Information on EC 4.4.1.28 - L-cysteine desulfidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
4.4.1.28
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RECOMMENDED NAME
GeneOntology No.
L-cysteine desulfidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-aminoprop-2-enoate = 2-iminopropanoate
show the reaction diagram
2-iminopropanoate + H2O = pyruvate + NH3
show the reaction diagram
L-cysteine + H2O = sulfide + NH3 + pyruvate
show the reaction diagram
L-cysteine = 2-aminoprop-2-enoate + sulfide
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Cysteine and methionine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-cysteine sulfide-lyase (deaminating; pyruvate-forming)
The enzyme from the archaeon Methanocaldococcus jannaschii contains a [4Fe-4S] cluster and is specific for L-cysteine (cf. EC 4.4.1.1, cystathionine gamma-lyase). It cleaves a carbon-sulfur bond releasing sulfide and the unstable enamine product 2-aminoprop-2-enoate that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The same reaction can also be catalysed by some pyridoxal-phosphate proteins (cf. EC 4.4.1.1, cystathionine gamma-lyase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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H7C6D3
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-chloro-L-alanine + H2O
sulfide + ?
show the reaction diagram
-
-
-
-
?
cystathionine + H2O
NH3 + pyruvate + homocysteine
show the reaction diagram
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
L-cysteine methyl ester + H2O
sulfide + ?
show the reaction diagram
-
-
-
-
?
S-aminoethyl-L-cysteine + H2O
NH3 + pyruvate + cysteamine
show the reaction diagram
-
-
-
-
?
S-ethyl-L-cysteine + H2O
sulfide + ?
show the reaction diagram
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-
-
-
?
S-methyl-L-cysteine + H2O
sulfide + ?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
the air-inactivated enzyme is activated by reaction with Fe2+ and dithiothreitol in the absence of air
Iron-sulfur cluster
the air-inactivated enzyme contains 3 mol of iron per subunit
ZnCl2
1 mM, completely inhibits
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cyanoborohydride
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complete inactivation
dithiothreitol
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0.5 mM
EDTA
7.1 mM, 70% inhibition
glycine
hydroxylamine
iodoacetamide
0.42 mM, half-life: 12 min. 17 mM, preincubation completely abolishes activity
L-alanine
L-asparagine
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less effective inhibitor, Ki-value above 150 mM
L-methionine
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less effective inhibitor, Ki-value above 150 mM
L-serine
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L-threonine
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less effective inhibitor, Ki-value above 150 mM
L-tryptophan
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competitive inhibitor
L-valine
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less effective inhibitor, Ki-value above 150 mM
N-ethylmaleimide
0.42 mM, half-life: 8 min
additional information
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not inhibited by Nalpha-p-tosyl-L-lysine chloromethyl ketone, pronase, proteinase K, CaCl2, MgCl2, ZnCl2, PMSF or benzamidine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
0.5 mM, enhances activity
dithiothreitol
the air-inactivated enzyme is activated by reaction with Fe2+ and dithiothreitol in the absence of air
methyl viologen
4 mM, 40% stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36
beta-chloro-L-alanine
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pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
0.1 - 3.4
L-cysteine
62
L-cysteine methyl ester
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pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
0.28
S-ethyl-L-cysteine
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pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
1.26
S-methyl-L-cysteine
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pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.5
beta-chloro-L-alanine
Treponema denticola
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pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
5.5 - 39.6
L-cysteine
32
L-cysteine methyl ester
Treponema denticola
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pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
9.5
S-ethyl-L-cysteine
Treponema denticola
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pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
5.95
S-methyl-L-cysteine
Treponema denticola
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pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.2
L-cysteine
Methanocaldococcus jannaschii
Q58431
65°C, pH 6.6, wild-type enzyme
74
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.4
glycine
-
pH 7.4, 22°C
22
L-alanine
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pH 7.4, 22°C
15
L-serine
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pH 7.4, 22°C
12
L-tryptophan
-
pH and temperature not specified in the publication, in absence of Brij 35
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.066
pH 9.0, 37°C, purified enzyme
0.22
65°C, pH 6.6, mutant enzyme C25A
2.8
65°C, pH 6.6, mutant enzyme C282A
4.2
pH 7.0, 37°C
6.5
65°C, pH 6.6, mutant enzyme C322S
6.8
65°C, pH 6.6, mutant enzyme C329S
30
65°C, pH 6.6, mutant enzyme D323N
49
65°C, pH 6.6, mutant enzyme H139N
55.8
65°C, pH 6.6, wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
activities at pH 6.5 and 8.5 are less than 20% of that observed at pH 7.6
8 - 9.5
pH 8.0: about 30% of maximal activity, pH 9.5: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
from seedling
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
x * 33000, SDS-PAGE, enzyme purified from Fusobacterium nucleatum
33400
x * 33400, calculated from sequence
34500
x * 34500, calculated from sequence
35000
x * 35000, SDS-PAGE
37000
x * 37000, SDS-PAGE, recombinant His6-tagged fusion protein
43000
3 * 43000, SDS-PAGE
44000
x * 44000, SDS-PAGE
46000
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x * 46000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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significant decrease in enzymatic activity above 50°C
70
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30 min, complete inactivation
90
10 min, 22% loss of activity, mutant enzyme C278A; 10 min, 65% loss of activity, mutant enzyme C318S; 10 min, 80% loss of activity, mutant enzyme C325S; 10 min, no loss of activity, wild-type enzyme
100
10 min, 80% loss of activity, wild-type enzyme
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is completely lost by incubating the native protein solution in air for 15 min prior to the incubation
726942
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme purified form Fusobacterium nucleatum cell extract and from recombinant Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression as a His-tagged fusion protein in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli as a His6-tagged fusion protein
overexpressed in Escherichia coli LC-67
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
abscisic acid and gibberellic acid moderately induce the expression of the enzyme (BnDES1), and the maximal inducible time points are 24 h and 48 h, separately. Kinetin and indole-3-acetic acid induce the BnDES1 transcripts, with the same time point of 12 h for the maximal induction. BnDES1 transcripts are gradually up-regulated during 24 h or 12 h treatment periods by sodium nitroprusside or salicylic acid, and then fall back or keep the higher level until 48 h, respectively. The addition of paraquat brings about the rapid and moderated induction of BnDES1 during 3 h treatment period. BnDES1 transcript is induced sharply by the NaHS and L-cysteine treatments, both with maximum induction at 12 h following treatments
BnDES1 expression is significantly down-regulated by cadmium
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C25A
mutation reduces the catalytic efficiency and thermal stability of the enzyme
C282A
mutation reduces the catalytic efficiency and thermal stability of the enzyme
C322S
mutation reduces the catalytic efficiency and thermal stability of the enzyme
C329S
mutation reduces the catalytic efficiency and thermal stability of the enzyme
C332A/C329A
complete loss of activity
D323N
about 45% loss of specific activity
H139N
about 10% loss of specific activity
C25A
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mutation reduces the catalytic efficiency and thermal stability of the enzyme
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C282A
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mutation reduces the catalytic efficiency and thermal stability of the enzyme
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C322S
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mutation reduces the catalytic efficiency and thermal stability of the enzyme
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C329S
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mutation reduces the catalytic efficiency and thermal stability of the enzyme
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C332A/C329A
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complete loss of activity
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D198N
mutation resuklts in complete disappearance of the L-cysteine desulfhydrase activity
K233N
mutation resuklts in complete disappearance of the L-cysteine desulfhydrase activity
R365G
mutant enzyme retains catalytic activity as well as the wild-type enzyme
Y118A
mutation resuklts in complete disappearance of the L-cysteine desulfhydrase activity
Y59A
mutation resuklts in complete disappearance of the L-cysteine desulfhydrase activity
D198N
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mutation resuklts in complete disappearance of the L-cysteine desulfhydrase activity
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K233N
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mutation resuklts in complete disappearance of the L-cysteine desulfhydrase activity
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R365G
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mutant enzyme retains catalytic activity as well as the wild-type enzyme
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Y118A
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mutation resuklts in complete disappearance of the L-cysteine desulfhydrase activity
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Y59A
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mutation resuklts in complete disappearance of the L-cysteine desulfhydrase activity
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