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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
- beta-synthase
- sulfur
- nahs
- homocysteine
- pyridoxal
-
transsulfuration
- propargylglycine
- dl-propargylglycine
-
gasotransmitter
-
sulfur-containing
- sulfurtransferase
- taurine
-
gaseous
- hydrosulfide
- cystathionine-beta-synthase
- 3-mercaptopyruvate
- ppg
-
h2s-generating
- o-acetylserine
- rhodanese
-
adenosyltransferase
-
beta-lyase
-
h2s-producing
- l-methionine
-
vasorelaxation
-
desulfuration
- treponema
- glibenclamide
- persulfide
- medicine
- hyperhomocysteinemia
- hypotaurine
- denticola
- alpha-ketobutyrate
- l-cystine
-
gamma-synthase
-
s-sulfhydration
-
cysteinesulfinate
- synthesis
- agriculture
- biotechnology
- cys3
- nutrition
-
h2s-induced
-
sulfhydrylase
- l-homoserine
-
cowden
- analysis
-
aldimine
-
remethylation
-
aminooxyacetic
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
cystathionine gamma-lyase, cystathionase, gamma-cystathionase, cystathionine-gamma-lyase, cs-like, cystalysin, cysteine desulfhydrase, l-cysteine desulfhydrase, cystathionine gamma lyase, prb-ra, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AFUA_8G04340
cgl
CSE
CSEgamma
CTH
cystathionase
cystathionine gamma lyase
cystathionine gamma-lyase
cystathionine-gamma-lyase
cysteine desulfhydrase
gamma-cystathionase
human cystathionine-gamma-lyase
pyridoxal-5'-phosphate (PLP)-dependent enzyme
LCD
TGME49_112930
cgl
CGL variant S403 and I403, polymorphic variants at amino acid residues 403
CSE
-
-
CSE
-
-
CSE
-
-
cystathionine-gamma-lyase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 + 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-cystathionine
L-homocysteine + pyruvate + NH3
-
-
-
?
L-cystathionine
L-homocysteine + pyruvate + NH3
-
alpha,beta-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
-
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 + 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-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 + 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
?
-
-
hydrogen sulfide is a gas signalling molecule which is produced endogenously from L-cysteine
-
?
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 responsible for amino acid catabolism
-
?
additional information
?
-
-
enzyme responsible for amino acid catabolism
-
?
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
?
-
-
cysteine desulfhydrase in Rhodobacter sphaeroides can produce sulfide under aerobic conditions and precipitate metal sulfide complexes on the cell wall
-
?
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-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
?
-
-
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
?
-
-
cysteine desulfhydrase in Rhodobacter sphaeroides can produce sulfide under aerobic conditions and precipitate metal sulfide complexes on the cell wall
-
-
?
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY