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 (Natural Substrates Products
Natural Substrates Products on EC 4.4.1.15 - D-cysteine desulfhydrase
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NATURAL SUBSTRATE 
NATURAL 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
D-cysteine + H2O
sulfide + NH3 + pyruvate
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plant sulfur metabolism
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?
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
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?
D-cysteine + H2O
sulfide + NH3 + pyruvate
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plant sulfur metabolism
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?
D-cysteine + H2O
sulfide + NH3 + pyruvate
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-
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?
D-cysteine + H2O
sulfide + NH3 + pyruvate
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-
more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
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plant sulfur metabolism
additional product suggested, more sulfide than pyruvate and ammonium formed
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
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additional product suggested, more sulfide than pyruvate and ammonium formed
?
additional information
?
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extracellular production of hydrogen selenide accounts for thiol-assisted toxicity of selenite against Saccharomyces cerevisiae
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?
additional information
?
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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
?
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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
?
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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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?
