
-
-
-
elimination of H2S or RSH
-
-
-
-
elimination of H2S or RSH
-
-
elimination of H2S or RSH
-
-
-
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D-cysteine sulfide-lyase (deaminating; pyruvate-forming)
-
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3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
3-chloro-D-alanine + thioglycolic acid
S-carboxymethyl-D-cysteine
D-allocystathionine + H2O
?
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
D-cystine + H2O
?
-
-
-
-
?
DL-lanthionine + H2O
?
-
-
-
-
?
DL-selenocysteine + H2O
selenide + L-alanine
-
very poor substrate
-
-
?
DL-selenocystine + H2O
?
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
L-selenocystine + H2O
selenide + L-alanine
-
-
-
-
?
O-acetyl-D-serine + H2O
?
O-acetyl-D-serine + sulfide
D-cysteine + ?
O-methyl-DL-serine + H2O
?
-
poor substrate
-
-
?
S-benzyl-D-cysteine + H2O
benzyl hydrosulfide + pyruvate + NH3
-
-
-
-
?
S-carboxymethyl-D-cysteine + H2O
mercaptoacetic acid + pyruvate + NH3
-
-
-
-
?
S-ethyl-D-cysteine + H2O
ethanethiol + pyruvate + NH3
-
-
-
-
?
S-methyl-D-cysteine + H2O
methanethiol + pyruvate + NH3
-
-
-
-
?
S-n-butyl-D-cysteine + H2O
butane-1-thiol + pyruvate + NH3
-
-
-
-
?
S-n-propyl-D-cysteine + H2O
propane-1-thiol + pyruvate + NH3
-
-
-
-
?
S-phenyl-D-cysteine + H2O
benzenthiol + pyruvate + NH3
-
-
-
-
?
additional information
?
-
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
-
-
-
-
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
-
alpha,beta-elimination, more effective substrate than D-cysteine
-
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
-
alpha,beta-elimination, more effective substrate than D-cysteine
-
-
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
-
-
-
-
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
-
alpha,beta-elimination, more effective substrate than D-cysteine
-
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
-
-
-
-
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
-
-
-
-
?
3-chloro-D-alanine + thioglycolic acid
S-carboxymethyl-D-cysteine
-
i.e. mercaptoacetic acid, beta-replacement reaction
product is further metabolized to form pyruvate
?
3-chloro-D-alanine + thioglycolic acid
S-carboxymethyl-D-cysteine
-
i.e. mercaptoacetic acid, beta-replacement reaction
product is further metabolized to form pyruvate
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
37°C, pH 8.0
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
plant sulfur metabolism
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
alpha,beta-elimination
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
physiological function unknown, detoxification of D-cysteine suggested, contributes to utilization of D-cysteine as sulfur source
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
alpha,beta-elimination
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
plant sulfur metabolism
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
Ser78 and Gln77 are key determinants of enzyme specificity and the phenolate of Tyr287 is responsible for Calpha proton abstraction from D-Cys
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
very specific, no activity with L-cysteine, mercaptoacetic acid, mercaptoethanol, D-cystine, L-cystine, cysteamine, L-cysteine methylester and dithioerythritol
additional product suggested, more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
plant sulfur metabolism
additional product suggested, more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
additional product suggested, more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
very specific, only traces of activity with mercaptoacetic acid, mercaptoethanol, D-cystine, L-cystine, cysteamine, L-cysteine methylester
additional product suggested, more sulfide than pyruvate and ammonium formed
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
5% activity compared to D-cysteine
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
O-acetyl-D-serine + H2O
?
-
alpha,beta-elimination reaction
-
-
?
O-acetyl-D-serine + H2O
?
-
alpha,beta-elimination reaction
-
-
?
O-acetyl-D-serine + sulfide
D-cysteine + ?
-
beta-replacement reaction
-
?
O-acetyl-D-serine + sulfide
D-cysteine + ?
-
beta-replacement reaction
-
?
additional information
?
-
-
L-cysteine is not utilized
-
-
?
additional information
?
-
-
L-cysteine is not utilized
-
-
?
additional information
?
-
-
L-cysteine is not utilized
-
-
?
additional information
?
-
-
L-cysteine is not utilized
-
-
?
additional information
?
-
-
extracellular production of hydrogen selenide accounts for thiol-assisted toxicity of selenite against Saccharomyces cerevisiae
-
-
?
additional information
?
-
-
L-cysteine is not utilized
-
-
?
additional information
?
-
-
L-cysteine is not utilized
-
-
?
additional information
?
-
no substrate: L-cysteine, 1-aminocyclopropane-1-carboxylate
-
-
?
additional information
?
-
no substrate: L-cysteine, 1-aminocyclopropane-1-carboxylate
-
-
?
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.
-
-
?
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.
-
-
?
additional information
?
-
the enzyme is also active with beta-chloro-D-alanine which is converted to pyruvate, chloride, and NH3, EC 4.5.1.2. D-Ser is a poor substrate while the enzyme is inactive with respect to L-Ser and 1-amino-1-carboxy cyclopropane, substrate specificity and ligand binding structures, detailed overview. Ser78 and Gln77 are key determinants of enzyme specificity and the phenolate of Tyr287 is responsible for Calpha proton abstraction from D-Cys
-
-
?
additional information
?
-
-
the enzyme is also active with beta-chloro-D-alanine which is converted to pyruvate, chloride, and NH3, EC 4.5.1.2. D-Ser is a poor substrate while the enzyme is inactive with respect to L-Ser and 1-amino-1-carboxy cyclopropane, substrate specificity and ligand binding structures, detailed overview. Ser78 and Gln77 are key determinants of enzyme specificity and the phenolate of Tyr287 is responsible for Calpha proton abstraction from D-Cys
-
-
?
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.
-
-
?
additional information
?
-
-
L-cysteine is not utilized
-
-
?
additional information
?
-
-
L-cysteine is not utilized
-
-
?
additional information
?
-
-
L-cysteine is not utilized
-
-
?
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D-cysteine + H2O
sulfide + NH3 + pyruvate
additional information
?
-
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
plant sulfur metabolism
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
physiological function unknown, detoxification of D-cysteine suggested, contributes to utilization of D-cysteine as sulfur source
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
plant sulfur metabolism
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
plant sulfur metabolism
additional product suggested, more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
additional product suggested, more sulfide than pyruvate and ammonium formed
?
additional information
?
-
-
extracellular production of hydrogen selenide accounts for thiol-assisted toxicity of selenite against Saccharomyces cerevisiae
-
-
?
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.
-
-
?
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.
-
-
?
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.
-
-
?
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pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
2 mol per mol enzyme
pyridoxal 5'-phosphate
a fold type II pyridoxal 5'-phosphate-dependent enzyme
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(1-aminoethyl)phosphonic acid
-
-
aminooxy acetic acid
-
at 10 microM, IC50 value is 0.0305 mM
L-cysteine
-
mixed type inhibition
p-chloromercuribenzoate
-
-
additional information
-
no inhibition with EDTA and substrates
-
aminooxyacetic acid
-
-
aminooxyacetic acid
-
0.005-1 mM, enzymatic activity is progressively inhibited as the aminooxyacetic acid concentration is increased
aminooxyacetic acid
0.005-1 mM, enzymatic activity is progressively inhibited as the aminooxyacetic acid concentration is increased
Fe2+
-
-
hydroxylamine
-
at 10 microM, IC50 value is 0.0159 mM
NH4+
-
-
Ni2+
-
-
pyruvate
-
-
Zn2+
-
-
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dithiothreitol
-
-
dithiothreitol
-
probably by preventing autooxidation of substrate
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Dehydration
Hydrogen Sulfide-Mediated Activation of O-Acetylserine (Thiol) Lyase and l/d-Cysteine Desulfhydrase Enhance Dehydration Tolerance in Eruca sativa Mill.
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0.9 - 0.91
3-chloro-D-alanine
0.29
D-allocystathionine
-
30°C, pH 8.0
0.27
D-Cystine
-
30°C, pH 8.0
0.11
DL-lanthionine
-
30°C, pH 8.0, based on the concentration of the D-isomer, Escherichia coli
0.04
DL-selenocystine
-
30°C, pH 8.0, based on the concentration of the D-isomer, Escherichia coli
0.28
S-benzyl-D-cysteine
-
30°C, pH 8.0
0.83
S-carboxymethyl-D-cysteine
-
30°C, pH 8.0
0.42
S-ethyl-D-cysteine
-
30°C, pH 8.0
0.5
S-methyl-D-cysteine
-
30°C, pH 8.0
0.24
S-n-butyl-D-cysteine
-
30°C, pH 8.0
0.23
S-n-propyl-D-cysteine
-
30°C, pH 8.0
0.22
S-phenyl-D-cysteine
-
30°C, pH 8.0
0.9
3-chloro-D-alanine
-
37°C, pH 8.0
0.91
3-chloro-D-alanine
-
30°C, pH 8.0, alpha,beta-elimination
0.05
D-cysteine
-
-
0.14
D-cysteine
-
37°C, pH 9.0
0.15
D-cysteine
-
30°C, pH 8.0
0.16
D-cysteine
-
37°C, pH 9.0
0.21
D-cysteine
pH 8.0 at 37°C
0.25
D-cysteine
-
purified recombinant mature protein
0.3
D-cysteine
-
37°C, pH 8.0
0.34
D-cysteine
-
double mutant Pseudomonas putida E295S/L322T
0.34
D-cysteine
recombinant His6-tagged enzyme, pH and temperature not specified in the publication
0.46
D-cysteine
pH 7.4, 30°C
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281
3-chloro-D-alanine
-
37°C, pH 8.0
5.2
D-cysteine
pH 7.4, 30°C
72
D-cysteine
-
37°C, pH 8.0
654
D-cysteine
-
double mutant Pseudomonas putida E295S+L322T
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11.3
D-cysteine
pH 7.4, 30°C
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0.0033
aminooxyacetic acid
value bases on non-linear regression
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0.0305
aminooxy acetic acid
Arabidopsis thaliana
-
at 10 microM, IC50 value is 0.0305 mM
0.0159
hydroxylamine
Arabidopsis thaliana
-
at 10 microM, IC50 value is 0.0159 mM
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0.001594
-
D-cysteine desulfhydrase activity in WT
0.012
-
growth of the bacteria with methionine as sulfur source
0.0123
-
after partial purification
0.02
-
growth of the bacteria with MgSO4 and p-nitrophenlysulfate as sulfur source
0.022
-
growth of the bacteria with MgSO4 as sulfur source
0.03
-
growth of the bacteria with MgSO4 and Na2S2O3 as sulfur source
0.035
-
growth of the bacteria with reduced glutathione as sulfur source
0.0356
-
D-cysteine desulfhydrase activity in mutant E295S
0.1475
-
D-cysteine desulfhydrase activity in double mutant E295S/L322T
0.21
-
purified enzyme, 37°C, pH 9.0
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.
13
-
purified enzyme, 30°C, pH 8.0, with D-cysteine as substrate
5.784
D-cysteine desulfhydrase activity in wild-type
56.3
-
purified enzyme, 30°C, pH 8.0, with 3-chloro-D-alanine as substrate
0.01
-
purified enzyme, 37°C, pH 9.0
0.01
-
growth of the bacteria with p-nitrophenlysulfate as sulfur source
0.018
-
growth of the bacteria with L-cysteine as sulfur
0.018
-
growth of the bacteria with Na2S2O3 and p-nitrophenlysulfate as sulfur
0.018
-
growth of the bacteria with Na2S2O3 as sulfur source
additional information
activity below detection, D-cysteine desulfhydrase activity in double mutant S358E/T386L
additional information
activity below detection, D-cysteine desulfhydrase activity in mutant S358E. Serine at 358 residue is essential for D-cysteine desulfhydrase activity.
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7.6
with estimated 6.7 (pKa1) and 8.9 (pKa2)
8
-
-
8.5 - 9
-
-
9
-
alpha,beta-elimination
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7 - 11
-
-
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additional information
-
loss of activity at 50°C, no activity at 60°C. The enzyme is also very sensitive to freezing. One freeze-thaw cycle leads to a loss of activity of 75%.
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4.34
-
mature protein without N-terminal extension, calculated from amino acid sequence
7.2
-
calculated from amino acid sequence
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-
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
deltatrpED102/F'deltatrpED102
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
tobacco, var. Samsun
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
bony best variety
UniProt
brenda
-
-
-
brenda
strain PCC7942
-
-
brenda
strain PCC7942
-
-
brenda
-
-
-
brenda
green alga, strain 211-8b, formerly Chlorella pyrenoidosa strain 211-8b
-
-
brenda
-
UniProt
brenda
ecotype C24
-
-
brenda
-
-
-
brenda
cv. small sugar pumpkin
-
-
brenda
-
-
-
brenda
deltatrpED102/F'deltatrpED102
-
-
brenda
various strains
-
-
brenda
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high expression
brenda
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collected at the breaker stage, which is defined as the stage where first spot of pink/red color appears at the blossom end
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primary leaf
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collected at the mature green stage
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high expression
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high expression
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additional information
the enzyme expression levels gradually increase in an age-dependent manner, expression profiling, overview
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additional information
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the enzyme expression levels gradually increase in an age-dependent manner, expression profiling, overview
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additional information
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the enzyme expression levels gradually increase in an age-dependent manner, expression profiling, overview
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evolution
the enzyme structurally belongs to the fold type II pyridoxal 5'-phosphate-dependent enzyme family
metabolism
the two cysteine desulfhydrases, L-cysteine desulfhydrase and D-cysteine desulfhydrase, are mainly responsible for the degradation of cysteine in order to generate H2S, they show similar expression patterns in tissues
metabolism
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the two cysteine desulfhydrases, L-cysteine desulfhydrase and D-cysteine desulfhydrase, are mainly responsible for the degradation of cysteine in order to generate H2S, they show similar expression patterns in tissues
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physiological function
D-cysteine desulfhydrase is one of two enzymes mainly responsible for the degradation of cysteine in order to generate H2S, the most important is L-cysteine desulfhydrase, EC 4.4.1.1. Gene expression regulation relationship to drought tolerance in Arabidopsis thaliana, protective effect of H2S against drought, and H2S induces stomatal closure, overview
physiological function
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overexpression in Arabidopsis thaliana. Compared with wild-type plants, seed germination, root growth, and stomatal closure of the overexpressing plants are more sensitive to abscisic acid, resulting from upregulation of ABA-responsive genes such as PYR1, ABI1, ABI2, HAB1, HAB2, SnRK2, ABF2, and ABF4. Ooverexpressing plants do not show higher drought resistance than wild-type
physiological function
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D-cysteine desulfhydrase is one of two enzymes mainly responsible for the degradation of cysteine in order to generate H2S, the most important is L-cysteine desulfhydrase, EC 4.4.1.1. Gene expression regulation relationship to drought tolerance in Arabidopsis thaliana, protective effect of H2S against drought, and H2S induces stomatal closure, overview
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additional information
active site structure analysis and comparisons, residue Tr287 is important for catalysis, while His80 and Tyr261 may not be directly involved in the degradation of D-Cys, overview
additional information
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active site structure analysis and comparisons, residue Tr287 is important for catalysis, while His80 and Tyr261 may not be directly involved in the degradation of D-Cys, overview
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35000
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SDS-PAGE, gel filtration
35150
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calculated from amino acid sequence including N-terminal methionine
41700
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monomer, mature protein without N-terminal extension, calculated from amino acid sequence
42000
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x * 42000, SDS-PAGE, unprocessed protein
43000
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x * 43000, SDS-PAGE, mature protein
43900
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monomer, calculated from amino acid sequence
44000
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x * 44000, SDS-PAGE, post-translationally modified protein
51480
recombinant protein is determined by mass spectrometry
74000
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HPLC gel filtration
67000
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gel filtration
67000
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sedimentation equilibrium centrifugation
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?
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x * 42000, SDS-PAGE, unprocessed protein
?
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x * 43000, SDS-PAGE, mature protein
?
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x * 44000, SDS-PAGE, post-translationally modified protein
dimer
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2 * 36500, SDS-PAGE
dimer
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2 * 36500, SDS-PAGE
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additional information
the polypeptide fold of the enzyme consists of a small domain (residues 48161) and a large domain (residues 1-47 and 162-328)
additional information
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the polypeptide fold of the enzyme consists of a small domain (residues 48161) and a large domain (residues 1-47 and 162-328)
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purified enzyme in complex with D-Cys, beta-chloro-D-alanine, 1-amino-1-carboxy cyclopropane, D-Ser, L-Ser, D-cycloserine, and L-cycloserine, X-ray diffraction structure determination and analysis at 1.7-2.6 A resolution, modeling
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E295S
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By site-directed mutagenesis. The Pseudomonas putida UW4 single mutant is constructed using pET30a (+) with the full-length ACC deaminase as the template
E295S/L322T
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The double mutant is constructed using the E295S mutant as the template.
E295S
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By site-directed mutagenesis. The Pseudomonas putida UW4 single mutant is constructed using pET30a (+) with the full-length ACC deaminase as the template
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E295S/L322T
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The double mutant is constructed using the E295S mutant as the template.
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H80Q
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
Q77H
site-directed mutagenesis, the mutant is inactive with respect to D-Cys, but retains significant 30% activity with beta-chloro-D-alanine
S78A
site-directed mutagenesis, the mutant is inactive with respect to D-Cys, but retains significant 20% activity with beta-chloro-D-alanine
T288E
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
T315L/T288E
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
Y261F
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
Y287F
site-directed mutagenesis, inactive mutant with all substrates tested
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
S358E/T386L
The double mutant is constructed using an additional round of mutagenesis and with the S358E single mutant as the template
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50
The enzyme is found to be very stable with almost 80% of its activity still remaining at 50°C
60
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no loss of activity within 30 min incubation, 0.1 M phosphate buffer, pH 8.0
65
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11% loss of activity within 30 min incubation, 0.1 M phosphate buffer, pH 8.0
70
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24% loss of activity within 30 min incubation, 0.1 M phosphate buffer, pH 8.0
75
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40% loss of activity within 30 min incubation, 0.1 M phosphate buffer, pH 8.0
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glycerol, pyridoxal-5'-phosphate, dithiothreitol and EDTA do not increase the stability of the protein after freezing
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-20°C, 10 mM phosphate buffer, pH 7, 0.01 mM pyridoxal phosphate, 0.1 mM DTT, 0.1 mM EDTA 50% glycerol, at least 2 months, no loss of activity
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partial, does not bind to Blue-Sepharose affinity resin
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partially by Sephadex G-100 and DEAE column chromatography
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purified from Escherichia coli XL1-Blue cells harboring plasmid pKKyedO
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recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
Recombinant protein expressed with an N-terminal 6xHis-tag is purified under native/non-denaturing conditions using Ni-NTA Superflow resin.
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The recombinant protein expressed with an N-terminal 6xHis-tag is purified under native/non-denaturing conditions using Ni-NTA Superflow resin
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cloning into the pET30a (+) vector at the EcoRV/HindIII sites, all single and double mutants are constructed using a Phusion Site Directed Mutagenesis Kit.
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epression of His6-tagged enzyme in Escherichia coli
expression in Escherichia coli
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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.
overexpressed in host strain, enables Escherichia coli to utilize D-cysteine as sole sulfur source
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semi-quantitative reverse transcription-PCR analysis
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H2S fumigation stimulates the expression of drought associated genes. The enzyme is strongly induced by drought stress, with a maximum accumulation after 6 h, overview
the enzyme expression levels gradually increases in an age-dependent manner
H2S fumigation stimulates the expression of drought associated genes. The enzyme is strongly induced by drought stress, with a maximum accumulation after 6 h, overview
H2S fumigation stimulates the expression of drought associated genes. The enzyme is strongly induced by drought stress, with a maximum accumulation after 6 h, overview
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the enzyme expression levels gradually increases in an age-dependent manner
the enzyme expression levels gradually increases in an age-dependent manner
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Nagasawa, T.; Ishii, T.; Yamada, H.
Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1
Arch. Microbiol.
149
413-416
1988
Escherichia coli, Pseudomonas putida, Pseudomonas putida CR 1-1, Escherichia coli W3110 / ATCC 27325
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Bagchi, D.; Verma, D.
Partial purification and regulation of sulfur metabolizing enzymes in a cyanobacterium Phormidium uncinatum
Indian J. Exp. Biol.
35
876-880
1997
Phormidium uncinatum, Phormidium uncinatum CU 1462/7
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brenda
Nagasawa, T.; Ishii, T.; Kumagai, H.; Yamada, H.
D-Cysteine desulfhydrase of Escherichia coli. Purification and characterization
Eur. J. Biochem.
153
541-551
1985
Enterobacter cloacae, Citrobacter freundii, Escherichia coli, Klebsiella pneumoniae, Escherichia coli W3110 / ATCC 27325
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Schmidt, A.
A cysteine desulfhydrase from spinach leaves specific for D-cysteine
Z. Pflanzenphysiol.
107
295-300
1982
Spinacia oleracea
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Schmidt, A.; Erdle, I.
A cysteine desulfhydrase specific for D-cysteine from the green alga Chlorella fusca
Z. Naturforsch. C
38 c
428-435
1983
[Chlorella] fusca
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Schmidt, A.
D-cysteine desulfhydrase from spinach
Methods Enzymol.
143
449-453
1987
Spinacia oleracea
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brenda
Rennenberg, H.; Arabatzis, N.; Grundel, I.
Cysteine desulphydrase activity in higher plants: evidence for the action of L- and D-cysteine specific enzymes
Phytochemistry
26
1583-1589
1987
Cucurbita pepo, Nicotiana tabacum
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brenda
Schuetz, B.; De Kok, L.J.; Rennenberg, H.
Thiol accumulation and cysteine desulfhydrase activity in hydrogen sulfide-fumigated leaves and leaf homogenates of cucurbit plants
Plant Cell Physiol.
32
733-736
1991
Cucurbita pepo
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Soutourina, J.; Blanquet, S.; Plateau, P.
Role of D-cysteine desulfhydrase in the adaptation of Escherichia coli to D-cysteine
J. Biol. Chem.
276
40864-40872
2001
Escherichia coli
brenda
Riemenschneider, A.; Wegele, R.; Schmidt, A.; Papenbrock, J.
Isolation and characterization of a D-cysteine desulfhydrase protein from Arabidopsis thaliana
FEBS J.
272
1291-1304
2005
Arabidopsis thaliana
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Jain, A.; Verma, D.; Bagchi, D.
Catalytic and regulatory properties of sulphur metabolizing enzymes in cyanobacterium Synechococcus elongatus PCC 7942
Indian J. Exp. Biol.
44
767-772
2006
Synechococcus elongatus, Synechococcus elongatus PCC 7942
brenda
Tarze, A.; Dauplais, M.; Grigoras, I.; Lazard, M.; Ha-Duong, N.T.; Barbier, F.; Blanquet, S.; Plateau, P.
Extracellular production of hydrogen selenide accounts for thiol-assisted toxicity of selenite against Saccharomyces cerevisiae
J. Biol. Chem.
282
8759-8767
2007
Escherichia coli
brenda
Todorovic, B.; Glick, B.R.
The interconversion of ACC deaminase and D-cysteine desulfhydrase by diected mutagenesis
Planta
229
193-205
2008
Pseudomonas putida, Solanum lycopersicum (B2MWN0), Pseudomonas putida UW4
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Jin, Z.; Shen, J.; Qiao, Z.; Yang, G.; Wang, R.; Pei, Y.
Hydrogen sulfide improves drought resistance in Arabidopsis thaliana
Biochem. Biophys. Res. Commun.
414
481-486
2011
Arabidopsis thaliana (F4HYF3), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (F4HYF3)
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Bharath, S.R.; Bisht, S.; Harijan, R.K.; Savithri, H.S.; Murthy, M.R.
Structural and mutational studies on substrate specificity and catalysis of Salmonella typhimurium D-cysteine desulfhydrase
PLoS ONE
7
e36267
2012
Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZNT7), Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Ekimova, G.; Fedorov, D.; Tani, A.; Doronina, N.; Trotsenko, Y.
Distribution of 1-aminocyclopropane-1-carboxylate deaminase and d-cysteine desulfhydrase genes among type species of the genus Methylobacterium
Antonie van Leeuwenhoek
111
1723-1734
2018
Methylorubrum extorquens (C5AQP6), Methylorubrum extorquens DSM 1338 (C5AQP6)
brenda
Li, H.; Zhang, Y.; Li, X.; Xue, R.; Zhao, H.
Identification of wheat D-cysteine desulfhydrase (TaD-CDes) required for abscisic acid regulation of seed germination, root growth, and stomatal closure in Arabidopsis
J. Plant Growth Regul.
37
1175-1184
2018
Triticum aestivum
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