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(DL)-homocysteine
H2S + ?
3-chloro-2-aminobutanoate
?
-
-
-
-
?
3-chloro-DL-alanine + H2O
NH3 + ?
-
-
-
?
alpha,beta-diaminopropionate
?
-
beta,gamma-elimination
-
-
?
beta-chloro-L-alanine + H2O
pyruvate + NH3 + HCl
-
-
-
-
?
beta-methylcystine
?
-
-
-
-
?
D-alanine + H2O
?
-
-
-
-
?
D-Cys + D-homoserine
D-cystathionine
-
-
-
?
D-Cys + L-homoserine
D-allocystathionine
DL-cystathionine
?
-
-
-
?
DL-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
DL-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
?
homocysteine
?
-
beta,gamma-elimination
-
-
?
L-alanine + H2O
?
-
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
L-Cys + D-homoserine
L-allocystathionine
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
L-cystathionine + H2O
2-oxobutyrate + L-cysteine + NH3
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
L-cystathionine + H2O
L-cysteine + ?
-
-
-
?
L-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
L-cysteine
H2S + NH3 + pyruvate
L-cysteine + H2O
H2S + pyruvate + NH3
L-cysteine + H2O
sulfide + NH3 + pyruvate
L-cysteine + L-cysteine
H2S + L-lanthionine
-
-
-
-
?
L-cysteine + L-cysteine
L-lanthionine + H2S
-
-
-
-
?
L-cystine + 2 H2O
2 NH3 + 2 pyruvate + 2 hydrogen sulfide
-
-
-
?
L-cystine + H2O
L-thiocysteine + pyruvate + NH3
L-cystine + H2O
NH3 + pyruvate + L-thiocysteine
L-cystine + H2O
pyruvate + NH3 + L-thiocysteine
-
-
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
-
-
-
-
?
L-djenkolic acid + H2O
NH3 + ?
L-homocysteine + H2O
H2S + ?
-
-
-
-
?
L-homocysteine + H2O
NH3 + 2-oxobutanoate + H2S
-
-
-
-
?
L-homocysteine + L-cysteine
L-cystathionine + H2S
-
-
-
-
?
L-homocysteine + L-homocysteine
L-homolanthionine + H2S
-
-
-
-
?
L-homocystine
?
-
-
-
-
?
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 + 2-mercaptopropionate
S-methylcarboxymethyl-L-homocysteine
L-homoserine + 3-mercaptopropionate
S-carboxyethyl-L-homocysteine
L-homoserine + 4-mercaptobutanoate
S-carboxy-n-propyl-L-homocysteine
-
14% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + D-homocysteine
meso-homolanthionine
L-homoserine + H2O
2-oxobutanoate + NH3 + H2O
L-homoserine + H2O
H2O + NH3 + 2-oxobutanoate
-
-
-
-
?
L-homoserine + H2O
NH3 + ?
-
-
-
?
L-homoserine + L-Cys
L-cystathionine
L-homoserine + L-homocysteine
L-homolanthionine
L-homoserine + thioglycerol
S-(2,3-dihydroxypropyl)-L-homocysteine
-
5% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + thioglycolate
S-carboxymethyl-L-homocysteine
L-methionine + H2O
NH3 + ?
L-serine + H2O
NH3 + ?
-
-
-
?
lanthionine + H2O
NH3 + ?
131% of activity compared to cystathionine
-
?
mixed disulfide of L-cystine and L-homocystine
?
-
-
-
-
?
O-acetyl-L-homoserine
?
-
-
-
-
?
O-acetyl-L-homoserine + H2O
NH3 + ?
-
-
-
?
O-acetyl-L-serine + H2O
acetate + pyruvate + NH3
-
-
-
-
?
O-succinyl-L-homoserine
?
-
decomposed most rapidly of all the above substrates
-
-
?
O-succinyl-L-homoserine + H2O
NH3 + ?
-
-
-
?
S-(2-aminoethyl)-L-cysteine + H2O
NH3 + pyruvate + cysteamine
-
-
-
?
S-methyl-L-cysteine + H2O
NH3 + pyruvate + methyl mercaptan
-
-
-
?
seleno-L-methionine
methylselenol + 2-oxobutyrate + NH3
-
-
-
-
?
additional information
?
-
(DL)-homocysteine
H2S + ?
-
-
-
-
?
(DL)-homocysteine
H2S + ?
-
-
-
-
?
beta-chloro-L-Ala
?
-
alpha,beta-elimination
-
-
?
beta-chloro-L-Ala
?
-
alpha,gamma-elimination
-
-
?
D-Cys + L-homoserine
D-allocystathionine
-
-
-
-
?
D-Cys + L-homoserine
D-allocystathionine
-
-
-
?
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
-
?
djenkolic acid
?
-
L-djenkolic acid
-
-
?
djenkolic acid
?
-
-
-
-
?
djenkolic acid
?
-
-
-
-
?
djenkolic acid
?
-
beta,gamma-elimination
-
-
?
djenkolic acid
?
-
alpha,beta-elimination
-
-
?
djenkolic acid
?
-
alpha-gamma-elimination
-
-
?
DL-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
-
?
DL-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
-
?
DL-vinylglycine
?
-
alpha,beta-elimination
-
-
?
DL-vinylglycine
?
-
alpha,gamma-elimination
-
-
?
L-Cys
H2S + NH3 + pyruvate
-
alpha,beta-elimination
-
-
?
L-Cys
H2S + NH3 + pyruvate
-
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
-
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
-
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
-
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
-
alpha,beta-elimination
-
-
?
L-Cys
H2S + NH3 + pyruvate
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
-
-
-
?
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-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
-
?
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-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
?
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-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
?
L-cystathionine + H2O
?
-
-
-
-
?
L-cystathionine + H2O
?
-
-
-
-
?
L-cystathionine + H2O
?
-
-
-
-
?
L-cystathionine + H2O
?
-
-
-
-
?
L-cystathionine + H2O
?
-
-
-
-
?
L-cystathionine + H2O
?
-
beta,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
-
-
-
-
r
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
-
-
-
?
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
-
-
-
r
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 + 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
-
-
-
?
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
-
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
-
r
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
-
-
-
-
?
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
-
-
-
?
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-cysteine + NH3 + 2-oxobutanoate
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
?
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
-
-
-
-
?
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-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
?
L-cysteine
H2S + NH3 + pyruvate
-
best substrate
-
?
L-cysteine
H2S + NH3 + pyruvate
-
best substrate
-
?
L-cysteine
H2S + NH3 + pyruvate
-
-
-
-
?
L-cysteine
H2S + NH3 + pyruvate
-
-
-
-
?
L-cysteine
H2S + NH3 + pyruvate
-
-
-
-
?
L-cysteine
H2S + NH3 + pyruvate
poor substrate
-
-
?
L-cysteine
H2S + NH3 + pyruvate
poor substrate
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
690781, 691828, 691972, 692207, 693818, 693936, 694398, 695079, 708133, 708300, 708411, 708627, 709212, 709676, 709778, 710627 -
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cystine
?
-
alpha,beta-elimination
-
-
?
L-cystine
?
-
alpha,beta-elimination
-
-
?
L-cystine
?
-
alpha,gamma-elimination
-
-
?
L-cystine + H2O
L-thiocysteine + pyruvate + NH3
-
-
-
-
?
L-cystine + H2O
L-thiocysteine + pyruvate + NH3
-
-
-
-
?
L-cystine + H2O
NH3 + ?
133% of activity compared to cystathionine
-
?
L-cystine + H2O
NH3 + ?
-
-
-
?
L-cystine + H2O
NH3 + pyruvate + L-thiocysteine
-
-
-
?
L-cystine + H2O
NH3 + pyruvate + L-thiocysteine
-
-
-
-
?
L-cystine + H2O
NH3 + pyruvate + L-thiocysteine
-
-
-
-
?
L-djenkolic acid + H2O
NH3 + ?
24% of activity compared to cystathionine
-
?
L-djenkolic acid + H2O
NH3 + ?
-
-
-
?
L-homocysteine
?
-
-
-
?
L-homocysteine
?
-
-
-
-
?
L-homoserine
?
-
-
-
-
?
L-homoserine
?
-
beta,gamma-elimination
-
-
?
L-homoserine
?
-
alpha,gamma-elimination
-
-
?
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
-
-
-
?
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
-
-
-
?
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 + H2O
2-oxobutanoate + NH3 + H2O
-
-
-
?
L-homoserine + H2O
2-oxobutanoate + NH3 + H2O
-
-
-
-
?
L-homoserine + H2O
2-oxobutanoate + NH3 + H2O
-
-
-
-
?
L-homoserine + L-Cys
L-cystathionine
-
-
-
?
L-homoserine + L-Cys
L-cystathionine
-
-
-
?
L-homoserine + L-Cys
L-cystathionine
-
-
-
?
L-homoserine + L-homocysteine
L-homolanthionine
-
-
-
-
?
L-homoserine + L-homocysteine
L-homolanthionine
-
-
-
?
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
-
-
-
-
?
L-homoserine + thioglycolate
S-carboxymethyl-L-homocysteine
-
gamma-replacement reaction, 69% of the activity with L-homocysteine and L-Cys
-
?
L-Met
methanethiol + ?
-
alpha,gamma-elimination
-
?
L-Met
methanethiol + ?
-
-
-
-
?
L-methionine + H2O
NH3 + ?
-
-
-
?
L-methionine + H2O
NH3 + ?
-
-
-
?
Lanthionine
?
-
-
-
-
?
Lanthionine
?
-
beta,gamma-elimination
-
-
?
Lanthionine
?
-
meso-lanthionine
-
-
?
Lanthionine
?
-
L-lanthionine
-
-
?
Lanthionine
?
-
alpha,beta-elimination
-
-
?
Lanthionine
?
-
alpha,gamma-elimination
-
-
?
Lanthionine
?
-
DL-lanthionine
-
-
?
meso-cystine
?
-
-
-
-
?
S-aminoethyl-L-Cys
?
-
-
-
-
?
S-aminoethyl-L-Cys
?
-
-
-
-
?
S-aminoethyl-L-Cys
?
-
-
-
-
?
S-methyl-L-Cys
?
-
-
-
-
?
S-methyl-L-Cys
?
-
alpha,beta-elimination
-
-
?
additional information
?
-
-
enzyme activity is required for high-level cephalosporin biosynthesis but not for low-level production of the antibiotic
-
?
additional information
?
-
-
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
?
-
-
no activity with L-methionine
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
L-cystathionine + H2O
2-oxobutyrate + L-cysteine + NH3
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
L-cysteine + H2O
H2S + pyruvate + NH3
L-cysteine + H2O
sulfide + NH3 + pyruvate
L-cystine + H2O
pyruvate + NH3 + L-thiocysteine
-
-
-
-
?
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
-
-
-
?
additional information
?
-
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-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
-
r
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
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
-
-
-
-
r
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
-
-
-
-
r
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
-
-
-
?
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
H2S + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
additional information
?
-
-
enzyme activity is required for high-level cephalosporin biosynthesis but not for low-level production of the antibiotic
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(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
1,10-phenanthroline
-
2 mM, 20% inhibition
1-nitroso-2-naphthol-3,6-disulfonic acid
-
2 mM, 55% inhibition
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
2-(prop-2-yn-1-ylamino)acetic acid
-
-
3-methyl-2-benzothiazolinone
-
31% residual activity at 5 mM
3-Methyl-2-benzothiazolinone hydrazone
4-chloromercuribenzoate
-
-
5,5'-dithiobis(2-nitrobenzoate)
6-diazo-5-oxonorleucine
-
-
8-Hydroxyquinoline-5-sulfonic acid
-
2 mM, 13% inhibition
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
AgNO3
-
alpha,beta-elimination L-homoserine
alpha-amino-gamma-aminooxybutanoate
-
-
aminoethoxyvinylglycine
-
-
beta,beta,beta-trifluoroalanine
beta-cyano-L-Ala
-
alpha,beta-elimination L-homoserine
beta-trifluoromethyl-D,L-Ala
-
i.e. 2-amino-4,4,4-trifluorobutanoate
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
DL-Penicillamine
-
3% residual activity at 5 mM
EDTA
-
2 mM, 13% inhibition
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
iodoacetamide
-
22% residual activity at 2.5 mM
Isonicotinic acid hydrazide
-
-
L-aminoethoxyvinylglycine
-
-
L-beta-oxalyl amino-L-alanine
-
inhibition only after long exposure
N-prop-2-yn-1-ylglycine
-
-
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
Sodium cyanide
-
alpha,beta-elimination, 1 mM, 82% inhibition
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
3-Methyl-2-benzothiazolinone hydrazone
-
-
3-Methyl-2-benzothiazolinone hydrazone
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
8 of the 12 -SH groups in native enzyme react reversibly. Cystathionine at high concentrations, partially relieves the inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
-
aminooxyacetic acid
-
-
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,beta,beta-trifluoroalanine
-
-
beta,beta,beta-trifluoroalanine
-
irreversible
Beta-cyano-L-alanine
-
-
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
Beta-cyanoalanine
-
-
Beta-cyanoalanine
-
reversible inhibitor of CSE
cycloserine
-
DL-cycloserine
cycloserine
-
partially competitive
cycloserine
-
D-cycloserine
Cys
-
-
Cys
-
the regulatory site of the enzyme is specific for L-Cys
Cys
-
above 10 mM, inhibits replacement reaction with L-homoserine and L-Cys
DL-propargylglycine
-
-
DL-propargylglycine
-
irreversible inhibitor of CSE
DL-propargylglycine
-
irreversible inhibitor
DL-propargylglycine
an irreversible enzyme inhibitor, molecular mechanism of DL-propargylglycine action in vivo
DL-propargylglycine
-
2% residual activity at 5 mM
DL-propargylglycine
-
elevates blood pressure
DL-propargylglycine
-
irreversible inhibitor of CSE
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
DL-propargylglycine
-
irreversible inhibitor of CSE
DL-propargylglycine
-
irreversible inhibitor of CSE
DL-propargylglycine
-
selective inhibitor of cystathionine gamma-lyase
Hg2+
-
strong
Hg2+
-
HgCl2, alpha,beta-elimination L-homoserine
hydroxylamine
-
-
hydroxylamine
-
alpha,beta-elimination of L-homoserine
L-cysteine
-
0.4 mM, 6% residual activity
L-cysteine
-
substrate inhibition mainly due to removal of cofactor
L-cysteine
-
inhibits alpha,gamma elimination activity
N-ethylmaleimide
-
81% residual activity at 5 mM
NaCl
-
5% w/v
NaCl
-
59% residual activity at 5 mM
PCMB
-
0.05 mM, inhibition is partly relieved by 0.2 mM 2,3-dimercaptopropanol
PCMB
-
alpha,beta-elimination L-homoserine
Penicillamine
-
D-penicillamine; L-penicillamine
Penicillamine
-
D-penicillamine; L-penicillamine
Penicillamine
-
alpha,beta-elimination of L-homoserine; D-penicillamine; L-penicillamine
phenylhydrazine
-
2.8% residual activity at 5 mM
phenylhydrazine
-
alpha,beta-elimination L-homoserine as substrate
propargylglycine
-
-
propargylglycine
-
10 mM inhibits testosterone induced H2S biosynthesis
propargylglycine
-
alpha,beta-elimination L-homoserine
Semicarbazide
-
-
Semicarbazide
-
11% residual activity at 5 mM
Semicarbazide
-
alpha,beta-elimination L-homoserine as substrate
trifluoro-Ala
-
-
trifluoro-Ala
-
trifluoro-D,L-Ala
Zn2+
-
0.1 mM, weak
Zn2+
-
ZnCl2, alpha,beta-elimination L-homoserine
additional information
-
no or poor inhibition by methylselenocysteine, D-cycloserine, pargyline, and parsalmide
-
additional information
-
no inhibition by 4-hydroxybutyrate
-
additional information
-
not inhibitory: EDTA
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.153 - 1.417
(DL)-homocysteine
28.41
3-chloro-DL-alanine
-
pH 8.0, 37°C
2.39
beta-chloro-L-Ala
-
-
0.1 - 3.2
beta-chloro-L-alanine
0.51 - 1.5
djenkolic acid
3.27 - 3.4
DL-cystathionine
0.204 - 25.5
L-cystathionine
0.7 - 5.3
O-acetyl-L-serine
2.75
S-(2-aminoethyl)-L-cysteine
-
pH 8.0, 37°C
13.13
S-methyl-L-cysteine
-
pH 8.0, 37°C
additional information
additional information
-
1.153
(DL)-homocysteine
-
pH 8.0, 37°C
1.417
(DL)-homocysteine
-
pH 8.0, 37°C
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
0.51
djenkolic acid
wild-type, pH 9.0, 40°C
0.86
djenkolic acid
mutant N360S, pH 9.0, 40°C
1.5
djenkolic acid
mutant S77A, pH 9.0, 40°C
3.27
DL-cystathionine
-
pH 8.0, 37°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
0.029
L-Cys
-
pH 8.0, 37°C
0.069
L-Cys
-
pH 8.0, 37°C
0.204
L-cystathionine
-
-
0.232
L-cystathionine
-
pH 8.0, 37°C
0.236
L-cystathionine
-
pH 8.0, 37°C
0.4
L-cystathionine
for variant S403
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
0.6
L-cystathionine
for mutant T67I
0.6
L-cystathionine
for variant I403
0.71
L-cystathionine
-
pH 7.2, 25°C, recombinant wild-type enzyme
0.72
L-cystathionine
for mutant Q240E
0.76
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48A
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
0.87
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48D
0.9
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48Q
0.9
L-cystathionine
wild-type, pH 9.0, 40°C
1.11
L-cystathionine
-
mutant enzyme E48D, in 50 mM potassium phosphate, pH 7.8, at 25°C
2.4
L-cystathionine
mutant S77A, pH 9.0, 40°C
5.2
L-cystathionine
-
mutant enzyme E333A, in 50 mM potassium phosphate, pH 7.8, at 25°C
6.1
L-cystathionine
mutant N360S, pH 9.0, 40°C
8.7
L-cystathionine
-
pH 7.6, 37°C
10.6
L-cystathionine
-
pH 7.6, 37°C
11.1
L-cystathionine
-
pH 7.6, 37°C
11.2
L-cystathionine
-
pH 7.6, 37°C
11.8
L-cystathionine
-
pH 7.6, 37°C
12
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E333A
12
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E333D
13
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E333Q
25.5
L-cystathionine
-
pH 7.6, 37°C
0.09
L-cysteine
-
pH 7.2, 25°C, recombinant wild-type enzyme
0.11
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48A
0.18
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48Q
0.21
L-cysteine
wild-type, pH 9.0, 40°C
0.4
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48D
0.4
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48Q/E333Q
0.4
L-cysteine
mutant N360S, pH 9.0, 40°C
0.5
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48A/E333A
0.5
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48D/E333D
0.62
L-cysteine
-
pH 8.0, 37°C
0.68
L-cysteine
-
pH 7.6, 37°C
0.7
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E333Q
0.75
L-cysteine
-
pH 7.6, 37°C
0.76
L-cysteine
-
mutant enzyme E339Y, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.88
L-cysteine
-
pH 7.6, 37°C
1.08
L-cysteine
-
pH 7.6, 37°C
1.16
L-cysteine
-
pH 7.6, 37°C
1.2
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E333A
1.8
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E333D
1.9
L-cysteine
-
wild type enzyme, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
2.46
L-cysteine
-
pH 7.6, 37°C
3.3
L-cysteine
-
mutant enzyme E339K, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
3.4
L-cysteine
for variant I403
3.5
L-cysteine
for variant S403
4.1
L-cysteine
for mutant T67I
7.7
L-cysteine
-
mutant enzyme E339A, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.032
L-cystine
-
-
1.29
L-cystine
-
pH 8.0, 37°C
5.4
L-homocysteine
for variant S403
7
L-homocysteine
for variant I403
8
L-homocysteine
for mutant T67I
0.7
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48D/E333D
0.9
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E333D
1.4
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48D
1.5
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48A
1.5
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48Q/E333Q
2.2
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E333A
2.5
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant wild-type enzyme
2.9
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48A/E333A
4.4
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48Q
5.3
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E333Q
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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.
0.19 - 0.24
djenkolic acid
0.11 - 0.13
DL-cystathionine
0.02 - 7.5
L-cystathionine
0.82 - 3.7
L-homocysteine
0.0035 - 0.0142
O-acetyl-L-serine
0.19
djenkolic acid
mutant N360S, pH 9.0, 40°C
0.22
djenkolic acid
mutant S77A, pH 9.0, 40°C
0.24
djenkolic acid
wild-type, pH 9.0, 40°C
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
0.02
L-cystathionine
for mutante Q240E
0.24
L-cystathionine
mutant N360S, pH 9.0, 40°C
0.39
L-cystathionine
-
mutant enzyme E48F, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.45
L-cystathionine
for mutante T67I
0.48
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E333Q
0.54
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48A
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
0.7
L-cystathionine
mutant S77A, pH 9.0, 40°C
0.76
L-cystathionine
-
mutant enzyme E48D, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.78
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E333A
0.9
L-cystathionine
-
native wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.98
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E333D
1.29
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48Q
1.4
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48D
1.51
L-cystathionine
-
pH 7.2, 25°C, recombinant wild-type enzyme
1.7
L-cystathionine
for variante S403
1.81
L-cystathionine
-
His-tagged recombinant wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
1.9
L-cystathionine
for variante I403
2
L-cystathionine
wild-type, pH 9.0, 40°C
0.007
L-cysteine
mutant N360S, pH 9.0, 40°C
0.009
L-cysteine
wild-type, pH 9.0, 40°C
0.029
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48D/E333D
0.09
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48A
0.11
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48A/E333A
0.12
L-cysteine
-
wild type enzyme, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.15
L-cysteine
-
pH 7.2, 25°C, recombinant wild-type enzyme
0.16
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48Q/E333Q
0.18
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48Q
0.24
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E333D
0.3
L-cysteine
for mutante T67I
0.32
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48D
0.34
L-cysteine
-
mutant enzyme E339K, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.5
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E333Q
0.67
L-cysteine
for variante I403
0.67
L-cysteine
for variante S403
0.76
L-cysteine
-
mutant enzyme E339Y, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
1.3
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E333A
1.44
L-cysteine
-
mutant enzyme E339A, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.82
L-homocysteine
for mutante T67I
3.5
L-homocysteine
for variante S403
3.7
L-homocysteine
for variante I403
0.0035
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48D/E333D
0.0045
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E333D
0.0047
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48A/E333A
0.0053
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48D
0.0058
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant 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
0.0102
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E333Q
0.0124
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48Q
0.0142
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.15 - 0.47
djenkolic acid
0.029 - 0.04
DL-cystathionine
0.0037 - 4.3
L-cystathionine
0.0016 - 0.01
O-acetyl-L-serine
0.15
djenkolic acid
mutant S77A, pH 9.0, 40°C
0.22
djenkolic acid
mutant N360S, pH 9.0, 40°C
0.47
djenkolic acid
wild-type, pH 9.0, 40°C
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
0.036
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E333Q
0.039
L-cystathionine
mutant N360S, pH 9.0, 40°C
0.065
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E333A
0.082
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E333D
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
0.29
L-cystathionine
mutant S77A, pH 9.0, 40°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
0.71
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48A
0.82
L-cystathionine
-
mutant enzyme E48A, in 50 mM potassium phosphate, pH 7.8, at 25°C
1.4
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48Q
1.59
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48D
1.98
L-cystathionine
-
native wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
2.1
L-cystathionine
-
pH 7.2, 25°C, recombinant wild-type enzyme
2.2
L-cystathionine
wild-type, pH 9.0, 40°C
4.3
L-cystathionine
-
His-tagged recombinant wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.018
L-cysteine
mutant N360S, pH 9.0, 40°C
0.043
L-cysteine
wild-type, pH 9.0, 40°C
0.06
L-cysteine
-
wild type enzyme, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.06
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48D/E333D
0.11
L-cysteine
-
mutant enzyme E339K, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.13
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E333D
0.19
L-cysteine
-
mutant enzyme E339A, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.21
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48A/E333A
0.31
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48Q/E333Q
0.43
L-cysteine
-
mutant enzyme E339Y, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C
0.49
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E333Q
0.72
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48D
0.8
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48A
0.81
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E333A
1.02
L-cysteine
-
pH 7.2, 25°C, recombinant mutant E48Q
1.7
L-cysteine
-
pH 7.2, 25°C, recombinant wild-type enzyme
0.0016
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48A/E333A
0.0019
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E333Q
0.0026
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E333A
0.0028
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48Q
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 E333D
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
0.01
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
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
-
-
brenda
-
-
brenda
-
mainly expressed in airway and vascular smooth muscle cells in rat lung tissue
brenda
-
cultured human aorta smooth muscle cell
brenda
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
enzyme expression in numerous oval or polygonal cells
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
high expression
brenda
-
whole cells, cell lysate of a culture broth, cell wall of a subcellular fraction
brenda
-
-
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
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
CSE is localized in the muscular trabeculae and the smooth-muscle component of the penile artery
brenda
-
culture broth
brenda
-
only in the anterior- and the postero-lateral areas of the body
brenda
-
-
brenda
-
-
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
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
in neurons and nerve fibers of the lateral nerve cords immediately behind the ventral ganglia
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
smooth muscle cells
brenda
-
brenda
-
-
brenda
-
pregnant myometrium, primarily localized to smooth muscle cells of pregnant myometrium
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
peripheral blood mononuclear cells, PBMC, isolated from healthy subjects and type 1 diabetic patients
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
primarily localized to smooth muscle cells of pregnant myometrium
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
a pro-monocytic cell line
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
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
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
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
tail
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
predominantly localized to the endothelial layer of blood vessels
brenda
-
with a decreasing activity in tail artery, aorta and mesenteric arteries
brenda
-
mainly in the ventral ganglia
brenda
-
-
brenda
-
activity in human brain is 100fold higher than that observed in mouse brain
brenda
-
-
brenda
-
acitvity only 1% of activity in liver
brenda
-
in the brain, where CSE levels are low, localizations are predominantly in white matter
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
enzyme activity remains low during all stages of development
brenda
-
-
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
-
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
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only in adult tissue, not detectable in fetal, premature and full-term neonatal liver
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34502, 664289, 664290, 672489, 675074, 676159, 693730, 707582, 708300, 709608, 710078 brenda
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5584, 34486, 34488, 34490, 34491, 34492, 34493, 34494, 34495, 34496, 34498, 34500, 34501, 672489, 690352, 690781, 693818, 694398, 708300, 709778, 721432 brenda
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high enzyme activity from late foetal life to maturity
brenda
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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)
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of type 1 diabetic rats
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of type 1 diabetic rats
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mainly expressed in airway and vascular smooth muscle cells in rat lung tissue
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of lateral nerve cord and in the area of the cell bodies
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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)
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only trace activity
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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
high expression
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high expression
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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
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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
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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
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the enzyme expression levels gradually increases in an age-dependent manner, expression profiling, overview
brenda
additional information
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the enzyme expression levels gradually increases in an age-dependent manner, expression profiling, overview
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brenda
additional information
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immunohistochemic analysis
brenda
additional information
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no expression in white muscle
brenda
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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
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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
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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
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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
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metabolism
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CSE is a key enzyme in the pathway of cystathionine metabolism to produce endogenous H2S
metabolism
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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
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the enzyme is involved in H2S biosynthesis
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
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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
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physiological function
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CSE activity may contribute to butyrate-stimulated H2S production in WiDr cells
physiological function
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DES1 from Arabidopsis is an L-Cys desulfhydrase involved in maintaining Cys homeostasis, mainly at late developmental stages or under environmental perturbations
physiological function
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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
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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
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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
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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
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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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E339K
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the mutant shows increased catalytic efficiency compared to the wild type enzyme
E339Y
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the mutant shows increased catalytic efficiency compared to the wild type enzyme
E59N/R119L/E339V
mutant engineered as an L-Met-degrading enzyme based on the human cystathionine-gamma-lyase
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
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
T311I
the mutant shows wild type activity
Y114F
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the mutation leads to significant increase in the production of H2S by CSE
E333D
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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
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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
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the mutation leads to 30fold reduction of kcat/Km for L-cystathionine
E48A/E333A
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site-directed mutagenesis of the active-site residues, pH optimum 8.4-9.2
E48D/E333D
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site-directed mutagenesis of the active-site residues, pH optimum 7.6-8.4
E48F
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the mutation leads to about 9fold reduction of kcat/Km for L-cystathionine
E48Q
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site-directed mutagenesis of the active-site residue, pH optimum 7.4-8.2
E48Q/E333Q
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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
S77A
kinetics are similar to wild-type
S77E
complete loss of activity with cystathionine
N360S
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mutation does not alter enzyme conformation, but leads to a 56fold decrease in catalyic efficiency for L-cystathionine
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S77A
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kinetics are similar to wild-type
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S77E
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complete loss of activity with cystathionine
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K238A
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mutant with complete loss of lyase and racemase activity
Y123F
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mutant with decreased activity
Y123F/Y124F
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mutant with decreased activity
Y124F
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mutant with 50% of kcat for transamination of L- and D-alanine
Y64A
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mutant with decreased PLP binding affinity
D187A
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0.5% of wild-type activity
D187A
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the mutation results in a loss of enzyme activity
E339A
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the mutant demonstrates an approximately 6fold enhancement in H2S production
E339A
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about 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
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activity similar to wild-type
E349A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
E349A
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the mutant displays enzyme activity comparable to that for wild type enzyme
K212A
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the mutation results in a loss of enzyme activity
K212A
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1.3% of wild-type activity, residue involved in binding of pyridoxal 5'-phosphate
R375A
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2% of wild-type activity
R375A
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the mutation results in a loss of enzyme activity
R62A
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3% of wild-type activity
R62A
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the mutation results in a loss of enzyme activity
S209A
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activity similar to wild-type
S209A
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the mutant displays enzyme activity comparable to that for wild type enzyme
T189A
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0.5% of wild-type activity
T189A
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the mutation results in a loss of enzyme activity
T211A
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activity similar to wild-type
T211A
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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
site-directed mutagenesis
Y114A
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the mutation results in a loss of enzyme activity
Y114A
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3% of wild-type activity, residue involved in binding of pyridoxal 5'-phosphate
Y60A
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13% of wild-type activity
Y60A
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the mutation results in a severe decrease of enzyme activity
Y60A
site-directed mutagenesis, inactive mutant, which cannot provide antioxidative activity
E333A
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the mutation leads to 30fold reduction of kcat/Km for L-cystathionine
E333A
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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
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the mutation leads to about 6fold reduction of kcat/Km for L-cystathionine
E48A
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site-directed mutagenesis of the active-site residue, pH optimum 7.6-8.4
E48D
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the mutation leads to about 5fold reduction of kcat/Km for L-cystathionine
E48D
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site-directed mutagenesis of the active-site residue, pH optimum 7.07.8
additional information
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gene disruption mutants, lower cephalosporin production in Shens defined fermentation medium supplemented with methionine, but not in the same medium without methionine
additional information
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gene disruption mutants, lower cephalosporin production in Shens defined fermentation medium supplemented with methionine, but not in the same medium without methionine
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additional information
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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
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various Aspergillus nidulans mutant strains (sconB, metR, metG, mecB, cysB)
additional information
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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
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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
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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
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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
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additional information
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CSE-/- mice and CSE-/+ mice, mice genetically deficient in this enzyme display marked hypertension, comparable to that of eNOS-/- mice
additional information
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enzyme silencing by CSE-specific siRNA
additional information
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enzyme silencing by CSE-specific siRNA
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additional information
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pH optima of the mutant enzymes vary from wild-type enzyme, overview
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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
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aortas from atherogenic apolipoprotein E knockout mice fed a high-fat diet show reduced CSEgamma mRNA expression and protein abundance
butyrate significantly increases CSE protein expression
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butyrate upregulates CSE expression
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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
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CSE activity and protein levels in the colonic tissue do not notably change in the mice with colitis
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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
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CSE mRNA and protein expression are upregulated by S-propargyl-cysteine
-
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 expression of CSE is increased by NaHS
-
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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analysis
-
use in biosensor for measurement of L-cysteine
biotechnology
-
use of strain as adjunct starter in cheese making
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
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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
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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
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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
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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
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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
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nutrition
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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
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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
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synthesis
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effective at the end of trans-sulfuration pathway
synthesis
effective at the end of trans-sulfuration pathway
synthesis
effective at the end of trans-sulfuration pathway
synthesis
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effective in detoxification and biotransformation of Se
synthesis
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effective in metabolism of Se compounds
additional information
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H2S donors elicit pharmacological effect on ocular smooth muscle is of great interest and merits further investigation
additional information
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H2S is a physiologic vasodilator and regulator of blood pressure
additional information
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H2S might be a novel insulin resistance regulator
additional information
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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