We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments 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).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
mj1025, l-cysteine desulfidase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
aecD
-
CFL1_01513
-
cystalysin
-
-
DES1
-
L-cysteine desulfhydrase
-
L-cysteine desulfhydrase
-
L-cysteine desulfhydrase
-
-
L-cysteine desulfhydrase
-
-
L-cysteine desulfhydrase
-
-
-
L-cysteine desulfhydrase
-
-
-
les
-
MJ1025
locus name
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-aminoprop-2-enoate = 2-iminopropanoate
2-iminopropanoate + H2O = pyruvate + NH3
L-cysteine + H2O = sulfide + NH3 + pyruvate
L-cysteine = 2-aminoprop-2-enoate + sulfide
2-aminoprop-2-enoate = 2-iminopropanoate
(1b), spontaneous
2-aminoprop-2-enoate = 2-iminopropanoate
(1b), spontaneous
-
-
2-aminoprop-2-enoate = 2-iminopropanoate
-
-
-
-
2-iminopropanoate + H2O = pyruvate + NH3
(1c), spontaneous
2-iminopropanoate + H2O = pyruvate + NH3
(1c), spontaneous
-
-
2-iminopropanoate + H2O = pyruvate + NH3
-
-
-
-
L-cysteine + H2O = sulfide + NH3 + pyruvate
overall reaction
L-cysteine + H2O = sulfide + NH3 + pyruvate
overall reaction
-
-
L-cysteine + H2O = sulfide + NH3 + pyruvate
-
-
-
-
L-cysteine = 2-aminoprop-2-enoate + sulfide
(1a)
L-cysteine = 2-aminoprop-2-enoate + sulfide
(1a)
-
-
L-cysteine = 2-aminoprop-2-enoate + sulfide
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
beta-chloro-L-alanine + H2O
sulfide + ?
-
-
-
-
?
cystathionine + H2O
NH3 + pyruvate + homocysteine
L-cystathionine + H2O
NH3 + pyruvate + homocysteine
L-cysteine + H2O
sulfide + NH3 + pyruvate
L-cysteine methyl ester + H2O
sulfide + ?
-
-
-
-
?
L-djenkolic acid
?
-
-
-
?
S-(2-methyl-4-oxopentan-2-yl)-L-cysteine + H2O
NH3 + pyruvate + 4-methyl-4-sulfanylpentan-2-one
-
-
-
?
S-aminoethyl-L-cysteine + H2O
NH3 + pyruvate + cysteamine
S-ethyl-L-cysteine + H2O
sulfide + ?
-
-
-
-
?
S-methyl-L-cysteine + H2O
sulfide + ?
-
-
-
-
?
additional information
?
-
cystathionine + H2O
NH3 + pyruvate + homocysteine
-
-
-
-
?
cystathionine + H2O
NH3 + pyruvate + homocysteine
-
-
-
-
?
cystathionine + H2O
NH3 + pyruvate + homocysteine
-
-
-
-
?
L-cystathionine + H2O
NH3 + pyruvate + homocysteine
-
-
-
?
L-cystathionine + H2O
NH3 + pyruvate + homocysteine
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
hydrogen sulfide generated by L-cysteine desulfhydrase acts upstream of nitric oxide to modulate abscisic acid-dependent stomatal closure
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
the enzyme plays an important role in L-cysteine degradation in Corynebacterium glutamicum cells
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
L-cysteine serves as a poor substrate
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
the enzyme plays an important role in L-cysteine degradation in Corynebacterium glutamicum cells
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
L-cysteine serves as a poor substrate
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
no activity with DLK-homocysteine, D-cysteine, L-cystine and cystathionine
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
possible involvement in iron-sulfur center biosynthesis
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
the enzyme is very specific for L-cysteine, with no activity being detected with D-cysteine, L-homocysteine, 3-mercaptopropionic acid (cysteine without the amino group), cysteamine (cysteine without the carboxylic acid), or mercaptolactate (the hydroxyl analogue of cysteine)
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
possible involvement in iron-sulfur center biosynthesis
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
the enzyme is very specific for L-cysteine, with no activity being detected with D-cysteine, L-homocysteine, 3-mercaptopropionic acid (cysteine without the amino group), cysteamine (cysteine without the carboxylic acid), or mercaptolactate (the hydroxyl analogue of cysteine)
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
DL-homocysteine, cysteinyl glycine, and glutathione are not substrates to produce hydrogen sulfide
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
DL-homocysteine, cysteinyl glycine, and glutathione are not substrates to produce hydrogen sulfide
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
the enzyme is responsible for in vivo cysteine catabolism by Treponema denticola
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
strong preference for L-cysteine over D-cysteine, H2S production is 483-fold slower with D-cysteine than with L-cysteine. It is far more active towards L-cysteine than towards the other standard amino acids that undergo pyridoxal phosphate-dependent beta-elimination reactions (serine, threonine, tryptophan and tyrosine). The enzyme tolerated small modifications to the carboxylate of L-cysteine (i.e., the methyl and ethyl esters of L-cysteine are good substrates), but the smallest possible peptide with an N-terminal cysteine, L-cysteinylglycine, is a very poor substrate
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cystine + H2O
?
-
-
-
?
L-cystine + H2O
?
-
-
-
?
S-aminoethyl-L-cysteine + H2O
NH3 + pyruvate + cysteamine
-
-
-
?
S-aminoethyl-L-cysteine + H2O
NH3 + pyruvate + cysteamine
-
-
-
?
S-aminoethyl-L-cysteine + H2O
NH3 + pyruvate + cysteamine
-
-
-
-
?
additional information
?
-
the enzyme shows a clear preference for aminoethyl-L-cysteine together with L-cystine and the non-protein amino acid L-djenkolate. Enzyme additionally acts as cysteine-S-conjugate beta-lyase in vitro, reaction of EC 4.4.1.13, and is able to cleave a cysteinylated substrate precursor into the corresponding thiol. Enzyme has no alpha,gamma-elimination activity towards L-methionine to produce methanethiol
-
-
?
additional information
?
-
the enzyme shows a clear preference for aminoethyl-L-cysteine together with L-cystine and the non-protein amino acid L-djenkolate. Enzyme additionally acts as cysteine-S-conjugate beta-lyase in vitro, reaction of EC 4.4.1.13, and is able to cleave a cysteinylated substrate precursor into the corresponding thiol. Enzyme has no alpha,gamma-elimination activity towards L-methionine to produce methanethiol
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-cysteine + H2O
sulfide + NH3 + pyruvate
L-cysteine + H2O
sulfide + NH3 + pyruvate
hydrogen sulfide generated by L-cysteine desulfhydrase acts upstream of nitric oxide to modulate abscisic acid-dependent stomatal closure
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
the enzyme plays an important role in L-cysteine degradation in Corynebacterium glutamicum cells
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
the enzyme plays an important role in L-cysteine degradation in Corynebacterium glutamicum cells
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
possible involvement in iron-sulfur center biosynthesis
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
possible involvement in iron-sulfur center biosynthesis
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
the enzyme is responsible for in vivo cysteine catabolism by Treponema denticola
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
required
pyridoxal 5'-phosphate
-
dependent on
additional information
both the isolated and recombinant enzymes are devoid of pyridoxal 5'-phosphate
-
additional information
-
both the isolated and recombinant enzymes are devoid of pyridoxal 5'-phosphate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cyanoborohydride
-
complete inactivation
EDTA
7.1 mM, 70% inhibition
iodoacetamide
0.42 mM, half-life: 12 min. 17 mM, preincubation completely abolishes activity
L-asparagine
-
less effective inhibitor, Ki-value above 150 mM
L-methionine
-
less effective inhibitor, Ki-value above 150 mM
L-threonine
-
less effective inhibitor, Ki-value above 150 mM
L-tryptophan
-
competitive inhibitor
L-valine
-
less effective inhibitor, Ki-value above 150 mM
N-ethylmaleimide
0.42 mM, half-life: 8 min
additional information
-
not inhibited by Nalpha-p-tosyl-L-lysine chloromethyl ketone, pronase, proteinase K, CaCl2, MgCl2, ZnCl2, PMSF or benzamidine
-
glycine
-
-
glycine
-
competitive inhibitor
hydroxylamine
34.5 mM, 12% inhibition
L-alanine
-
-
L-alanine
-
competitive inhibitor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
NH4Cl
-
levels of ammonium content and total enzyme activity are increased in a dose-dependent manner after NH4Cl treatment
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.36
beta-chloro-L-alanine
-
pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
4
L-cystathionine
pH 8.3, 30°C
62
L-cysteine methyl ester
-
pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
2.1
L-cystine
pH 8.3, 30°C
0.48
L-djenkolic acid
pH 8.3, 30°C
0.5
S-(2-methyl-4-oxopentan-2-yl)-L-cysteine
pH 8.3, 30°C
0.27
S-aminoethyl-L-cysteine
pH 8.3, 30°C
0.28
S-ethyl-L-cysteine
-
pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
1.26
S-methyl-L-cysteine
-
pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
0.1
L-cysteine
pH 9.0, 37°C
0.122
L-cysteine
pH 7.5, 37°C, recombinant enzyme purified from Escherichia coli
0.155
L-cysteine
pH 7.5, 37°C, enzyme purified from Fusobacterium nucleatum
0.4
L-cysteine
pH 8.3, 30°C
0.4
L-cysteine
-
pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
0.7
L-cysteine
pH 7.0, 37°C
1.78
L-cysteine
65°C, pH 6.6, wild-type enzyme
2.3
L-cysteine
-
pH and temperature not specified in the publication, in absence of Brij 35
3.4
L-cysteine
-
pH 7.4, 22°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
14.5
beta-chloro-L-alanine
-
pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
11
L-cystathionine
pH 8.3, 30°C
32
L-cysteine methyl ester
-
pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
29
L-cystine
pH 8.3, 30°C
19
L-djenkolic acid
pH 8.3, 30°C
4
S-(2-methyl-4-oxopentan-2-yl)-L-cysteine
pH 8.3, 30°C
17.8
S-aminoethyl-L-cysteine
pH 8.3, 30°C
9.5
S-ethyl-L-cysteine
-
pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
5.95
S-methyl-L-cysteine
-
pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
2.9
L-cysteine
pH 8.3, 30°C
5.5
L-cysteine
-
pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer
10.9
L-cysteine
-
pH and temperature not specified in the publication, in absence of Brij 35
12
L-cysteine
-
pH 7.4, 22°C
39.6
L-cysteine
65°C, pH 6.6, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3
L-cystathionine
pH 8.3, 30°C
14
L-cystine
pH 8.3, 30°C
40
L-djenkolic acid
pH 8.3, 30°C
8
S-(2-methyl-4-oxopentan-2-yl)-L-cysteine
pH 8.3, 30°C
66
S-aminoethyl-L-cysteine
pH 8.3, 30°C
7
L-cysteine
pH 8.3, 30°C
22.2
L-cysteine
65°C, pH 6.6, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.4
glycine
-
pH 7.4, 22°C
22
L-alanine
-
pH 7.4, 22°C
15
L-serine
-
pH 7.4, 22°C
12
L-tryptophan
-
pH and temperature not specified in the publication, in absence of Brij 35
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
6.5
65°C, pH 6.6, mutant enzyme C322S
6.8
65°C, pH 6.6, mutant enzyme C329S
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
37
assay at
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
SwissProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
SwissProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
SwissProt
brenda
-
SwissProt
brenda
-
-
-
brenda
Oryza sativa Wuyunjing 7
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
brenda
root
brenda
from seedling
brenda
-
-
brenda
Oryza sativa Wuyunjing 7
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
metabolism
the enzyme is closely associated with the pathogenesis of Prevotella intermedia
metabolism
-
the enzyme is responsible for in vivo cysteine catabolism by Treponema denticola. Unregulated enzyme, with the resulting H2S production being essential to the hemolytic activity
metabolism
the enzyme is responsible for the H2S production, and may play an important role in plant growth regulators and chemical stimuli responses
metabolism
the enzyme plays an important role in L-cysteine degradation in Corynebacterium glutamicum cells
metabolism
-
the enzyme plays an important role in L-cysteine degradation in Corynebacterium glutamicum cells
-
metabolism
-
the enzyme is closely associated with the pathogenesis of Prevotella intermedia
-
physiological function
possible involvement in iron-sulfur center biosynthesis
physiological function
hydrogen sulfide generated by L-cysteine desulfhydrase acts upstream of nitric oxide to modulate abscisic acid-dependent stomatal closure
physiological function
-
the enzyme could function in vivo as a virulence factor
physiological function
-
presence of NH4Cl triggers the induction of L-cysteine desulfhydrase-related H2S production in rice seedling roots. The activity of L-cysteine desulfidase, as well as the enzymes involved in nitrogen metabolism, is significantly increased in the photoperiod sensitivity SE5-overexpression line, whereas it impaired in the SE5-knockdown mutant
physiological function
-
possible involvement in iron-sulfur center biosynthesis
-
physiological function
-
the enzyme could function in vivo as a virulence factor
-
physiological function
-
the enzyme could function in vivo as a virulence factor
-
physiological function
Oryza sativa Wuyunjing 7
-
presence of NH4Cl triggers the induction of L-cysteine desulfhydrase-related H2S production in rice seedling roots. The activity of L-cysteine desulfidase, as well as the enzymes involved in nitrogen metabolism, is significantly increased in the photoperiod sensitivity SE5-overexpression line, whereas it impaired in the SE5-knockdown mutant
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MEGL_FUSNN
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355)
395
0
43306
Swiss-Prot
-
CYDE_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
388
0
42645
Swiss-Prot
-
CYDE_METM5
Methanococcus maripaludis (strain C5 / ATCC BAA-1333)
397
0
43604
Swiss-Prot
-
CYDE_METM6
Methanococcus maripaludis (strain C6 / ATCC BAA-1332)
396
0
43171
Swiss-Prot
-
CYDE_METM7
Methanococcus maripaludis (strain C7 / ATCC BAA-1331)
397
0
43732
Swiss-Prot
-
CYDE_METMP
Methanococcus maripaludis (strain S2 / LL)
396
0
43545
Swiss-Prot
-
METC_ECOLI
Escherichia coli (strain K12)
395
0
43212
Swiss-Prot
-
LCYD1_ARATH
454
0
50692
Swiss-Prot
other Location (Reliability: 3 )
LCYD1_ORYSJ
482
0
52121
Swiss-Prot
other Location (Reliability: 4 )
LCYD2_ORYSJ
479
0
51237
Swiss-Prot
other Location (Reliability: 2 )
D3S649_METSF
Methanocaldococcus sp. (strain FS406-22)
388
0
42562
TrEMBL
-
A0A7J9P3Y1_METMI
397
0
43500
TrEMBL
-
N6VPY2_9EURY
365
0
40992
TrEMBL
-
A0A7J9NYL9_METMI
397
0
43556
TrEMBL
-
A0A7J9NRZ1_METMI
396
0
43495
TrEMBL
-
A0A8D6PUI3_9EURY
390
0
43010
TrEMBL
-
F6BCV2_METIK
Methanotorris igneus (strain DSM 5666 / JCM 11834 / Kol 5)
384
0
41963
TrEMBL
-
A0A2Z5PEC6_METMI
396
0
43440
TrEMBL
-
A0A8J2FVC0_9BACT
321
0
34525
TrEMBL
-
G0H2U2_METMI
396
0
43502
TrEMBL
-
C9RFZ5_METVM
Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)
384
0
42062
TrEMBL
-
A0A7J9NG07_METMI
397
0
43637
TrEMBL
-
A0A7J9PPP5_METMI
397
0
43635
TrEMBL
-
A0A2Z5PWE0_METMI
396
0
43488
TrEMBL
-
A0A076LH42_9EURY
384
0
42417
TrEMBL
-
A0A7J9P9U4_METMI
397
0
43503
TrEMBL
-
A0A7J9PKJ0_METMI
397
0
43464
TrEMBL
-
C7P8X1_METFA
Methanocaldococcus fervens (strain DSM 4213 / JCM 15782 / AG86)
384
0
41958
TrEMBL
-
H1KZQ8_9EURY
381
0
41776
TrEMBL
-
A0A7J9NRI4_METMI
396
0
43586
TrEMBL
-
A0A7J9PDV5_METMI
397
0
43732
TrEMBL
-
A0A8D6SVS3_9EURY
390
0
43055
TrEMBL
-
A0A7J9S647_METMI
397
0
43576
TrEMBL
-
A0A2L1CBR0_METMI
397
0
43492
TrEMBL
-
D5VSW9_METIM
Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME)
386
0
42533
TrEMBL
-
A0A7J9RYV6_METMI
396
0
43438
TrEMBL
-
A0A0U5KG73_LACDE
390
0
43995
TrEMBL
-
B9X1L2_PREIN
390
0
44416
TrEMBL
-
CGL_ARATH
323
0
34326
Swiss-Prot
-
J9WJN8_BRANA
323
0
34548
TrEMBL
-
Q46061_CORGT
325
0
35485
TrEMBL
-
Q6B7Z5_PSEPU
404
0
44504
TrEMBL
Mitochondrion (Reliability: 4 )
Q8L0X3_FUSNU
306
0
33276
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
x * 46000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
x * 35000, SDS-PAGE
?
x * 34500, calculated from sequence
?
x * 33000, SDS-PAGE, enzyme purified from Fusobacterium nucleatum
?
x * 33400, calculated from sequence
?
x * 37000, SDS-PAGE, recombinant His6-tagged fusion protein
?
-
x * 44000, SDS-PAGE
-
?
-
x * 46000, SDS-PAGE
-
?
-
x * 46000, SDS-PAGE
-
tetramer
4 * 45000, SDS-PAGE
tetramer
-
4 * 45000, SDS-PAGE
-
trimer
3 * 43000, SDS-PAGE
trimer
-
3 * 43000, SDS-PAGE
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
100
10 min, 80% loss of activity, wild-type enzyme
44
thermal inactivation midpoint
50
-
significant decrease in enzymatic activity above 50°C
70
-
30 min, complete inactivation
90
10 min, 22% loss of activity, mutant enzyme C278A
90
10 min, 65% loss of activity, mutant enzyme C318S
90
10 min, 80% loss of activity, mutant enzyme C325S
90
10 min, no loss of activity, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
activity is completely lost by incubating the native protein solution in air for 15 min prior to the incubation
726942
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-20°C, stable for several months
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
enzyme purified form Fusobacterium nucleatum cell extract and from recombinant Escherichia coli
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Chu, L.; Ebersole, J.L.; Kurzban, G.P.; Holt, S.C.
Cystalysin, a 46-kDa L-cysteine desulfhydrase from Treponema denticola: biochemical and biophysical characterization
Clin. Infect. Dis.
28
442-450
1999
Treponema denticola, Treponema denticola ATCC 35404
brenda
Wada, M.; Awano, N.; Haisa, K.; Takagi, H.; Nakamori, S.
Purification, characterization and identification of cysteine desulfhydrase of Corynebacterium glutamicum, and its relationship to cysteine production
FEMS Microbiol. Lett.
217
103-107
2002
Corynebacterium glutamicum (Q46061), Corynebacterium glutamicum ATCC 13032 (Q46061)
brenda
Tchong, S.I.; Xu, H.; White, R.H.
L-Cysteine desulfidase: an [4Fe-4S] enzyme isolated from Methanocaldococcus jannaschii that catalyzes the breakdown of L-cysteine into pyruvate, ammonia, and sulfide
Biochemistry
44
1659-1670
2005
Methanocaldococcus jannaschii (Q58431), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58431)
brenda
Fukamachi, H.; Nakano, Y.; Yoshimura, M.; Koga, T.
Cloning and characterization of the L-cysteine desulfhydrase gene of Fusobacterium nucleatum
FEMS Microbiol. Lett.
215
75-80
2002
Fusobacterium nucleatum (Q8L0X3)
brenda
Yu, Y.; Bai, G.; Liu, C.; Cao, Y.; Geng, P.; Yang, W.
One-step elimination of L-cysteine desulfhydrase from crude enzyme extracts of Pseudomonas sp. TS1138 using an immunomagnetic affinity matrix improves the enzymatic production of L-cysteine
J. Chromatogr. B
853
247-253
2007
Pseudomonas sp. (Q6B7Z5), Pseudomonas sp. TS1138 (Q6B7Z5)
brenda
Xie, Y.; Lai, D.; Mao, Y.; Zhang, W.; Shen, W.; Guan, R.
Molecular cloning, characterization, and expression analysis of a novel gene encoding L-cysteine desulfhydrase from Brassica napus
Mol. Biotechnol.
54
737-746
2013
Brassica napus (J9WJN8)
brenda
Kurzban, G.P.; Chu, L.; Ebersole, J.L.; Holt, S.C.
Sulfhemoglobin formation in human erythrocytes by cystalysin, an L-cysteine desulfhydrase from Treponema denticola
Oral Microbiol. Immunol.
14
153-164
1999
Treponema denticola
brenda
Yano, T.; Fukamachi, H.; Yamamoto, M.; Igarashi, T.
Characterization of L-cysteine desulfhydrase from Prevotella intermedia
Oral Microbiol. Immunol.
24
485-492
2009
Prevotella intermedia (B9X1L2), Prevotella intermedia ATCC 25611 (B9X1L2)
brenda
Scuffi, D.; Alvarez, C.; Laspina, N.; Gotor, C.; Lamattina, L.; Garcia-Mata, C.
Hydrogen sulfide generated by L-cysteine desulfhydrase acts upstream of nitric oxide to modulate abscisic acid-dependent stomatal closure
Plant Physiol.
166
2065-2076
2014
Arabidopsis thaliana (F4K5T2)
brenda
Allegrini, A.; Astegno, A.; La Verde, V.; Dominici, P.
Characterization of C-S lyase from Lactobacillus delbrueckii subsp. bulgaricus ATCC BAA-365 and its potential role in food flavour applications
J. Biochem.
161
349-360
2017
Lactobacillus delbrueckii subsp. bulgaricus (A0A0U5KG73), Lactobacillus delbrueckii subsp. bulgaricus ATCC BAA-365 (A0A0U5KG73)
brenda
Guo, H.; Zhou, H.; Zhang, J.; Guan, W.; Xu, S.; Shen, W.; Xu, G.; Xie, Y.; Foyer, C.H.
L-cysteine desulfhydrase-related H2S production is involved in OsSE5-promoted ammonium tolerance in roots of Oryza sativa
Plant Cell Environ.
40
1777-1790
2017
Oryza sativa, Oryza sativa Wuyunjing 7
brenda
Select items on the left to see more content.
html completed