Any feedback?
No. of entries
Information on EC 4.4.1.15 - D-cysteine desulfhydrase
for references in articles please use BRENDA:EC4.4.1.15
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 4 Lyases
4.4 Carbon-sulfur lyases
4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)
4.4.1.15 D-cysteine desulfhydrase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 4.4.1.15
- h2s
- l-cysteine
- nahs
- hypotaurine
- 1-aminocyclopropane-1-carboxylate
- betaine
-
h2s-dependent
- hydrosulfide
-
postharvest
-
cd-induced
-
gasotransmitter
-
beta-replacement
- oas-tl
- o-acetylserine
- dehydrochlorinase
-
cptio
-
o-acetylserinethiollyase
showSynonyms
d-cysteine desulfhydrase, d-cdes, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cysteine desulfhydrase
D-cysteine desulfhydrase
D-cysteine lyase
-
-
-
-
DCD
DCyD
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-cysteine + H2O = sulfide + NH3 + pyruvate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-S-bond cleavage
elimination of H2S or RSH
C-S-bond cleavage
-
-
-
-
elimination of H2S or RSH
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
D-cysteine sulfide-lyase (deaminating; pyruvate-forming)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
84012-74-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DL-selenocysteine + H2O
selenide + L-alanine
-
Substrates: very poor substrate
Products: -
Products: -
?
S-benzyl-D-cysteine + H2O
benzyl hydrosulfide + pyruvate + NH3
-
Substrates: -
Products: -
Products: -
?
S-carboxymethyl-D-cysteine + H2O
mercaptoacetic acid + pyruvate + NH3
-
Substrates: -
Products: -
Products: -
?
S-ethyl-D-cysteine + H2O
ethanethiol + pyruvate + NH3
-
Substrates: -
Products: -
Products: -
?
S-methyl-D-cysteine + H2O
methanethiol + pyruvate + NH3
-
Substrates: -
Products: -
Products: -
?
S-n-butyl-D-cysteine + H2O
butane-1-thiol + pyruvate + NH3
-
Substrates: -
Products: -
Products: -
?
S-n-propyl-D-cysteine + H2O
propane-1-thiol + pyruvate + NH3
-
Substrates: -
Products: -
Products: -
?
S-phenyl-D-cysteine + H2O
benzenthiol + pyruvate + NH3
-
Substrates: -
Products: -
Products: -
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
-
Substrates: alpha,beta-elimination, more effective substrate than D-cysteine
Products: -
Products: -
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
Escherichia coli W3110 / ATCC 27325
-
Substrates: -
Products: -
Products: -
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
Escherichia coli W3110 / ATCC 27325
-
Substrates: alpha,beta-elimination, more effective substrate than D-cysteine
Products: -
Products: -
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
-
Substrates: -
Products: -
Products: -
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
-
Substrates: -
Products: -
Products: -
?
3-chloro-D-alanine + thioglycolic acid
S-carboxymethyl-D-cysteine
-
Substrates: i.e. mercaptoacetic acid, beta-replacement reaction
Products: product is further metabolized to form pyruvate
Products: product is further metabolized to form pyruvate
?
3-chloro-D-alanine + thioglycolic acid
S-carboxymethyl-D-cysteine
Escherichia coli W3110 / ATCC 27325
-
Substrates: i.e. mercaptoacetic acid, beta-replacement reaction
Products: product is further metabolized to form pyruvate
Products: product is further metabolized to form pyruvate
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: 37°C, pH 8.0
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: plant sulfur metabolism
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: alpha,beta-elimination
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: physiological function unknown, detoxification of D-cysteine suggested, contributes to utilization of D-cysteine as sulfur source
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
Escherichia coli W3110 / ATCC 27325
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
Escherichia coli W3110 / ATCC 27325
-
Substrates: alpha,beta-elimination
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: plant sulfur metabolism
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
Substrates: Ser78 and Gln77 are key determinants of enzyme specificity and the phenolate of Tyr287 is responsible for Calpha proton abstraction from D-Cys
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: more sulfide than pyruvate and ammonium formed
Products: more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: very specific, no activity with L-cysteine, mercaptoacetic acid, mercaptoethanol, D-cystine, L-cystine, cysteamine, L-cysteine methylester and dithioerythritol
Products: additional product suggested
Products: additional product suggested
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: very specific, no activity with L-cysteine, mercaptoacetic acid, mercaptoethanol, D-cystine, L-cystine, cysteamine, L-cysteine methylester and dithioerythritol
Products: more sulfide than pyruvate and ammonium formed
Products: more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: plant sulfur metabolism
Products: additional product suggested
Products: additional product suggested
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: plant sulfur metabolism
Products: more sulfide than pyruvate and ammonium formed
Products: more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: additional product suggested
Products: additional product suggested
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: more sulfide than pyruvate and ammonium formed
Products: more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: very specific, only traces of activity with mercaptoacetic acid, mercaptoethanol, D-cystine, L-cystine, cysteamine, L-cysteine methylester
Products: additional product suggested
Products: additional product suggested
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: very specific, only traces of activity with mercaptoacetic acid, mercaptoethanol, D-cystine, L-cystine, cysteamine, L-cysteine methylester
Products: more sulfide than pyruvate and ammonium formed
Products: more sulfide than pyruvate and ammonium formed
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: 5% activity compared to D-cysteine
Products: -
Products: -
?
O-acetyl-D-serine + H2O
?
-
Substrates: alpha,beta-elimination reaction
Products: -
Products: -
?
O-acetyl-D-serine + H2O
?
Escherichia coli W3110 / ATCC 27325
-
Substrates: alpha,beta-elimination reaction
Products: -
Products: -
?
O-acetyl-D-serine + sulfide
D-cysteine + ?
-
Substrates: beta-replacement reaction
Products: -
Products: -
?
O-acetyl-D-serine + sulfide
D-cysteine + ?
Escherichia coli W3110 / ATCC 27325
-
Substrates: beta-replacement reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-cysteine is not utilized
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-cysteine is not utilized
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-cysteine is not utilized
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-cysteine is not utilized
Products: -
Products: -
?
additional information
?
-
-
Substrates: extracellular production of hydrogen selenide accounts for thiol-assisted toxicity of selenite against Saccharomyces cerevisiae
Products: -
Products: -
?
additional information
?
-
Escherichia coli W3110 / ATCC 27325
-
Substrates: L-cysteine is not utilized
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-cysteine is not utilized
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: L-cysteine, 1-aminocyclopropane-1-carboxylate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: L-cysteine, 1-aminocyclopropane-1-carboxylate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-cysteine is not utilized
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-cysteine is not utilized
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-cysteine is not utilized
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: plant sulfur metabolism
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: physiological function unknown, detoxification of D-cysteine suggested, contributes to utilization of D-cysteine as sulfur source
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
Escherichia coli W3110 / ATCC 27325
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: plant sulfur metabolism
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
Substrates: -
Products: -
Products: -
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: more sulfide than pyruvate and ammonium formed
Products: more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: plant sulfur metabolism
Products: additional product suggested
Products: additional product suggested
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: plant sulfur metabolism
Products: more sulfide than pyruvate and ammonium formed
Products: more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: additional product suggested
Products: additional product suggested
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
Substrates: -
Products: more sulfide than pyruvate and ammonium formed
Products: more sulfide than pyruvate and ammonium formed
?
additional information
?
-
-
Substrates: extracellular production of hydrogen selenide accounts for thiol-assisted toxicity of selenite against Saccharomyces cerevisiae
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
Substrates: 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.
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
a fold type II pyridoxal 5'-phosphate-dependent enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Hydrogen Sulfide-Mediated Activation of O-Acetylserine (Thiol) Lyase and l/d-Cysteine Desulfhydrase Enhance Dehydration Tolerance in Eruca sativa Mill.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.34
D-cysteine
recombinant His6-tagged enzyme, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
0.018
0.02
-
growth of the bacteria with MgSO4 and p-nitrophenlysulfate 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
0.6653
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.
additional information
0.01
-
growth of the bacteria with p-nitrophenlysulfate as sulfur source
0.018
-
growth of the bacteria with Na2S2O3 and p-nitrophenlysulfate as sulfur
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5 - 9
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE