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Information on EC 4.4.1.1 - cystathionine gamma-lyase
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4.4.1.1 cystathionine gamma-lyaseIUBMB Comments
A multifunctional pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing L-cysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also catalyses the conversion of L-homoserine to 2-oxobutanoate and ammonia, of L-cystine to thiocysteine, pyruvate and ammonia, and of L-cysteine to pyruvate, hydrogen sulfide and ammonia.
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Word Map
- 4.4.1.1
- sulfide
- h2s
- nahs
- beta-synthase
- sulfur
- homocysteine
-
transsulfuration
- pyridoxal
- propargylglycine
- dl-propargylglycine
-
gasotransmitter
- cystathionine-beta-synthase
- sulfurtransferase
-
gaseous
- 3-mercaptopyruvate
-
sulfur-containing
- hydrosulfide
- treponema
- hyperhomocysteinemia
-
adenosyltransferase
- l-methionine
-
desulfuration
- glibenclamide
-
beta-lyase
- denticola
-
vasorelaxation
- hypotaurine
- rhodanese
- persulfide
- alpha-ketobutyrate
- d-cysteine
- ppg
-
s-sulfhydration
-
h2s-producing
-
h2s-generating
- medicine
-
cowden
-
gamma-synthase
- synthesis
-
sulfhydrylase
- analysis
-
aminooxyacetic
- o-acetylserine
-
h2s-induced
-
remethylation
- agriculture
-
cysteinesulfinate
- nutrition
- l-homoserine
- biotechnology
- cys3
-
aldimine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
cystathionine gamma-lyase, cystathionase, gamma-cystathionase, cystathionine-gamma-lyase, cs-like, cysteine desulfhydrase, l-cysteine desulfhydrase, cystalysin, cystathionine gamma lyase, prb-ra, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AFUA_8G04340
cgl
CSE
CSEgamma
CTH
cystalysin
-
-
-
-
cystathionase
cystathioninase
-
-
-
-
cystathionine gamma lyase
cystathionine gamma-lyase
cystathionine-gamma-lyase
cysteine desulfhydrase
cysteine lyase
-
-
-
-
cystine desulfhydrase
-
-
-
-
dehydratase, homoserine
-
-
-
-
desulfhydrase, cysteine
-
-
-
-
EC 4.2.1.15
-
-
formerly
-
gamma-CTL
-
-
-
-
gamma-cystathionase
homoserine deaminase
-
-
-
-
homoserine deaminase-cystathionase
-
-
-
-
homoserine dehydratase
-
-
-
-
human cystathionine-gamma-lyase
pyridoxal-5'-phosphate (PLP)-dependent enzyme
LCD
lyase, cystathionine gamma-
-
-
-
-
PRB-RA
-
-
-
-
Probasin-related antigen
-
-
-
-
TGME49_112930
cgl
CGL variant S403 and I403, polymorphic variants at amino acid residues 403
CSE
-
-
CSE
-
-
CSE
-
-
cystathionase
-
-
-
-
cystathionine gamma-lyase
-
-
-
-
cystathionine-gamma-lyase
-
-
cysteine desulfhydrase
-
-
-
-
gamma-cystathionase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-aminobut-2-enoate = 2-iminobutanoate
spontaneous
-
-
-
2-iminobutanoate + H2O = 2-oxobutanoate + NH3
spontaneous
-
-
-
L-cystathionine = L-cysteine + 2-aminobut-2-enoate
(1a)
-
-
-
L-cystathionine + H2O = L-cysteine + 2-oxobutanoate + NH3
mechanism
-
L-cystathionine + H2O = L-cysteine + 2-oxobutanoate + NH3
mechanism
L-cystathionine + H2O = L-cysteine + 2-oxobutanoate + NH3
the active site consists of two subsites. One recognizes the L-form of amino acids and the other shows affinity for thiol compounds with a carbonyl group
-
L-cystathionine + H2O = L-cysteine + 2-oxobutanoate + NH3
overall reaction
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
of H2S or RSH, C-S bond cleavage
-
hydrolysis
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-cystathionine cysteine-lyase (deaminating; 2-oxobutanoate-forming)
A multifunctional pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing L-cysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also catalyses the conversion of L-homoserine to 2-oxobutanoate and ammonia, of L-cystine to thiocysteine, pyruvate and ammonia, and of L-cysteine to pyruvate, hydrogen sulfide and ammonia.
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CAS REGISTRY NUMBER
COMMENTARY
9012-96-8
-
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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
DL-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
?
L-cystine + 2 H2O
2 NH3 + 2 pyruvate + 2 hydrogen sulfide
-
-
-
?
L-homoserine
2-oxobutyrate + NH3
-
the hydrolysis reaction is balanced by elimination of H2O, the net reaction does not include an H2O term
-
-
?
L-homoserine + 2-mercaptoethanol
S-hydroxyethyl-L-homocysteine
-
8% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + 4-mercaptobutanoate
S-carboxy-n-propyl-L-homocysteine
-
14% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + thioglycerol
S-(2,3-dihydroxypropyl)-L-homocysteine
-
5% of the activity with L-homocysteine and L-Cys
-
?
lanthionine + H2O
NH3 + ?
131% of activity compared to cystathionine
-
?
O-succinyl-L-homoserine
?
-
decomposed most rapidly of all the above substrates
-
-
?
S-(2-aminoethyl)-L-cysteine + H2O
NH3 + pyruvate + cysteamine
-
-
-
?
S-methyl-L-cysteine + H2O
NH3 + pyruvate + methyl mercaptan
-
-
-
?
D-Cys + L-homoserine
D-allocystathionine
-
at 318% of the activity with L-homocysteine and L-cysteine
-
?
D-Cys + L-homoserine
D-allocystathionine
-
gamma-replacement
-
-
?
D-Cys + L-homoserine
D-allocystathionine
-
gamma-replacement
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
alpha,gamma-elimination
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
alpha,gamma-elimination
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
alpha,gamma-elimination
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
alpha,gamma-elimination
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
alpha,gamma-elimination
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
?
L-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
?
L-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
alpha,beta-elimination
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
15% of activity compared to cystathionine
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
measurement of hydrogen sulfide production
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
measurement of hydrogen sulfide production
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
690781, 691828, 691972, 692207, 693818, 693936, 694398, 695079, 708133, 708300, 708411, 708627, 709212, 709676, 709778, 710627
-
-
?
L-cystine + H2O
NH3 + ?
133% of activity compared to cystathionine
-
?
L-djenkolic acid + H2O
NH3 + ?
24% of activity compared to cystathionine
-
?
L-homoserine + 2-mercaptopropionate
S-methylcarboxymethyl-L-homocysteine
-
-
-
-
?
L-homoserine + 2-mercaptopropionate
S-methylcarboxymethyl-L-homocysteine
-
-
-
?
L-homoserine + 2-mercaptopropionate
S-methylcarboxymethyl-L-homocysteine
-
gamma-replacement reaction
-
-
?
L-homoserine + 2-mercaptopropionate
S-methylcarboxymethyl-L-homocysteine
-
gamma-replacement reaction
-
?
L-homoserine + 2-mercaptopropionate
S-methylcarboxymethyl-L-homocysteine
-
73% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + 3-mercaptopropionate
S-carboxyethyl-L-homocysteine
-
-
-
?
L-homoserine + 3-mercaptopropionate
S-carboxyethyl-L-homocysteine
-
187% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + 3-mercaptopropionate
S-carboxyethyl-L-homocysteine
-
gamma-replacement reaction
-
-
?
L-homoserine + 3-mercaptopropionate
S-carboxyethyl-L-homocysteine
-
gamma-replacement reaction
-
?
L-homoserine + D-homocysteine
meso-homolanthionine
-
-
-
?
L-homoserine + D-homocysteine
meso-homolanthionine
-
gamma-replacement reaction, 368% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + H2O
2-oxobutanoate + NH3 + H2O
-
-
-
?
L-homoserine + L-homocysteine
L-homolanthionine
-
gamma-replacement reaction, 314% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + thioglycolate
S-carboxymethyl-L-homocysteine
-
gamma-replacement reaction, 69% of the activity with L-homocysteine and L-Cys
-
?
additional information
?
-
-
enzyme activity is required for high-level cephalosporin biosynthesis but not for low-level production of the antibiotic
-
?
additional information
?
-
Acremonium chrysogenum C10 / ATCC 48272
-
enzyme activity is required for high-level cephalosporin biosynthesis but not for low-level production of the antibiotic
-
?
additional information
?
-
-
cysteine desulfhydrase in Rhodobacter sphaeroides can produce sulfide under aerobic conditions and precipitate metal sulfide complexes on the cell wall
-
-
?
additional information
?
-
-
hydrogen sulfide is a gas signalling molecule which is produced endogenously from L-cysteine
-
-
?
additional information
?
-
-
enzyme responsible for amino acid catabolism
-
-
?
additional information
?
-
-
enzyme responsible for amino acid catabolism
-
-
?
additional information
?
-
-
activity decreases in the following order of substrates: L-cystathione, L-djenkolic, L-cystine, L-cysteine, L-methionine, L-serine
-
?
additional information
?
-
-
enzyme is able to demethiolate methionine into methanethiol
-
-
?
additional information
?
-
-
enzyme is able to demethiolate methionine into methanethiol
-
-
?
additional information
?
-
-
the Streptomyces enzyme has a lower substrate specificity than the rat-liver one
-
-
?
additional information
?
-
-
hydrogen sulfide is a gas signalling molecule which is produced endogenously from L-cysteine
-
-
?
additional information
?
-
-
responsible for the formation of nanocrystals
-
-
?
additional information
?
-
-
Glu333 of cystathionine gamma-lyase acts as a determinant of specificity, it interacts with the distal amine moiety of L-cystathionine, which is not present in the alternative substrate O-acetyl-L-serine. Catalytic efficiency of the yeast enzyme for alpha,gamma-elimination of O-succinyl-L-homoserine, which possesses a distal carboxylate, but lacks an amino group, is 300fold lower than that of the physiological L-cystathionine substrate and 260fold higher than that of L-Hcys, which lacks both distal polar moieties. Proposed polar contacts of the yCGL active site that interact with or are influenced by E48 and E333 overview
-
-
?
additional information
?
-
-
the Streptomyces enzyme has a lower substrate specificity than the rat-liver one
-
-
?
additional information
?
-
catalyzes the second step in the reverse-transsulfuration pathway, which is essential for the metabolic interconversion of the sulfur-containing amino acids cysteine and methionine
-
-
?
additional information
?
-
-
catalyzes the second step in the reverse-transsulfuration pathway, which is essential for the metabolic interconversion of the sulfur-containing amino acids cysteine and methionine
-
-
?
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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
L-homoserine
2-oxobutyrate + NH3
-
the hydrolysis reaction is balanced by elimination of H2O, the net reaction does not include an H2O term
-
-
?
L-homoserine + H2O
2-oxobutanoate + NH3 + H2O
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
-
r
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
-
?
additional information
?
-
-
enzyme activity is required for high-level cephalosporin biosynthesis but not for low-level production of the antibiotic
-
?
additional information
?
-
Acremonium chrysogenum C10 / ATCC 48272
-
enzyme activity is required for high-level cephalosporin biosynthesis but not for low-level production of the antibiotic
-
?
additional information
?
-
-
cysteine desulfhydrase in Rhodobacter sphaeroides can produce sulfide under aerobic conditions and precipitate metal sulfide complexes on the cell wall
-
-
?
additional information
?
-
-
hydrogen sulfide is a gas signalling molecule which is produced endogenously from L-cysteine
-
-
?
additional information
?
-
-
enzyme responsible for amino acid catabolism
-
-
?
additional information
?
-
-
enzyme responsible for amino acid catabolism
-
-
?
additional information
?
-
-
hydrogen sulfide is a gas signalling molecule which is produced endogenously from L-cysteine
-
-
?
additional information
?
-
-
responsible for the formation of nanocrystals
-
-
?
additional information
?
-
catalyzes the second step in the reverse-transsulfuration pathway, which is essential for the metabolic interconversion of the sulfur-containing amino acids cysteine and methionine
-
-
?
additional information
?
-
-
catalyzes the second step in the reverse-transsulfuration pathway, which is essential for the metabolic interconversion of the sulfur-containing amino acids cysteine and methionine
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
690781, 691972, 692207, 693818, 693936, 694398, 708300, 708411, 708627, 709212, 709213, 709676, 709778, 710078, 710627, 730038
pyridoxal 5'-phosphate
-
contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
the epsilon-NH2 group of the active-site Lys forms a Schiff base with pyridoxal 5'phosphate. The enzyme contains the sequence -Ser-X-X-Lys(pyridoxal-5'-phosphate)
pyridoxal 5'-phosphate
a salt bridge between the phosphate of cofactor pyridoxal 5'-phosphate and residue R62 plays an important role in catalyzing beta- and gamma-eliminations
pyridoxal 5'-phosphate
presence of cofactor increases the thermal stability
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
Ca2+ promotes activation of CSE, H2S production by CSE is a Ca2+-dependent phenomenon
Cd2+
HgCl2
-
a potent irreversible enzyme inhibitor, but HgCl2 is also a strong inactivator of cystathionine gamma-lyase
Cd2+
-
activities of cysteine desulfhydrase in strains grown in the presence of 10 and 20 mg/l of cadmium are higher than in the control, while the activities in the presence of 30 and 40 mg/l of cadmium are lower than in the control
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(DL)-propargylglycine
-
chronical treatment of rats with CGL inhibitor (DL)-propargylglycine or cystathionine beta-synthase inhibitor aminooxyacetic acid or a combination of both. Only the rats with combination therapy show a decrease in urinary sulfate excretion rate, which is associated with an increase in mean arterial pressure. Urine flow and sodium excretion are also increased in combination group as consequent to the increase in mean arterial pressure. Glomerular filtration rate does not alter due to these treatments, renal blood flow is lowered only in the combination group compared to the control group
2-(4-methoxyanilino)-2-oxoethyl-(2E)-2-[(3-fluoropyridin-2-yl)methylidene]hydrazine-1-carbodithioate
compound shows at least 400fold selectivity for CSEgamma over inhibition of cystathionine beta-synthase
acetoacetate
-
treatment with 0.025-0.035 mM H2O2, 4-8 mM acetoacetate and high D-glucose of 25 mM causes a significant decrease in enzyme protein expression, enzyme activity, and H2S levels, and an increase in intracellular reactive oxygen species production compared with those in normal controls
CH3-Hg-S-Cys
-
the cysteine S-conjugate of Hg2+ is a potent irreversible enzyme inhibitor
Cys-S-Hg-S-Cys
-
the cysteine S-conjugate of Hg2+ is a potent irreversible enzyme inhibitor
D-glucose
-
treatment with 0.025-0.035 mM H2O2, 4-8 mM acetoacetate and high D-glucose of 25 mM causes a significant decrease in enzyme protein expression, enzyme activity, and H2S levels, and an increase in intracellular reactive oxygen species production compared with those in normal controls
H2O2
-
treatment with 0.025-0.035 mM H2O2, 4-8 mM acetoacetate and high D-glucose of 25 mM causes a significant decrease in enzyme protein expression, enzyme activity, and H2S levels, and an increase in intracellular reactive oxygen species production compared with those in normal controls
HgCl2
-
a potent irreversible enzyme inhibitor, but HgCl2 is also a strong inactivator of cystathionine gamma-lyase
NEM
-
0.05 mM, inhibition is partly relieved by 0.2 mM 2,3-dimercaptopropanol
O2
-
homogenized gills produces H2S enzymatically, and H2S production is inhibited by O2, whereas mitchondrial H2S consumption is O2 dependent
streptozotocin
-
livers from streptozotocin-treated type I diabetic rats have lower levels of enzyme protein expression, enzyme activity, reduced tissue H2S formation, and increased reactive oxygen species production compared with those of controls
5,5'-dithiobis(2-nitrobenzoate)
-
8 of the 12 -SH groups in native enzyme react reversibly. Cystathionine at high concentrations, partially relieves the inhibition
aminooxyacetic acid
-
chronical treatment of rats with CGL inhibitor (DL)-propargylglycine or cystathionine beta-synthase inhibitor aminooxyacetic acid or a combination of both. Only the rats with combination therapy show a decrease in urinary sulfate excretion rate, which is associated with an increase in mean arterial pressure. Urine flow and sodium excretion are also increased in combination group as consequent to the increase in mean arterial pressure. Glomerular filtration rate does not alter due to these treatments, renal blood flow is lowered only in the combination group compared to the control group
beta,beta,beta-trifluoroalanine
-
the epsilon-NH2 group of the active-site Lys forms a Schiff base with pyridoxal 5'phosphate is capable of interacting with the beta carbon of the suicide inactivator beta,beta,beta-trifluoroalanine
Beta-cyano-L-alanine
-
pretreating adiopose tissues with the CSE inhibitor beta-cyano-L-alanine (BCA) (2 mmol/l) for 20 min significantly decreased the endogenous H2S production by 89%, as compared with controls
Beta-cyano-L-alanine
-
10 mM inhibits testosterone induced H2S biosynthesis
Cys
-
above 10 mM, inhibits replacement reaction with L-homoserine and L-Cys
DL-propargylglycine
an irreversible enzyme inhibitor, molecular mechanism of DL-propargylglycine action in vivo
DL-propargylglycine
-
pretreating adiopose tissues with the CSE inhibitor DL-propargylglycine (PPG) (10 mmol/l) for 20 min significantly decreased the endogenous H2S production by 85%, as compared with controls
PCMB
-
0.05 mM, inhibition is partly relieved by 0.2 mM 2,3-dimercaptopropanol
Penicillamine
-
alpha,beta-elimination of L-homoserine; D-penicillamine; L-penicillamine
phenylhydrazine
-
alpha,beta-elimination L-homoserine as substrate
Semicarbazide
-
alpha,beta-elimination L-homoserine as substrate
additional information
-
no or poor inhibition by methylselenocysteine, D-cycloserine, pargyline, and parsalmide
-
additional information
-
the reaction of cystathionase with cystathionine and homoserine decreases rapidly with time. The reaction becomes inhibited, probably by the formation of a stable enzyme-bound intermediate. The inhibition can be partially relieved by pyridoxal 5'-phosphate, NaCl, alpha-keto acids, and other compounds. These agents prevent the inhibition by providing an environment that helps to decrease the nucleophilicity of the sulfhydryl
-
additional information
-
inhibitory effect of the chelating agents and related compounds is at least partly and in some instances completely eliminated in the presence of an increased concentration of pyridoxal 5'-phosphate
-
additional information
-
administration of CSE inhibitors enhances the glucose uptake of adipocytes
-
additional information
-
dexamethasone reduces the expression of cystathionine gamma lyase. Also reduces LPS-induced upregulation of CSE in fetal liver cells. 6-amino-4-(4-phenoxyphenylethylamino) quinazoline (QNZ) 10 nM, a selective inhibitor of transcription via the NF-kappaB pathway, abolishs lipopolysaccharide-induced upregulation of CSE expression
-
additional information
-
extent to which inactivation occurs with the various mercury-containing compounds in descending order: Cys-S-Hg-S-Cys, HgCl2, CH3Hg-S-Cys
-
additional information
cystathionine gamma-lyase encoded by CYS3 is repressed by addition of cysteine to the growth medium
-
additional information
-
cystathionine gamma-lyase encoded by CYS3 is repressed by addition of cysteine to the growth medium
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-propargyl-cysteine
-
(S)-propargyl-cysteine increases CSE activity by 1.6fold in myocardial infarction rats
calcium-calmodulin
-
catalytic activity of pure CSE is increased more than 2fold by calcium and calmodulin, but not by either substance alone
-
CYS3
a bZIP transcriptional activator, is the key regulator and necessary for regulation expression of the sulfur-related genes, binds on a consensus sequence for CYS3 binding
-
L-cysteine
low concentration of cellular cysteine leads to elevation of cystathionine gamma-lyase
additional information
-
presence of 10 mM L-cysteine increases H2S production rate. Low oxygen levels increases H2S production rates
-
additional information
-
glucose (10 or 20 mM) increases the cystathionine-gamma-lyase expression in the beta-cells
-
additional information
-
NO increases the production of hydrogen sulphide in fetal membranes. Presence of 10 mM L-cysteine increases H2S production rate. Low oxygen levels increases H2S production rates
-
additional information
-
testosterone incubation of rat aorta does not change CSE expression. Testosterone modulates H2S levels by increasing the enzymatic conversion of L-cysteine to H2S
-
additional information
cystathionine gamma-lyase encoded by CYS3 is induced by sulfur starvation
-
additional information
-
cystathionine gamma-lyase encoded by CYS3 is induced by sulfur starvation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
beta-chloro-L-alanine
-
Y123F/Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C
0.17
beta-chloro-L-alanine
-
Y123F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C
1.21
beta-chloro-L-alanine
-
wild type, 20 mM potassium phosphate buffer, pH 7.4, 25°C
3.2
beta-chloro-L-alanine
-
Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C
0.76
D-alanine
-
racemization, Y123F/Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C
10
D-alanine
-
racemization, wild type, 20 mM potassium phosphate buffer, pH 7.4, 25°C
22.4
D-alanine
-
racemization, Y123F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C
25.3
D-alanine
-
racemization, Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C
3.36
DL-cystathionine
-
native enzyme, pH not specified in the publication, temperature not specified in the publication
3.4
DL-cystathionine
-
protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication
1
L-alanine
-
racemization, Y123F/Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C
10
L-alanine
-
racemization, wild type, 20 mM potassium phosphate buffer, pH 7.4, 25°C
14.3
L-alanine
-
racemization, Y123F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C
20
L-alanine
-
racemization, Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C
0.42
L-cystathionine
-
His-tagged recombinant wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.45
L-cystathionine
-
native wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.81
L-cystathionine
-
mutant enzyme E48F, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.82
L-cystathionine
-
mutant enzyme E48A, in 50 mM potassium phosphate, pH 7.8, at 25°C
1.11
L-cystathionine
-
mutant enzyme E48D, in 50 mM potassium phosphate, pH 7.8, at 25°C
5.2
L-cystathionine
-
mutant enzyme E333A, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.76
L-cysteine
-
mutant enzyme E339Y, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
1.9
L-cysteine
-
wild type enzyme, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
3.3
L-cysteine
-
mutant enzyme E339K, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
7.7
L-cysteine
-
mutant enzyme E339A, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
DL-cystathionine
-
protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication
0.13
DL-cystathionine
-
native enzyme, pH not specified in the publication, temperature not specified in the publication
0.39
L-cystathionine
-
mutant enzyme E48F, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.67
L-cystathionine
-
mutant enzyme E48A, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.69
L-cystathionine
-
mutant enzyme E333A, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.76
L-cystathionine
-
mutant enzyme E48D, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.9
L-cystathionine
-
native wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
1.81
L-cystathionine
-
His-tagged recombinant wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.12
L-cysteine
-
wild type enzyme, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.34
L-cysteine
-
mutant enzyme E339K, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.76
L-cysteine
-
mutant enzyme E339Y, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
1.44
L-cysteine
-
mutant enzyme E339A, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.0035
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48D/E333D
0.0047
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48A/E333A
0.0092
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48Q/E333Q
0.0097
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.029
DL-cystathionine
-
protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication
0.04
DL-cystathionine
-
native enzyme, pH not specified in the publication, temperature not specified in the publication
0.0037
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48A/E333A
0.0088
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48D/E333D
0.0169
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48Q/E333Q
0.132
L-cystathionine
-
mutant enzyme E333A, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.147
L-cystathionine
-
mutant enzyme E333Y, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.49
L-cystathionine
-
mutant enzyme E48F, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.68
L-cystathionine
-
mutant enzyme E48D, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.82
L-cystathionine
-
mutant enzyme E48A, in 50 mM potassium phosphate, pH 7.8, at 25°C
1.98
L-cystathionine
-
native wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
4.3
L-cystathionine
-
His-tagged recombinant wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.06
L-cysteine
-
wild type enzyme, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.11
L-cysteine
-
mutant enzyme E339K, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.19
L-cysteine
-
mutant enzyme E339A, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.43
L-cysteine
-
mutant enzyme E339Y, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.0016
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48A/E333A
0.0038
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant wild-type enzyme and mutant E48D
0.005
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48D/E333D
0.006
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48Q/E333Q
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
2-(4-methoxyanilino)-2-oxoethyl-(2E)-2-[(3-fluoropyridin-2-yl)methylidene]hydrazine-1-carbodithioate
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
1.34
6-diazo-5-oxonorleucine
Aspergillus carneus
-
protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication
2.16
6-diazo-5-oxonorleucine
Aspergillus carneus
-
native enzyme, pH not specified in the publication, temperature not specified in the publication
0.66
iodoacetate
Aspergillus carneus
-
protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication
0.98
iodoacetate
Aspergillus carneus
-
native enzyme, pH not specified in the publication, temperature not specified in the publication
0.91
propargylglycine
Aspergillus carneus
-
native enzyme, pH not specified in the publication, temperature not specified in the publication
1.49
propargylglycine
Aspergillus carneus
-
protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.49
48.71
-
protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication
59.71
-
native enzyme, pH not specified in the publication, temperature not specified in the publication
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.5
-
pH 5.0: about 60% of maximal activity, pH 8.5: about 55% of maximal activity
6.5 - 8.5
-
pH 6.5: about 20% of maximal activity, pH 8.5: about 70% of maximal activity. No activity below pH 5.0 and above pH 9
8 - 9
-
pH 8.0: about 85% of maximal activity, pH 9.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
50
-
alpha,gamma-elimination of L-cystathionine and L-homoserine
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
-
10°C: about 35% of maximal activity, 40°C: rapid decrease of activity above
30 - 55
-
0.1 M potassium phosphate buffer, pH 7.8, 0.2 mM pyridoxal-5'-phosphate and 1 mM EDTA
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
5584, 34486, 34488, 34489, 34490, 34491, 34492, 34493, 34494, 34495, 34496, 34497, 34498, 34500, 34501
-
-
brenda
-
671177, 671768, 672489, 691972, 693818, 699119, 707176, 708133, 708300, 708411, 708627, 709212, 709213, 709676, 709778, 710078, 710627, 713713, 721432, 730038
-
-
brenda
76 male Sprague-Dawley rats (200-250 g), 96 different age rats (from 1 month to 12 months old) and insulin-resistant animals
-
-
brenda
Zucker diabetic fatty rats, comparison with Zucker fatty and Zucker lean rats
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression of both cystathionine gamma-lyase and 3-mercaptopyruvate sulfurtransferase, the activity of 3-mercaptopyruvate sulfurtransferase is higher than that of cystathionine gamma-lyase
brenda
-
mainly expressed in airway and vascular smooth muscle cells in rat lung tissue
brenda
-
enzyme expression in numerous oval or polygonal cells
brenda
-
whole cells, cell lysate of a culture broth, cell wall of a subcellular fraction
brenda
-
high expression in cerebral organs and in the epithelium of the lateral cephalic slits through which these organs open to the outside, highest in the cerebral organs in the cells lining the inner channel and also in the rear cluster of neuro-glandular cells
brenda
-
of the canals of the cerebral organs, enzyme expression
brenda
-
CSE is localized in the muscular trabeculae and the smooth-muscle component of the penile artery
brenda
-
only in the anterior- and the postero-lateral areas of the body
brenda
-
order of hydrogen sulfide production rates for different tissues are: liver (777 nM/min/g), followed by uterus (168 nM/min/g), fetal membranes (22.3 nM/min/g), placenta (11.1 nM/min/g), compared to human placenta (200 nM/min/g)
brenda
-
in neurons and nerve fibers of the lateral nerve cords immediately behind the ventral ganglia
brenda
-
pregnant myometrium, primarily localized to smooth muscle cells of pregnant myometrium
brenda
-
peripheral blood mononuclear cells, PBMC, isolated from healthy subjects and type 1 diabetic patients
brenda
-
primarily localized to smooth muscle cells of pregnant myometrium
brenda
-
order of hydrogen sulfide production rates for different tissues are: liver (777 nM/min/g), followed by uterus (168 nM/min/g), fetal membranes (22.3 nM/min/g), placenta (11.1 nM/min/g), compared to human placenta (200 nM/min/g)
brenda
-
expression of both cystathionine gamma-lyase and 3-mercaptopyruvate sulfurtransferase, the activity of 3-mercaptopyruvate sulfurtransferase is higher than that of cystathionine gamma-lyase
brenda
additional information
-
predominantly localized to the endothelial layer of blood vessels
brenda
-
with a decreasing activity in tail artery, aorta and mesenteric arteries
brenda
-
activity in human brain is 100fold higher than that observed in mouse brain
brenda
-
in the brain, where CSE levels are low, localizations are predominantly in white matter
brenda
-
cystathionine-beta-synthase and cystathionine-gamma-lyase are expressed in the normal human colon. Expression is significantly decreased in the ganglionic and aganglionic bowel of patients with Hirschsprung Disease
brenda
only in adult tissue, not detectable in fetal, premature and full-term neonatal liver
brenda
-
-
brenda
-
-
5584, 34486, 34488, 34490, 34491, 34492, 34493, 34494, 34495, 34496, 34498, 34500, 34501, 672489, 690352, 690781, 693818, 694398, 708300, 709778, 721432
brenda
-
order of hydrogen sulfide production rates for different tissues are: liver (777 nM/min/g), followed by uterus (168 nM/min/g), fetal membranes (22.3 nM/min/g), placenta (11.1 nM/min/g), compared to human placenta (200 nM/min/g)
brenda
-
mainly expressed in airway and vascular smooth muscle cells in rat lung tissue
brenda
-
of lateral nerve cord and in the area of the cell bodies
brenda
-
order of hydrogen sulfide production rates for different tissues are: liver (777 nM/min/g), followed by uterus (168 nM/min/g), fetal membranes (22.3 nM/min/g), placenta (11.1 nM/min/g), compared to human placenta (200 nM/min/g)
brenda
-
expression of both cystathionine gamma-lyase and 3-mercaptopyruvate sulfurtransferase, the activity of 3-mercaptopyruvate sulfurtransferase is higher than that of cystathionine gamma-lyase. The low level of cystathionine gamma-lyase and low GSH/GSSG ratio correspond with the highest cystathionine gamma-lyase activity mong the cell lines tested
brenda
-
expression of both cystathionine gamma-lyase and 3-mercaptopyruvate sulfurtransferase, the activity of 3-mercaptopyruvate sulfurtransferase is higher than that of cystathionine gamma-lyase. Very low activity of cystathionine gamma-lyase
brenda
-
order of hydrogen sulfide production rates for different tissues are: liver (777 nM/min/g), followed by uterus (168 nM/min/g), fetal membranes (22.3 nM/min/g), placenta (11.1 nM/min/g), compared to human placenta (200 nM/min/g)
brenda
-
mainly expressed in airway and vascular smooth muscle cells in rat lung tissue
brenda
additional information
the enzyme expression levels gradually increases in an age-dependent manner, expression profiling, overview
brenda
additional information
-
the enzyme expression levels gradually increases in an age-dependent manner, expression profiling, overview
brenda
additional information
-
the enzyme expression levels gradually increases in an age-dependent manner, expression profiling, overview
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
content of cysteine desulfhydrase depending on the growth phase of cells
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
the Leishmania major enzyme is able to rescue the wild-type phenotype of a Saccharomyces cerevisiae enzyme-null mutant
malfunction
severe loss of cystathionine gamma-lyase activity is accompanied by adverse clinical effects
malfunction
-
both hyperglycemia and hyperketonemia mediate a reduction in enzyme expression and activity, which can contribute to the impaired H2S signaling associated with diabetes. Livers from streptozotocin-treated type I diabetic rats have lower levels of enzyme protein expression, enzyme activity, reduced tissue H2S formation, and increased reactive oxygen species production compared with those of controls
malfunction
-
both hyperglycemia and hyperketonemia mediate a reduction in enzyme expression and activity, which can contribute to the impaired H2S signaling associated with diabetes. Treatment with 0.025-0.035 mM H2O2, 4-8 mM acetoacetate and high D-glucose of 25 mM causes a significant decrease in enzyme protein expression, enzyme activity, and H2S levels, and an increase in intracellular reactive oxygen species production compared with those in normal controls
malfunction
inhibiting the enzyme activity with propargylglycine or silencing CSE expression using an siRNA approach results in a greater reduction in cell viability under exposure to the oxidizing agent hydrogen peroxide. Cellular oxidative stress also increases significantly upon propargylglycine inhibition or enzyme knockdown. Increased sensitivity towards H2O2-induced cytotoxicity in CSE-siRNAtransfected cells is associated with a decreased glutathione concentration (GSH) and glutathione ratio (GSH/GSSG). Incubation of cells with exogenous H2S increases the GSH concentration and GSH/GSSG ratio
malfunction
-
both hyperglycemia and hyperketonemia mediate a reduction in enzyme expression and activity, which can contribute to the impaired H2S signaling associated with diabetes. Livers from streptozotocin-treated type I diabetic rats have lower levels of enzyme protein expression, enzyme activity, reduced tissue H2S formation, and increased reactive oxygen species production compared with those of controls
-
metabolism
-
CSE is a key enzyme in the pathway of cystathionine metabolism to produce endogenous H2S
metabolism
-
cystathionine gamma-lyase catalyzes the hydrolysis of L-cystathionine in the second step of the reverse transsulfuration pathway, which converts L-homocysteine to L-Cys
metabolism
the two cysteine desulfhydrases, L-cysteine desulfhydrase and D-cysteine desulfhydrase, are mainly responsible for the degradation of cysteine in order to generate H2S, they show similar expression patterns in tissues
metabolism
-
the two cysteine desulfhydrases, L-cysteine desulfhydrase and D-cysteine desulfhydrase, are mainly responsible for the degradation of cysteine in order to generate H2S, they show similar expression patterns in tissues
-
physiological function
-
CSE activity may contribute to butyrate-stimulated H2S production in WiDr cells
physiological function
-
DES1 from Arabidopsis is an L-Cys desulfhydrase involved in maintaining Cys homeostasis, mainly at late developmental stages or under environmental perturbations
physiological function
-
human myometrium smooth muscle cells express cystathionine beta-synthase and cystathionine gamma-lyase. Endogenous H2S generated by cystathionine beta-synthase and cystathionine gamma-lyase locally modulates the contractility of pregnant myometrium
physiological function
-
Mice with a targeted deletion of the CSE gene fed a cysteine-limited diet exhibit growth retardation, decreased levels of cysteine, glutathione, and H2S, and increased plasma homocysteine level. Histological examinations of liver do not reveal any abnormality and plasma levels of aspartate aminotransferase, alanine aminotransferase, and albumin are normal in these animals. No CSE-KO mice survive after 12 weeks of feeding with the cysteine-limited diet. Supplementation of H2S to the CSE-KO mice fails to reverse the aforementioned abnormalities. Supplementation of cysteine in the drinking water of the CSE-KO mice significantly increases plasma cysteine and glutathione levels. This eventually leads to an increase in body weight and rescues the animals from death
physiological function
cystathionine gamma-lyase is an important enzyme responsible for endogenous H2S production in mammalian systems. Modulation of enzyme catalytic activity alters its antioxidative activity. Role of CSE in contributing to cellular antioxidative mechanisms in cell lines of peripheral tissue origin. Knockdown of CSE does not result in significant spontaneous cell death, indicating that CSE is not vital for cell survival in the cell lines studied
physiological function
L-cysteine desulfhydrase is the enzyme mainly responsible for the degradation of cysteine in order to generate H2S, D-cysteine desulfhydrase, EC 4.4.1.15, is also involved. Gene expression regulation relationship to drought tolerance in Arabidopsis thaliana, protective effect of H2S against drought, and H2S induces stomatal closure, overview
physiological function
aortas from atherogenic apolipoprotein E knockout mice fed a high-fat diet show reduced CSEgamma mRNA expression and protein abundance
physiological function
CSE expression and H2S production are increased during adipocyte differentiation, and the pattern of CSE mRNA expression is similar to that of CCAAT/enhancer-binding protein C/EBPbeta and C/EBPdelta, key regulators for adipogenesis. High fat diet-induced fat mass is lost in CSE deficient mice
physiological function
CSE-H2S is a dominant H2S generating system in osteoclasts, while cystathionine synthase beta does not generate H2S. A significant increase in CSE mRNA expression and H2S production is observed in periodontal ligament tissues after 3 days of mechanical loading. CSE gene knockout leads to a significant reduction in the number of maxillary osteoclasts and in the amount of tooth movement. The expression of IL-1, IL-6 and TNF-alpha is lower in CSE-/- mice after mechanical loading. Application of the H2S donor GYY4137 increases the number of RANKL-induced osteoclasts, the number of osteoclasts in periodontal tissues and tooth movement distance in CSE-/- mice
physiological function
-
CSE/H2S significantly upregulates the expression of ATP-binding cassette transporter A1 mRNA and protein via PI3K/AKT pathway in foam cells derived from human THP-1 macrophages. The microRNA R-216a directly targets the 3' untranslated region of CSE and significantly reduces CSE and ATP-binding cassette transporter A1 expression, and also decreases the phosphorylation of PI3K and AKT. Cholesterol efflux decrease, and cholesterol levels increase in THP-1 macrophage-derived foam cells in response to treatment with miR-216a
physiological function
CSEgamma expression is upregulated by pan-histone deacetylase inhibitors and by class II-specific HDAC inhibitors, but not by other class-specific inhibitors. The histone deacetylase 6 selective inhibitor tubacin and histone deacetylase 6-specific siRNA increase CSEgamma expression and block oxidized LDL-mediated reductions in endothelial CSEgamma expression and CSEgamma promoter activity
physiological function
deficiency of cystathionine beta synthase upregulates cardiac cystathionine gamma lyase, plausibly by inducing specificity protein SP1
physiological function
in an in vitro model of disturbed flow, laminar flow significantly reduces CSE expression in vitro, and only disturbed flow regions show discernable CSE protein expression in vivo. CSE expression in disturbed flow regions critically regulates both endothelial activation and flow-dependent vascular remodeling, in part through altered NO availability
physiological function
levels of serum creatinine and renal expression of acute kidney injury marker proteins are equivalent between Cth deficient and control mice. Renal ischemia/reperfusion injury causes less renal tubular damage in Cth deficient mice. The renal population of infiltrated granulocytes/macrophages is equivalent in these mice. Renal expression levels of certain inflammatory cytokines/adhesion molecules believed to play a role in renal ischemia/reperfusion injury are lower after renal ischemia/reperfusion injury in Cth deficient mice
physiological function
-
overexpressing Arabidopsis thaliana cystathionine gamma-synthase in Solanum tuberosum increases tuber methionine levels. Solanum tuberosum cv. Desiree plants with overexpression of Arabidopsis thaliana cystathionine gamma-synthase and endogenous methionine gamma-lyase silenced by RNA interference are morphologically normal and accumulate higher free methionine levels than either single-transgenic line
physiological function
unilateral ureteral obstruction of wild-type mice reduces the expression of H2S-producing enzymes, CSE, cystathionine beta-synthase, and 3-mercaptopyruvate sulfurtransferase in the obstructed kidneys, resulting in decreased H2S and GSH levels. CSE gene deletion lowers H2S and GSH levels in the kidneys and exacerbates the decrease in H2S and GSH levels and increase in superoxide formation and oxidative damage to proteins, lipids, and DNA in the kidneys after unilateral ureteral obstruction, accompanied by greater kidney fibrosis, deposition of extracellular matrixes, expression of alpha-smooth muscle actin, tubular damage, and infiltration of inflammatory cells. CSE gene deletion exacerbates mitochondrial fragmentation and apoptosis of renal tubule cells after unilateral ureteral obstruction
physiological function
-
L-cysteine desulfhydrase is the enzyme mainly responsible for the degradation of cysteine in order to generate H2S, D-cysteine desulfhydrase, EC 4.4.1.15, is also involved. Gene expression regulation relationship to drought tolerance in Arabidopsis thaliana, protective effect of H2S against drought, and H2S induces stomatal closure, overview
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Show AA Sequence and Transmembrane Helices (5091 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
156000
160000
170000
178000
wild-type, molecular masses of both the T67I CGL (156 kDa) and the Q240E mutant (170 kDa) are comparable to that of wild-type CGL (167 kDa), indicating that both mutants exist as tetrameric proteins
39700
the 44.5 kDa bands for variant 1 of CSE are detected in all arteries tested with Western blotting. CSE variant 2 is also detected at 39.7 kDa in a few arteries, but the band is not as intense and is not detected in most arteries
40000
41000
43000
43600
44000
44500
45000
44500
the 44.5 kDa bands for variant 1 of CSE are detected in all arteries tested with Western blotting. CSE variant 2 is also detected at 39.7 kDa in a few arteries, but the band is not as intense and is not detected in most arteries
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
In the three-dimensional structure of human CGL, two monomers contribute residues to each of the two active sites in the dimer, and two dimers come together to form a tetramer
tetramer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling and dynamics simulations. Enzyme has high conformational stability with high flexibility at the nonstructural regions
structures of mutant E59N/R119L/E339V with distinct reaction intermediates, including internal aldimine, substrate-bound, gem-diamine, and external aldimine forms. A locally unfolded active site correlates with inhibition of activity as a function of ionic strength
using sitting drop and hanging drop vapor diffusion methods at room temperature
-
molecular modeling of the external aldimine of wild-type in complex with L-cystathionine
crystals of two different shapes, plate-shaped and pyramid-shaped, diffract to 2.9 and 3.2 A resolution and belong to the primitive orthogonal space group P212121 and the tetragonal space group P41 (or P43), with unit-cell parameters a = 73.0, b = 144.9, c = 152.3 A and a = b = 78.2, c = 300.7 A, respectively. For the P212121 crystals, three or four monomers exist in the asymmetric unit with a corresponding VM of 3.02 or 2.26 A3/Da and a solvent content of 59.3 or 45.7%. For the P41 (or P43) crystals, four or five monomers exist in the asymmetric unit with a corresponding VM of 2.59 or 2.09 A3/Da and a solvent content of 52.5 or 40.6%
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D187A
E339A
E339K
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
E339Y
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
E349A
E59N/R119L/E339V
mutant engineered as an L-Met-degrading enzyme based on the human cystathionine-gamma-lyase
K212A
Q240E
missense mutation. Exhibits a 70fold decrease in Vmax compared to that of wild-type CGL. The KMs for L-cystathionine are comparable to that of wild type CGL. The pyridoxal 5'-phosphate content of the Q240E mutant is about 80fold lower than that of wild-type enzyme
R197C
the mutant shows about 44% activity compared to the wild type enzyme
R375A
R62A
R62H
exchange of Arg62 for His62 shifts the geometry of the active site, decreases the strength of pyridoxal 5'-phosphate binding, and makes this bond pH dependent under physiological conditions
S209A
T189A
T211A
T67I
Y114A
Y114F
-
the mutation leads to significant increase in the production of H2S by CSE
Y60A
E333A
E333D
-
site-directed mutagenesis of the active-site residue, pH optimum 7.2-8.0, the mutant shows increased KM for L-cystathionine up to 17fold, and 2.5fold for O-acetyl-L-serine
E333Q
-
site-directed mutagenesis of the active-site residue, pH optimum 7.6-8.4, the mutant shows increased KM for L-cystathionine up to 17fold, and 2.5fold for O-acetyl-L-serine
E333Y
-
the mutation leads to 30fold reduction of kcat/Km for L-cystathionine
E48A
E48A/E333A
-
site-directed mutagenesis of the active-site residues, pH optimum 8.4-9.2
E48D
E48D/E333D
-
site-directed mutagenesis of the active-site residues, pH optimum 7.6-8.4
E48F
-
the mutation leads to about 9fold reduction of kcat/Km for L-cystathionine
E48Q
-
site-directed mutagenesis of the active-site residue, pH optimum 7.4-8.2
E48Q/E333Q
-
site-directed mutagenesis of the active-site residues, pH optimum 7.9-8.7
N360S
mutation does not alter enzyme conformation, but leads to a 56fold decrease in catalyic efficiency for L-cystathionine
N360S
-
mutation does not alter enzyme conformation, but leads to a 56fold decrease in catalyic efficiency for L-cystathionine
-
additional information
E339A
-
the mutant demonstrates an approximately 6fold enhancement in H2S production
E339A
site-directed mutagenesis, the hyperactive mutant displays a 4fold greater H2S production compared to the wild-type enzyme
E349A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
E349A
-
the mutant displays enzyme activity comparable to that for wild type enzyme
K212A
-
1.3% of wild-type activity, residue involved in binding of pyridoxal 5'-phosphate
S209A
-
the mutant displays enzyme activity comparable to that for wild type enzyme
T211A
-
the mutant displays enzyme activity comparable to that for wild type enzyme
T67I
missense mutation. Exhibits a 3.5fold decrease in Vmax compared to that of wild-type CGL. The KMs for L-cystathionine are comparable to that of wild type CGL. The pyridoxal 5'-phosphate content of the T67I mutant is about 4fold lower than that of wild-type enzyme
T67I
the mutant shows about 13% activity compared to the wild type enzyme
Y114A
-
3% of wild-type activity, residue involved in binding of pyridoxal 5'-phosphate
Y60A
site-directed mutagenesis, inactive mutant, which cannot provide antioxidative activity
E333A
-
the mutation leads to 30fold reduction of kcat/Km for L-cystathionine
E333A
-
site-directed mutagenesis of the active-site residue, pH optimum 7.8-8.6, the mutant shows increased KM for L-cystathionine up to 17fold, and 2.5fold for O-acetyl-L-serine
E48A
-
the mutation leads to about 6fold reduction of kcat/Km for L-cystathionine
E48A
-
site-directed mutagenesis of the active-site residue, pH optimum 7.6-8.4
E48D
-
the mutation leads to about 5fold reduction of kcat/Km for L-cystathionine
E48D
-
site-directed mutagenesis of the active-site residue, pH optimum 7.07.8
additional information
-
gene disruption mutants, lower cephalosporin production in Shens defined fermentation medium supplemented with methionine, but not in the same medium without methionine
additional information
Acremonium chrysogenum C10 / ATCC 48272
-
gene disruption mutants, lower cephalosporin production in Shens defined fermentation medium supplemented with methionine, but not in the same medium without methionine
-
additional information
-
the total DES activity in mutants des1-1 and des1-2 plants is reduced by 20% to 25% in both mutants relative to their respective wild types
additional information
various Aspergillus nidulans mutant strains (sconB, metR, metG, mecB, cysB)
additional information
-
various Aspergillus nidulans mutant strains (sconB, metR, metG, mecB, cysB)
additional information
-
loss of enzyme activity in patients with hereditary cystathioninuria can be caused by nonsense mutations or by missense mutations
additional information
enzyme silencing by CSE-specific siRNA in HEK-293 cells, Hep-G2 cells, and IMR90 cells with loss of the protein band to at least 90% efficacy in the siRNA-transfected samples as compared with the scrambled-siRNA negative control
additional information
-
enzyme silencing by CSE-specific siRNA, treatment with acetoacetate and high D-glucose of 25 mM causes a significant decrease in enzyme protein expression compared with those in normal controls, while 4-hydroxybutyrate has no effect
additional information
-
PNG902 and PNG903 strains (cgl, cyuC and mlp mutants), constructing a cgl mutant (PNG901) and comparing it to a similarly constructed cyuC mutant (PNG902). The growth defects in aerated cultures of both mutants are alleviated by supplementation with cysteine (and cystine in the cgl mutant) but not methionine, with the cyuC mutant showing a much higher requirement
additional information
-
PNG902 and PNG903 strains (cgl, cyuC and mlp mutants), constructing a cgl mutant (PNG901) and comparing it to a similarly constructed cyuC mutant (PNG902). The growth defects in aerated cultures of both mutants are alleviated by supplementation with cysteine (and cystine in the cgl mutant) but not methionine, with the cyuC mutant showing a much higher requirement
-
additional information
-
CSE-/- mice and CSE-/+ mice, mice genetically deficient in this enzyme display marked hypertension, comparable to that of eNOS-/- mice
additional information
-
pH optima of the mutant enzymes vary from wild-type enzyme, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
-
rapid loss of activity at 60°C, 0.1 M potassium phosphate buffer, pH 7.8, 0.2 mM pyridoxal-5'-phosphate and 1 mM EDTA
40
50
55
60
73.3
melting temperature, potassium phosphate buffer, pH 7.0-8.0
76.3
melting temperature, MES or sodium phosphate buffer, pH 7.0
55
-
0.04 mM pyridoxal 5'-phosphate, 10 min, 15% loss of activity
60
-
0.04 mM pyridoxal 5'-phosphate, 10 min, 50% loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 45% glycerol solution, containing 10 mM potassium phosphate, pH 7.5, 0.02 mM pyridoxal 5'-phosphate, 0.12 mM EDTA, 0.2 mM DTT, stable for 2 months or more
-
-50°C, potassium phosphate buffer, pH 7.5, enzyme stabilized by pyridoxal 5'-phosphate, EDTA, and dithiothreitol retains full activity for several months
-
4°C, 10 mM potassium phosphate, pH 7.5, containing 0.02 mM pyridoxal phosphate, 0.12 mM EDTA, 0.2 mM dithiothreitol stable for 2 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, butyl-Toyopearl 650M resin column chromatography, and DEAE column chromatography
-
combination of Ni-NTA chromatography, anion exchange chromatography, and gel filtration steps
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Codon Plus by metal affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
gene cys-16+, DNA and amino acid sequence determination and analysis, gene cys-16+ gene encodes a polypeptide of 417 amino acids with a highly conserved pyridoxal 5'-phosphate binding site and substrate-cofactor binding pocket
gene LmjF35.3230 or Lmj_CGL, functional complementation of a CGL null mutant strain DELTA CYS3 of Saccharomyces cerevisiae
overexpression in HEK-293, overexpression inhibits cell proliferation and DNA synthesis
quantitative enzyme expression PCR analysis
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Codon Plus using expression vector pGEX-4T3/GST-CSE
-
the His-tagged enzyme is expressed in Escherichia coli KS1000 cells
-
transfection into HEK-293 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
0.001 mg/ml lipopolysaccharide stimulates the CSE mRNA and protein levels 2.5fold, L-arginine (0.1-1 mM) dose-dependently enhances CSE mRNA and protein expression in lipopolysaccharide-treated primary macrophages
-
aortas from atherogenic apolipoprotein E knockout mice fed a high-fat diet show reduced CSEgamma mRNA expression and protein abundance
cobalt-60 gamma radiation at doses of 14 Gy and 25 Gy decrease the cystathionine-gamma-lyase activity by 15.1% and 20.5%, respectively, and cystathionine-gamma-lyase mRNA expression by 29.3% and 38.2%, respectively
-
CSE activity and protein levels in the colonic tissue do not notably change in the mice with colitis
-
CSE expression and H2S production are increased during adipocyte differentiation, and the pattern of CSE mRNA expression is similar to that of CCAAT/enhancer-binding protein C/EBPbeta and C/EBPdelta, key regulators for adipogenesis. C/EBPbeta and gamma bind to the CCAAT box in CSE promoter and stimulate CSE gene transcription
CSE expression is significantly downregulated in patients with chronic kidney disease
CSE expression s lower, by 15.8%, 19.5% and 23.2%, following 24 h treatment with 0.1, 1 and 10 ng/ml transforming growth factor-beta1
-
CSEgamma expression is upregulated by pan-histone deacetylase inhibitors and by class II-specific HDAC inhibitors, but not by other class-specific inhibitors. The histone deacetylase 6 selective inhibitor tubacin and histone deacetylase 6-specific siRNA increase CSEgamma expression and block oxidized LDL-mediated reductions in endothelial CSEgamma expression and CSEgamma promoter activity
cys-16+ transcript levels in a activator/regulator CYS3-defective DELTAcys-3 regulatory mutant are present at a low level under either derepressing or repressing conditions
dexamethasone (0.001 mM) causes an about 85% decrease in CSE mRNA and 95% decrease in CSE protein levels, 1 mM NG-nitro-L-arginine methyl ester decreases lipopolysaccharide-induced CSE expression in macrophages
-
either the activity or protein expression of pancreatic CSE increase after the development of caerulein-induced pancreatitis in mice
-
enzyme expression levels are present only at a low level under sulfur sufficient (repressing) conditions
enzyme expression levels increase under sulfur limiting (derepressing) conditions
glutathione depletion causes a JNK and p38MAPK-mediated increase in expression of cystathionine-gamma-lyase. Expression of cystathionine-gamma-lyase is 1.5fold increased following incubation of the cells with diethylmaleate for 3 h. Co-incubation of C6 cells with diethylmaleate and the JNK-inhibitor, SP600125, abolishes the increase in expression of cystathionine-gamma-lyase that is observed in the presence of diethylmaleate alone
-
H2S fumigation stimulates the expression of drought associated genes. The enzyme is strongly induced by drought stress, with a maximum accumulation after 6 h, overview
higher rate of H2S production corresponds to an up-regulation of CSE expression in liver and kidney
-
human aortic endothelial cells exposed to oxidized LDL show reduced CSEgamma mRNA expression and protein abundance
livers from streptozotocin-treated type I diabetic rats have lower levels of enzyme protein expression, enzyme activity, reduced tissue H2S formation, and increased reactive oxygen species production compared with those of controls
mice that undergo 30 min of renal ischaemia and 24 h of reperfusion exhibit a significant increase in the expression of cystathionine gamma-lyase protein in the kidney
-
presence of homocysteine upregulates cystathionine gamma lyase but downregulates cystathionine beta synthase whereas H2S-donor Na2S/GYY4137 downregulates cystathionine gamma lyase but upregulates cystathionine beta. The Na2S-treatment downregulates specificity protein-1, an inducer for cystathionine gamma lyase, and upregulates microRNA miR-133a that targets specificity protein-1, and inhibits cardiomyocytes hypertrophy. In the homocysteine-treated cardiomyocytes, cystathionine beta synthase and miR-133a are downregulated and hypertrophy is induced
serum deprivation induces smooth muscle cell differentiation marker gene expressions and increases CSE expression and H2S production. The region between -226 to +140 base pair contains the core promoter for the CSE gene
-
the enzyme expression levels gradually increases in an age-dependent manner
the expression level and activity of cystathionine gamma-lyase is significantly decreased by methylglyoxal treatment (0.01-0.05 mM)
-
the level of CSE mRNA expression in liver are increased by hepatic ischemia-reperfusion
-
cys-16+ transcript levels in a activator/regulator CYS3-defective DELTAcys-3 regulatory mutant are present at a low level under either derepressing or repressing conditions
cys-16+ transcript levels in a activator/regulator CYS3-defective DELTAcys-3 regulatory mutant are present at a low level under either derepressing or repressing conditions
-
-
enzyme expression levels are present only at a low level under sulfur sufficient (repressing) conditions
enzyme expression levels are present only at a low level under sulfur sufficient (repressing) conditions
-
-
enzyme expression levels increase under sulfur limiting (derepressing) conditions
enzyme expression levels increase under sulfur limiting (derepressing) conditions
-
-
H2S fumigation stimulates the expression of drought associated genes. The enzyme is strongly induced by drought stress, with a maximum accumulation after 6 h, overview
H2S fumigation stimulates the expression of drought associated genes. The enzyme is strongly induced by drought stress, with a maximum accumulation after 6 h, overview
-
-
livers from streptozotocin-treated type I diabetic rats have lower levels of enzyme protein expression, enzyme activity, reduced tissue H2S formation, and increased reactive oxygen species production compared with those of controls
-
livers from streptozotocin-treated type I diabetic rats have lower levels of enzyme protein expression, enzyme activity, reduced tissue H2S formation, and increased reactive oxygen species production compared with those of controls
-
-
the enzyme expression levels gradually increases in an age-dependent manner
the enzyme expression levels gradually increases in an age-dependent manner
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
-
use of strain as adjunct starter in cheese making
medicine
nutrition
synthesis
additional information
agriculture
-
infection with Pyrenopeziza brassicae led to increased LCD activity
agriculture
enzyme is an antibacterial drug-target protein against Xanthomonas oryzae pv. oryzae. Bacterial blight caused by Xanthomonas oryzae pv. oryzae is the most destructive bacterial disease of rice
medicine
-
enzyme participates in hydrogen sulfide production in the oral cavity
medicine
-
enzyme participates in hydrogen sulfide production in the oral cavity
medicine
-
enzyme participates in hydrogen sulfide production in the oral cavity
medicine
-
enzyme participates in hydrogen sulfide production in the oral cavity
medicine
-
enzyme participates in hydrogen sulfide production in the oral cavity
medicine
-
enzyme participates in hydrogen sulfide production in the oral cavity
medicine
-
molecular basis of cystathioninuria, MIM 219500, revealed by mutations of enzyme
medicine
-
physiologic importance of increased expression and activity of enzyme during lactation
medicine
high doses of pyridoxine could be an effective therapy for cystathioninuric patients harboring the T67I mutation and be somewhat less effective in ameliorating the symptoms associated with the Q240E mutation
medicine
-
inhibition of CSE expression and reduction in formation of the pro-inflammatory component of H(2)S activity contributes to the anti-inflammatory effect of dexamethasone in endotoxic shock. Whether H(2)S plays a part in the anti-inflammatory effect of this steroid in other forms of inflammation such as arthritis or asthma warrants further study
medicine
inhibition of hydrogen sulfide synthesis attenuates chemokine production and protects mice against acute pancreatitis and associated lung injury
medicine
-
CSE is not associated with dextran sulfate sodium-induced colitis in mice
medicine
-
CSE is not associated with dextran sulfate sodium-induced colitis in mice
medicine
-
chronical treatment of rats with CGL inhibitor (DL)-propargylglycine or cystathionine beta-synthase inhibitor aminooxyacetic acid or a combination of both. Only the rats with combination therapy show a decrease in urinary sulfate excretion rate, which is associated with an increase in mean arterial pressure. Urine flow and sodium excretion are also increased in combination group as consequent to the increase in mean arterial pressure. Glomerular filtration rate does not alter due to these treatments, renal blood flow is lowered only in the combination group compared to the control group
medicine
-
cumulative administration of L-cysteine causes a dose-dependent decrease in the amplitude of spontaneous contractions in nonlabouring and labouring myometrium strips. L-cysteine at high concentration increases the frequency of spontaneous contractions and induces tonic contraction. These effects of L-cysteine are blocked by inhibitors of cystathionen beta-synthase and cystathionine gamma-lyase. Pretreatment of myometrium strips with glibenclamide, an inhibitor of ATP-sensitive potassium channels, abolishes the inhibitory effect of L-cysteine on spontaneous contraction amplitude. The effects of L-cysteine on the amplitude of spontaneous contractions and baseline muscle tone are less potent in labouring tissues than that in nonlabouring strips
medicine
-
covalent binding of enzyme to polyethylene glycol moieties reduces the specific activity from 59.71 U/mg of free enzyme to 48.71 U/mg, with a PEGylation yield of 81.5 and 70.7% modification of surface epsilon-amino groups. The pH stability does not change upon modification, and at 50 ° C, the thermal stability of PEG-CGL is increased by 40% in comparison to free CGL. By in vitro proteolysis, PEG-CGL retains more than 50% of its initial activity compared to less than 10% of the free-CGL for acid protease for 30 min. The biochemical and hematological responses of rabbits indicate nil toxicity of free and PEG-CGL
medicine
-
cystathionine-beta-synthase and cystathionine-gamma-lyase are expressed in the normal human colon. Expression is significantly decreased in the ganglionic and aganglionic bowel of patients with Hirschsprung Disease. Expression in smooth muscles, interstitial cells of Cajal, platelet-derived growth factor-alpha receptor-positive cells, enteric neurons and colonic epithelium is markedly decreased in Hirschsprung Disease specimens compared to controls
medicine
Aspergillus carneus KF723837
-
covalent binding of enzyme to polyethylene glycol moieties reduces the specific activity from 59.71 U/mg of free enzyme to 48.71 U/mg, with a PEGylation yield of 81.5 and 70.7% modification of surface epsilon-amino groups. The pH stability does not change upon modification, and at 50 ° C, the thermal stability of PEG-CGL is increased by 40% in comparison to free CGL. By in vitro proteolysis, PEG-CGL retains more than 50% of its initial activity compared to less than 10% of the free-CGL for acid protease for 30 min. The biochemical and hematological responses of rabbits indicate nil toxicity of free and PEG-CGL
-
nutrition
-
Lactobacillus fermentum is contained in the natural starter used for producing Parmesan cheese and as adventitious non-starter lactic acid bacteria. It also populates several Italian and Swiss cheeses. EC 4.4.1.1 is stable in the conditions of cheese ripening and may contribute to the biosynthesis of sulfur-containing compounds
nutrition
-
Lactobacillus fermentum is contained in the natural starter used for producing Parmesan cheese and as adventitious non-starter lactic acid bacteria. It also populates several Italian and Swiss cheeses. EC 4.4.1.1 is stable in the conditions of cheese ripening and may contribute to the biosynthesis of sulfur-containing compounds
-
additional information
-
H2S donors elicit pharmacological effect on ocular smooth muscle is of great interest and merits further investigation
additional information
-
H2S is a physiologic vasodilator and regulator of blood pressure
additional information
-
insulin release is impaired in diabetic animals and inhibition of abnormally increased endogenous pancreatic H2S production in diabetes may represent a novel avenue for diabetes treatment
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Release 2023.1 (January 2023)
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