4.4.1.15: D-cysteine desulfhydrase
This is an abbreviated version!
For detailed information about D-cysteine desulfhydrase, go to the full flat file.
Word Map on EC 4.4.1.15
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4.4.1.15
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h2s
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l-cysteine
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nahs
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hypotaurine
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1-aminocyclopropane-1-carboxylate
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betaine
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h2s-dependent
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hydrosulfide
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postharvest
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cd-induced
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gasotransmitter
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beta-replacement
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oas-tl
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o-acetylserine
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dehydrochlorinase
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cptio
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o-acetylserinethiollyase
- 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
Reaction
Synonyms
cysteine desulfhydrase, D-CDes, D-cysteine desulfhydrase, D-cysteine lyase, DCD, DCyD
ECTree
4.4.1.15 D-cysteine desulfhydraseAdvanced search results
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results (Substrates Products
Substrates Products on EC 4.4.1.15 - D-cysteine desulfhydrase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-carboxymethyl-D-cysteine + H2O
mercaptoacetic acid + pyruvate + NH3
-
-
-
-
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
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alpha,beta-elimination, more effective substrate than D-cysteine
-
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
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alpha,beta-elimination, more effective substrate than D-cysteine
-
-
?
3-chloro-D-alanine + H2O
pyruvate + NH3 + Cl-
Escherichia coli W3110 / ATCC 27325
-
alpha,beta-elimination, more effective substrate than D-cysteine
-
?
3-chloro-D-alanine + thioglycolic acid
S-carboxymethyl-D-cysteine
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i.e. mercaptoacetic acid, beta-replacement reaction
product is further metabolized to form pyruvate
?
3-chloro-D-alanine + thioglycolic acid
S-carboxymethyl-D-cysteine
Escherichia coli W3110 / ATCC 27325
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i.e. mercaptoacetic acid, beta-replacement reaction
product is further metabolized to form pyruvate
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
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plant sulfur metabolism
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
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alpha,beta-elimination
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
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physiological function unknown, detoxification of D-cysteine suggested, contributes to utilization of D-cysteine as sulfur source
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
Escherichia coli W3110 / ATCC 27325
-
alpha,beta-elimination
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
plant sulfur metabolism
-
?
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
-
-
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
-
-
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
-
-
?
O-acetyl-D-serine + H2O
?
Escherichia coli W3110 / ATCC 27325
-
alpha,beta-elimination reaction
-
-
?
O-acetyl-D-serine + sulfide
D-cysteine + ?
-
beta-replacement reaction
-
?
O-acetyl-D-serine + sulfide
D-cysteine + ?
Escherichia coli W3110 / ATCC 27325
-
beta-replacement reaction
-
?
additional information
?
-
-
extracellular production of hydrogen selenide accounts for thiol-assisted toxicity of selenite against Saccharomyces cerevisiae
-
-
?
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.
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-
?
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.
-
-
?
