Information on EC 4.4.1.1 - cystathionine gamma-lyase

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

EC NUMBER
COMMENTARY
4.4.1.1
-
RECOMMENDED NAME
GeneOntology No.
cystathionine gamma-lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-aminobut-2-enoate = 2-iminobutanoate
show the reaction diagram
spontaneous
-
-
-
2-iminobutanoate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
spontaneous
-
-
-
L-cystathionine + H2O = L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
mechanism
-
L-cystathionine + H2O = L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
mechanism
A2RM21
L-cystathionine + H2O = L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
the active site consists of two subsites. One recognizes the L-form of amino acids and the other shows affinity for thiol compounds with a carbonyl group
-
L-cystathionine + H2O = L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
overall reaction
-
-
-
L-cystathionine = L-cysteine + 2-aminobut-2-enoate
show the reaction diagram
(1a)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alpha,beta-elimination
-
-
alpha,gamma-elimination
-
-
elimination
-
-
of H2S or RSH, C-S bond cleavage
-
transamination
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Cysteine and methionine metabolism
-
-
cysteine metabolism
-
-
Glycine, serine and threonine metabolism
-
-
Metabolic pathways
-
-
Selenocompound metabolism
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cgl
P32929
CGL variant S403 and I403, polymorphic variants at amino acid residues 403
cgl
B3TNN8 and B3TNN9
-
cgl
Lactobacillus reuteri BR11
-
-
-
cgl
E9AFE7
-
CGL like protein
Q5H4T8
-
CSE
P32929
-
CSE
Q8VCN5
-
CSE
Mus musculus C57/BL6
-
-
-
CSE
-
H2S-synthesizing enzyme
CSE
Q9EQS4
-
CSE
Rattus norvegicus Sprague-Dawley
-
-
-
CTH
P32929
-
cystalysin
-
-
-
-
cystathionase
-
-
-
-
cystathionase
-
-
cystathionase
P32929
-
cystathioninase
-
-
-
-
cystathionine beta/gamma-lyase
B3TNN8 and B3TNN9
-
cystathionine gamma lyase
-
-
cystathionine gamma lyase
-
-
cystathionine gamma lyase
-
-
cystathionine gamma lyase
-
-
cystathionine gamma-lyase
-
-
-
-
cystathionine gamma-lyase
-
-
cystathionine gamma-lyase
B2LXT6
-
cystathionine gamma-lyase
-
-
cystathionine gamma-lyase
-
-
cystathionine gamma-lyase
-
-
cystathionine gamma-lyase
-
-
cystathionine gamma-lyase
-
-
cystathionine gamma-lyase
Lactobacillus reuteri BR11
-
-
-
cystathionine gamma-lyase
-
-
cystathionine gamma-lyase
-
-
cystathionine gamma-lyase
Q8VCN5
-
cystathionine gamma-lyase
-
-
cystathionine gamma-lyase
-
-
cystathionine gamma-lyase
-
-
cystathionine gamma-lyase
P31373
-
cystathionine gamma-lyase
-
-
cystathionine gamma-lyase-like protein
Q5H4T8
-
cystathionine-gamma-lyase
-
-
cystathionine-gamma-lyase
-
-
cystathionine-gamma-lyase
Mus musculus C57/BL6
-
-
-
cystathionine-gamma-lyase
-
-
cysteine desulfhydrase
-
-
-
-
cysteine desulfhydrase
-
-
cysteine desulfhydrase
-
-
cysteine desulfhydrase
-
-
cysteine desulfhydrase
-
-
cysteine desulfhydrase
-
-
cysteine desulfhydrase
-
-
cysteine desulfhydrase
-
-
cysteine lyase
-
-
-
-
cystine desulfhydrase
-
-
-
-
dehydratase, homoserine
-
-
-
-
desulfhydrase, cysteine
-
-
-
-
EC 4.2.1.15
-
-
formerly
-
gamma-CTL
-
-
-
-
gamma-CTLase
P31373
-
gamma-cystathionase
-
-
-
-
gamma-cystathionase
-
-
gamma-cystathionase
Q96VU7
-
gamma-cystathionase
Neurospora crassa 74OR23-1a
Q96VU7
-
-
hCSE
-
-
homoserine deaminase
-
-
-
-
homoserine deaminase-cystathionase
-
-
-
-
homoserine dehydratase
-
-
-
-
human cystathionine-gamma-lyase
P32929
pyridoxal-5'-phosphate (PLP)-dependent enzyme
L-Cys desulfhydrase
-
-
L-cysteine desulfhydrase
-
-
L-cysteine desulphydrase
-
-
L-cysteine-desulfhydrase
-
-
LCD
Arabidopsis thaliana Col-0
Q9M1R1
-
-
lyase, cystathionine gamma-
-
-
-
-
PRB-RA
-
-
-
-
Probasin-related antigen
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9012-96-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acremonium chrysogenum C10
C10
-
-
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
UniProt
Manually annotated by BRENDA team
infected with Pyrenopeziza brassicae
-
-
Manually annotated by BRENDA team
Northern Chinese Han population
-
-
Manually annotated by BRENDA team
two isoforms
SwissProt
Manually annotated by BRENDA team
strain ATCC 334
B3TNN8 and B3TNN9
UniProt
Manually annotated by BRENDA team
Lactobacillus fermentum DT41
DT41
-
-
Manually annotated by BRENDA team
Lactobacillus reuteri BR11
BR11
-
-
Manually annotated by BRENDA team
ssp. cremoris MG1363, recombinant protein
SwissProt
Manually annotated by BRENDA team
subsp. cremonis SK11
-
-
Manually annotated by BRENDA team
gene LmjF35.3230 or Lmj_CGL
UniProt
Manually annotated by BRENDA team
C57/Bl6 strain
-
-
Manually annotated by BRENDA team
male ICR mice
-
-
Manually annotated by BRENDA team
Mus musculus C57/BL6
C57/Bl6 strain
-
-
Manually annotated by BRENDA team
gene cys-16+
UniProt
Manually annotated by BRENDA team
Neurospora crassa 74OR23-1a
gene cys-16+
UniProt
Manually annotated by BRENDA team
Neurospora sp.
-
-
-
Manually annotated by BRENDA team
Neurospora sp.
ATCC-10816
-
-
Manually annotated by BRENDA team
Neurospora sp. ATCC-10816
ATCC-10816
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas putida
-
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas putida strain S-313
-
-
-
Manually annotated by BRENDA team
Nocardia erythropolis
-
-
-
Manually annotated by BRENDA team
Oenococcus oeni R1105
-
-
-
Manually annotated by BRENDA team
strain PAO1
-
-
Manually annotated by BRENDA team
76 male Sprague-Dawley rats (200-250 g), 96 different age rats (from 1 month to 12 months old) and insulin-resistant animals
-
-
Manually annotated by BRENDA team
adult male Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
enzyme activity increases during lactation
-
-
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
male wistar rat
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
pregnant and nonpregnant Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
Zucker diabetic fatty rats, comparison with Zucker fatty and Zucker lean rats
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
CYS3, SF1-1C, and YPH500
UniProt
Manually annotated by BRENDA team
Treponema denticola LC-67
LC-67
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
severe loss of cystathionine gamma-lyase activity is accompanied by adverse clinical effects
malfunction
-
both hyperglycemia and hyperketonemia mediate a reduction in enzyme expression and activity, which can contribute to the impaired H2S signaling associated with diabetes. Livers from streptozotocin-treated type I diabetic rats have lower levels of enzyme protein expression, enzyme activity, reduced tissue H2S formation, and increased reactive oxygen species production compared with those of controls
malfunction
-
both hyperglycemia and hyperketonemia mediate a reduction in enzyme expression and activity, which can contribute to the impaired H2S signaling associated with diabetes. Treatment with 0.025-0.035 mM H2O2, 4-8 mM acetoacetate and high D-glucose of 25 mM causes a significant decrease in enzyme protein expression, enzyme activity, and H2S levels, and an increase in intracellular reactive oxygen species production compared with those in normal controls
malfunction
-
inhibiting the enzyme activity with propargylglycine or silencing CSE expression using an siRNA approach results in a greater reduction in cell viability under exposure to the oxidizing agent hydrogen peroxide. Cellular oxidative stress also increases significantly upon propargylglycine inhibition or enzyme knockdown. Increased sensitivity towards H2O2-induced cytotoxicity in CSE-siRNAtransfected cells is associated with a decreased glutathione concentration (GSH) and glutathione ratio (GSH/GSSG). Incubation of cells with exogenous H2S increases the GSH concentration and GSH/GSSG ratio
malfunction
Rattus norvegicus Sprague-Dawley
-
both hyperglycemia and hyperketonemia mediate a reduction in enzyme expression and activity, which can contribute to the impaired H2S signaling associated with diabetes. Livers from streptozotocin-treated type I diabetic rats have lower levels of enzyme protein expression, enzyme activity, reduced tissue H2S formation, and increased reactive oxygen species production compared with those of controls
-
metabolism
-
CSE is a key enzyme in the pathway of cystathionine metabolism to produce endogenous H2S
metabolism
-
cystathionine gamma-lyase catalyzes the hydrolysis of L-cystathionine in the second step of the reverse transsulfuration pathway, which converts L-homocysteine to L-Cys
metabolism
-
the enzyme is involved in H2S biosynthesis
metabolism
Q9M1R1
the two cysteine desulfhydrases, L-cysteine desulfhydrase and D-cysteine desulfhydrase, are mainly responsible for the degradation of cysteine in order to generate H2S, they show similar expression patterns in tissues
physiological function
-
CSE activity may contribute to butyrate-stimulated H2S production in WiDr cells
physiological function
-
DES1 from Arabidopsis is an L-Cys desulfhydrase involved in maintaining Cys homeostasis, mainly at late developmental stages or under environmental perturbations
physiological function
-
human myometrium smooth muscle cells express cystathionine beta-synthase and cystathionine gamma-lyase. Endogenous H2S generated by cystathionine beta-synthase and cystathionine gamma-lyase locally modulates the contractility of pregnant myometrium
physiological function
-
Mice with a targeted deletion of the CSE gene fed a cysteine-limited diet exhibit growth retardation, decreased levels of cysteine, glutathione, and H2S, and increased plasma homocysteine level. Histological examinations of liver do not reveal any abnormality and plasma levels of aspartate aminotransferase, alanine aminotransferase, and albumin are normal in these animals. No CSE-KO mice survive after 12 weeks of feeding with the cysteine-limited diet. Supplementation of H2S to the CSE-KO mice fails to reverse the aforementioned abnormalities. Supplementation of cysteine in the drinking water of the CSE-KO mice significantly increases plasma cysteine and glutathione levels. This eventually leads to an increase in body weight and rescues the animals from death
physiological function
-
cystathionine gamma-lyase is an important enzyme responsible for endogenous H2S production in mammalian systems. Modulation of enzyme catalytic activity alters its antioxidative activity. Role of CSE in contributing to cellular antioxidative mechanisms in cell lines of peripheral tissue origin. Knockdown of CSE does not result in significant spontaneous cell death, indicating that CSE is not vital for cell survival in the cell lines studied
physiological function
Q9M1R1
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
Arabidopsis thaliana Col-0
-
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
-
metabolism
Arabidopsis thaliana Col-0
-
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
-
additional information
E9AFE7
the Leishmania major enzyme is able to rescue the wild-type phenotype of a Saccharomyces cerevisiae enzyme-null mutant
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(DL)-homocysteine
H2S + ?
show the reaction diagram
Oenococcus oeni, Oenococcus oeni R1105
-
-
-
-
?
3-chloro-2-aminobutanoate
?
show the reaction diagram
Neurospora sp.
-
-
-
-
?
3-chloro-DL-alanine + H2O
NH3 + ?
show the reaction diagram
-
-
-
?
alpha,beta-diaminopropionate
?
show the reaction diagram
-
beta,gamma-elimination
-
-
?
beta-chloro-L-Ala
?
show the reaction diagram
-
alpha,beta-elimination, alpha,gamma-elimination
-
-
?
beta-chloro-L-alanine + H2O
pyruvate + NH3 + HCl
show the reaction diagram
-
-
-
-
?
beta-methylcystine
?
show the reaction diagram
Neurospora sp.
-
-
-
-
?
cysteine
H2S
show the reaction diagram
-
-
-
-
?
cystine
H2S + NH3 + pyruvate + L-thiocysteine
show the reaction diagram
Lactobacillus reuteri, Lactobacillus reuteri BR11
-
-
-
-
?
D-Cys + D-homoserine
D-cystathionine
show the reaction diagram
-
-
-
?
D-Cys + L-homoserine
D-allocystathionine
show the reaction diagram
-
-
-
-
?
D-Cys + L-homoserine
D-allocystathionine
show the reaction diagram
-
-
-
?
D-Cys + L-homoserine
D-allocystathionine
show the reaction diagram
-
at 318% of the activity with L-homocysteine and L-cysteine
-
?
D-Cys + L-homoserine
D-allocystathionine
show the reaction diagram
-
gamma-replacement
-
-
?
D-Cys + L-homoserine
D-allocystathionine
show the reaction diagram
-
gamma-replacement
-
?
djenkolic acid
?
show the reaction diagram
-
-
-
-
?
djenkolic acid
?
show the reaction diagram
Neurospora sp.
-
-
-
-
?
djenkolic acid
?
show the reaction diagram
-
alpha,beta-elimination
-
-
-
djenkolic acid
?
show the reaction diagram
-
beta,gamma-elimination
-
-
-
djenkolic acid
?
show the reaction diagram
-
alpha-gamma-elimination
-
-
-
djenkolic acid
?
show the reaction diagram
-
L-djenkolic acid
-
-
?
DL-cystathionine
?
show the reaction diagram
B2LXT6
-
-
-
?
DL-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
DL-lanthionine + H2O
NH3 + ?
show the reaction diagram
-
47% of activity compared to cystathionine
-
?
DL-vinylglycine
?
show the reaction diagram
-
alpha,beta-elimination, alpha,gamma-elimination
-
-
?
homocysteine
?
show the reaction diagram
-
beta,gamma-elimination
-
-
?
L-Cys
H2S + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
show the reaction diagram
-
alpha,beta-elimination
-
-
-
L-Cys
H2S + NH3 + pyruvate
show the reaction diagram
-
alpha,beta-elimination
-
-
-
L-Cys
H2S + NH3 + pyruvate
show the reaction diagram
Treponema denticola LC-67
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
show the reaction diagram
Oenococcus oeni R1105
-
-
-
-
?
L-Cys
H2S + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-Cys + D-homoserine
L-allocystathionine
show the reaction diagram
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-cystathionine
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
?
L-cystathionine
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
?
L-cystathionine
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
alpha,beta-elimination
-
?
L-cystathionine
L-homocysteine + pyruvate + NH3
show the reaction diagram
Treponema denticola LC-67
-
-
-
?
L-cystathionine
L-homocysteine + pyruvate + NH3
show the reaction diagram
Lactobacillus fermentum DT41
-
-
-
?
L-cystathionine
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
?
L-cystathionine
L-homoserine + L-cysteine
show the reaction diagram
P32929
-
-
-
?
L-cystathionine
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
-
L-cystathionine
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
Oenococcus oeni, Oenococcus oeni R1105
-
-
-
-
?
L-cystathionine
homocysteine + pyruvate + NH3
show the reaction diagram
Oenococcus oeni, Oenococcus oeni R1105
-
-
-
-
?
L-cystathionine
2-oxobutyrate + L-cysteine + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
?
show the reaction diagram
Neurospora sp.
-
-
-
-
?
L-cystathionine + H2O
?
show the reaction diagram
-
beta,gamma-elimination
-
-
?
L-cystathionine + H2O
?
show the reaction diagram
Neurospora sp. ATCC-10816
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
Neurospora sp.
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
B2LXT6
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
E9AFE7
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
alpha,gamma-elimination
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
alpha,gamma-elimination
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
alpha,gamma-elimination
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
alpha,gamma-elimination
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
Lactobacillus fermentum DT41
-
alpha,gamma-elimination
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
Neurospora sp. ATCC-10816
-
-
-
?
L-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
A2RM21
-
-
?
L-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
Q8VCN5
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
B7UDE6
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
B3TNN8 and B3TNN9
-
-
-
?
L-cystathionine + H2O
L-cysteine + ?
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH
show the reaction diagram
Neurospora crassa, Neurospora crassa 74OR23-1a
Q96VU7
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
P32929
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Q9EQS4
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
B3TNN8 and B3TNN9
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
measurement of hydrogen sulfide production
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
A2RM21
15% of activity compared to cystathionine
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
5.3% of activity compared to cystathionine
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Mus musculus C57/BL6
-
-
measurement of hydrogen sulfide production
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
?
L-cysteine + L-cysteine
H2S + L-lanthionine
show the reaction diagram
-
-
-
-
?
L-cysteine + L-cysteine
L-lanthionine + H2S
show the reaction diagram
-
-
-
-
?
L-cystine
?
show the reaction diagram
-
alpha,beta-elimination
-
-
?
L-cystine
?
show the reaction diagram
-
alpha,beta-elimination, alpha,gamma-elimination
-
-
?
L-cystine
H2S + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cystine
H2S + NH3 + pyruvate
show the reaction diagram
Neurospora sp.
-
-
-
-
?
L-cystine
H2S + NH3 + pyruvate
show the reaction diagram
Lactobacillus fermentum, Lactobacillus fermentum DT41
-
best substrate
-
?
L-cystine
H2S + NH3 + pyruvate
show the reaction diagram
Neurospora sp. ATCC-10816
-
-
-
-
?
L-cystine
H2S + NH3 + pyruvate + L-thiocysteine
show the reaction diagram
B2LXT6
-
-
-
?
L-cystine
thiocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystine
pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystine + H2O
NH3 + ?
show the reaction diagram
-
-
-
?
L-cystine + H2O
NH3 + ?
show the reaction diagram
-
120% of activity compared to cystathionine
-
?
L-cystine + H2O
NH3 + ?
show the reaction diagram
A2RM21
133% of activity compared to cystathionine
-
?
L-cystine + H2O
NH3 + pyruvate + hydrogen sulfide
show the reaction diagram
-
-
-
?
L-djenkolic acid + H2O
NH3 + ?
show the reaction diagram
-
-
-
?
L-djenkolic acid + H2O
NH3 + ?
show the reaction diagram
-
190% of activity compared to cystathionine
-
?
L-djenkolic acid + H2O
NH3 + ?
show the reaction diagram
A2RM21
24% of activity compared to cystathionine
-
?
L-homocysteine
?
show the reaction diagram
-
-
-
-
?
L-homocysteine
?
show the reaction diagram
P32929
-
-
-
?
L-homocysteine + H2O
H2S + ?
show the reaction diagram
-
-
-
-
?
L-homocysteine + H2O
NH3 + 2-oxobutanoate + H2S
show the reaction diagram
-
-
-
-
?
L-homocysteine + L-cysteine
L-cystathionine + H2S
show the reaction diagram
-
-
-
-
?
L-homocysteine + L-homocysteine
L-homolanthionine + H2S
show the reaction diagram
-
-
-
-
?
L-homocystine
?
show the reaction diagram
Neurospora sp.
-
-
-
-
?
L-homoserine
?
show the reaction diagram
-
-
-
-
?
L-homoserine
?
show the reaction diagram
-
-
-
-
?
L-homoserine
?
show the reaction diagram
Neurospora sp.
-
-
-
-
?
L-homoserine
?
show the reaction diagram
-
beta,gamma-elimination
-
-
?
L-homoserine
?
show the reaction diagram
-
alpha,gamma-elimination
-
-
?
L-homoserine
2-oxobutyrate + NH3
show the reaction diagram
-
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
show the reaction diagram
-
8% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + 2-mercaptopropionate
S-methylcarboxymethyl-L-homocysteine
show the reaction diagram
-
-
-
-
?
L-homoserine + 2-mercaptopropionate
S-methylcarboxymethyl-L-homocysteine
show the reaction diagram
-
-
-
?
L-homoserine + 2-mercaptopropionate
S-methylcarboxymethyl-L-homocysteine
show the reaction diagram
-
gamma-replacement reaction
-
-
?
L-homoserine + 2-mercaptopropionate
S-methylcarboxymethyl-L-homocysteine
show the reaction diagram
-
gamma-replacement reaction, 73% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + 3-mercaptopropionate
S-carboxyethyl-L-homocysteine
show the reaction diagram
-
-
-
-
?
L-homoserine + 3-mercaptopropionate
S-carboxyethyl-L-homocysteine
show the reaction diagram
-
-
-
?
L-homoserine + 3-mercaptopropionate
S-carboxyethyl-L-homocysteine
show the reaction diagram
-
187% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + 3-mercaptopropionate
S-carboxyethyl-L-homocysteine
show the reaction diagram
-
gamma-replacement reaction
-
-
?
L-homoserine + 3-mercaptopropionate
S-carboxyethyl-L-homocysteine
show the reaction diagram
-
gamma-replacement reaction
-
?
L-homoserine + 4-mercaptobutanoate
S-carboxy-n-propyl-L-homocysteine
show the reaction diagram
-
14% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + D-homocysteine
meso-homolanthionine
show the reaction diagram
-
-
-
-
?
L-homoserine + D-homocysteine
meso-homolanthionine
show the reaction diagram
-
-
-
?
L-homoserine + D-homocysteine
meso-homolanthionine
show the reaction diagram
-
gamma-replacement reaction, 368% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + H2O
NH3 + ?
show the reaction diagram
-
-
-
?
L-homoserine + H2O
2-oxobutanoate + NH3 + H2O
show the reaction diagram
-
-
-
-
?
L-homoserine + H2O
2-oxobutanoate + NH3 + H2O
show the reaction diagram
-
-
-
-
?
L-homoserine + H2O
2-oxobutanoate + NH3 + H2O
show the reaction diagram
-
-
-
-
?
L-homoserine + H2O
2-oxobutanoate + NH3 + H2O
show the reaction diagram
B3TNN8 and B3TNN9
-
-
-
?
L-homoserine + H2O
H2O + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-homoserine + L-Cys
L-cystathionine
show the reaction diagram
-
-
-
?
L-homoserine + L-Cys
L-cystathionine
show the reaction diagram
-
-
-
?
L-homoserine + L-Cys
L-cystathionine
show the reaction diagram
-
-
-
?
L-homoserine + L-homocysteine
L-homolanthionine
show the reaction diagram
-
-
-
-
?
L-homoserine + L-homocysteine
L-homolanthionine
show the reaction diagram
-
-
-
?
L-homoserine + L-homocysteine
L-homolanthionine
show the reaction diagram
-
gamma-replacement reaction, 314% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + thioglycerol
S-(2,3-dihydroxypropyl)-L-homocysteine
show the reaction diagram
-
5% of the activity with L-homocysteine and L-Cys
-
?
L-homoserine + thioglycolate
S-carboxymethyl-L-homocysteine
show the reaction diagram
-
-
-
-
?
L-homoserine + thioglycolate
S-carboxymethyl-L-homocysteine
show the reaction diagram
-
gamma-replacement reaction, 69% of the activity with L-homocysteine and L-Cys
-
?
L-Met
methanethiol + ?
show the reaction diagram
-
-
-
-
?
L-Met
methanethiol + ?
show the reaction diagram
-
alpha,gamma-elimination
-
?
L-methionine + H2O
NH3 + ?
show the reaction diagram
-
-
-
?
L-methionine + H2O
NH3 + ?
show the reaction diagram
-
-
-
?
L-methionine + H2O
NH3 + ?
show the reaction diagram
-
less than 1% of activity compared to cystathionine
-
?
L-serine + H2O
NH3 + ?
show the reaction diagram
-
-
-
?
Lanthionine
?
show the reaction diagram
-
-
-
-
?
Lanthionine
?
show the reaction diagram
Neurospora sp.
-
-
-
-
?
Lanthionine
?
show the reaction diagram
-
alpha,beta-elimination
-
-
?
Lanthionine
?
show the reaction diagram
-
beta,gamma-elimination
-
-
?
Lanthionine
?
show the reaction diagram
-
alpha,gamma-elimination
-
-
?
Lanthionine
?
show the reaction diagram
-
meso-lanthionine
-
-
?
Lanthionine
?
show the reaction diagram
-
DL-lanthionine
-
-
?
Lanthionine
?
show the reaction diagram
-
L-lanthionine
-
-
?
Lanthionine
?
show the reaction diagram
Lactobacillus fermentum DT41
-
-
-
-
?
Lanthionine
?
show the reaction diagram
Neurospora sp. ATCC-10816
-
-
-
-
?
lanthionine + H2O
NH3 + ?
show the reaction diagram
A2RM21
131% of activity compared to cystathionine
-
?
meso-cystine
?
show the reaction diagram
Neurospora sp.
-
-
-
-
?
meso-cystine
?
show the reaction diagram
Neurospora sp. ATCC-10816
-
-
-
-
?
O-acetyl-L-homoserine
?
show the reaction diagram
Neurospora sp.
-
-
-
-
?
O-acetyl-L-homoserine + H2O
NH3 + ?
show the reaction diagram
-
-
-
?
O-acetyl-L-serine + H2O
acetate + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
O-succinyl-L-homoserine
?
show the reaction diagram
Neurospora sp.
-
decomposed most rapidly of all the above substrates
-
-
?
O-succinyl-L-homoserine + H2O
NH3 + ?
show the reaction diagram
-
-
-
?
S-(2-aminoethyl)-L-cysteine + H2O
NH3 + pyruvate + cysteamine
show the reaction diagram
-
-
-
?
S-aminoethyl-L-Cys
?
show the reaction diagram
-
-
-
-
?
S-methyl-L-Cys
?
show the reaction diagram
Neurospora sp.
-
-
-
-
?
S-methyl-L-Cys
?
show the reaction diagram
-
alpha,beta-elimination
-
-
?
S-methyl-L-cysteine + H2O
NH3 + pyruvate + methyl mercaptan
show the reaction diagram
-
-
-
?
seleno-L-methionine
methylselenol + 2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
mixed disulfide of L-cystine and L-homocystine
?
show the reaction diagram
Neurospora sp.
-
-
-
-
?
additional information
?
-
-
the Streptomyces enzyme has a lower substrate specificity than the rat-liver one
-
-
-
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 activity is required for high-level cephalosporin biosynthesis but not for low-level production of the antibiotic
-
?
additional information
?
-
Q5H4T8
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
?
-
-
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
?
-
-
responsible for the formation of nanocrystals
-
-
-
additional information
?
-
-
enzyme is able to demethiolate methionine into methanethiol
-
-
-
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
?
-
-
no activity with L-methionine
-
-
-
additional information
?
-
Acremonium chrysogenum C10
-
enzyme activity is required for high-level cephalosporin biosynthesis but not for low-level production of the antibiotic
-
?
additional information
?
-
Lactobacillus fermentum DT41
-
enzyme responsible for amino acid catabolism
-
-
-
additional information
?
-
Oenococcus oeni R1105
-
enzyme is able to demethiolate methionine into methanethiol
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-cystathione + H2O
L-cysteine + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-cystathionine
2-oxobutyrate + L-cysteine + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
E9AFE7
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
r
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
show the reaction diagram
B3TNN8 and B3TNN9
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH
show the reaction diagram
Q96VU7
-
-
-
?
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH3
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
L-cystathionine + H2O
L-cysteine + 2-oxobutanoate + NH
show the reaction diagram
Neurospora crassa 74OR23-1a
Q96VU7
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
B3TNN8 and B3TNN9
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
H2S + pyruvate + NH3
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
?
L-cystine
pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-homoserine
2-oxobutyrate + NH3
show the reaction diagram
-
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
show the reaction diagram
B3TNN8 and B3TNN9
-
-
-
?
additional information
?
-
-
enzyme responsible for amino acid catabolism
-
-
-
additional information
?
-
-
enzyme activity is required for high-level cephalosporin biosynthesis but not for low-level production of the antibiotic
-
?
additional information
?
-
Q5H4T8
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
?
-
-
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
?
-
-
responsible for the formation of nanocrystals
-
-
-
additional information
?
-
Acremonium chrysogenum C10
-
enzyme activity is required for high-level cephalosporin biosynthesis but not for low-level production of the antibiotic
-
?
additional information
?
-
Lactobacillus fermentum DT41
-
enzyme responsible for amino acid catabolism
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
Neurospora sp.
-
coenzyme
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
-
coenzyme
pyridoxal 5'-phosphate
Neurospora sp.
-
required
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
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
-
1 molecule per subunit
pyridoxal 5'-phosphate
-
Km value 0.003 mM
pyridoxal 5'-phosphate
-
2 molecules per subunit
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
enzyme binds 2 mol per dimer
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
B3TNN8 and B3TNN9
-
pyridoxal 5'-phosphate
-
; residues K212 and Y114 are involved in binding
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q9M1R1
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q96VU7
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
E9AFE7
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
Ca2+ promotes activation of CSE, H2S production by CSE is a Ca2+-dependent phenomenon
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
HgCl2
-
a potent irreversible enzyme inhibitor, but HgCl2 is also a strong inactivator of cystathionine gamma-lyase
INHIBITORS
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
1,10-phenanthroline
-
2 mM, 20% inhibition
1-nitroso-2-naphthol-3,6-disulfonic acid
-
2 mM, 55% inhibition
2-(prop-2-yn-1-ylamino)acetic acid
-
-
3-methyl-2-benzothiazolinone
-
31% residual activity at 5 mM
3-Methyl-2-benzothiazolinone hydrazone
-
-
3-Methyl-2-benzothiazolinone hydrazone
-
-
4-chloromercuribenzoate
-
-
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)
-
-
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
Ala
-
competitive
alpha-amino-gamma-aminooxybutanoate
-
-
aminoethoxyvinylglycine
-
-
Aminooxyacetate
-
-
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
aminooxyacetic acid
-
-
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-Ala
-
alpha,beta-elimination L-homoserine
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-cyano-L-alanine
-
-
Beta-cyanoalanine
-
-
Beta-cyanoalanine
-
reversible inhibitor of CSE
Beta-cyanoalanine
-
-
beta-trifluoromethyl-D,L-Ala
-
i.e. 2-amino-4,4,4-trifluorobutanoate
Ca2+
-
0.1 mM, weak
carboxymethoxylamine
-
-
Cd2+
-
strong
CH3-Hg-S-Cys
-
the cysteine S-conjugate of Hg2+ is a potent irreversible enzyme inhibitor
-
Co2+
-
0.1 mM, weak
Cr2+
-
0.1 mM, weak
Cu2+
-
strong
cycloserine
-
D-cycloserine
cycloserine
-
DL-cycloserine
cycloserine
-
partially competitive
Cys
-
the regulatory site of the enzyme is specific for L-Cys
Cys
Neurospora sp.
-
-
Cys
-
above 10 mM, inhibits replacement reaction with L-homoserine and L-Cys
Cys-S-Hg-S-Cys
-
the cysteine S-conjugate of Hg2+ is a potent irreversible enzyme inhibitor
-
cysteamine
-
-
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
dichloro-D,L-Ala
-
-
DL-Penicillamine
-
3% residual activity at 5 mM
DL-propargylalanine
-
-
DL-propargylglycine
-
2% residual activity at 5 mM
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
-
elevates blood pressure
DL-propargylglycine
-
-
DL-propargylglycine
-
-
DL-propargylglycine
-
irreversible inhibitor of CSE
DL-propargylglycine
-
irreversible inhibitor of CSE
DL-propargylglycine
-
selective inhibitor of cystathionine gamma-lyase
DL-propargylglycine
-
irreversible inhibitor
DL-propargylglycine
E9AFE7
an irreversible enzyme inhibitor, molecular mechanism of DL-propargylglycine action in vivo
EDTA
-
2 mM, 13% inhibition
Fe2+
-
0.1 mM, weak
Fe3+
-
0.1 mM, weak
Gly
-
competitive
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
Hg2+
-
strong
Hg2+
-
HgCl2, alpha,beta-elimination L-homoserine
HgCl2
-
a potent irreversible enzyme inhibitor, but HgCl2 is also a strong inactivator of cystathionine gamma-lyase
hydroxylamine
-
-
hydroxylamine
-
-
hydroxylamine
-
-
hydroxylamine
-
alpha,beta-elimination of L-homoserine
hydroxylamine
-
-
iodoacetamide
-
22% residual activity at 2.5 mM
Iodosobenzoate
-
-
Isoniazid
-
-
Isonicotinic acid hydrazide
-
-
L-aminoethoxyvinylglycine
-
-
L-Asn
-
weak
L-beta-oxalyl amino-L-alanine
-
inhibition only after long exposure
L-cysteine
-
substrate inhibition mainly due to removal of cofactor
L-cysteine
-
inhibits alpha,gamma elimination activity
L-cysteine
-
0.4 mM, 6% residual activity
L-Met
-
weak
L-Propargylglycine
-
-
L-Thr
-
weak
L-Val
-
weak
Mercurials
Neurospora sp.
-
-
-
Mg2+
-
0.1 mM, weak
N-ethylmaleimide
-
81% residual activity at 5 mM
N-ethylmaleimide
-
-
N-prop-2-yn-1-ylglycine
-
-
NaCl
-
5% w/v
NaCl
-
59% residual activity at 5 mM
NEM
-
0.05 mM, inhibition is partly relieved by 0.2 mM 2,3-dimercaptopropanol
NH4Cl/NH4OH buffer
-
-
-
Ni2+
-
0.1 mM, weak
O2
-
homogenized gills produces H2S enzymatically, and H2S production is inhibited by O2, whereas mitchondrial H2S consumption is O2 dependent
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
-
-
Penicillamine
-
alpha,beta-elimination of L-homoserine; D-penicillamine; L-penicillamine
phenylhydrazine
-
-
phenylhydrazine
-
alpha,beta-elimination L-homoserine as substrate
phenylhydrazine
-
2.8% residual activity at 5 mM
propargyl glycine
-
-
propargylglycine
-
-
propargylglycine
-
alpha,beta-elimination L-homoserine
propargylglycine
-
-
propargylglycine
-
10 mM inhibits testosterone induced H2S biosynthesis
propargylglycine
-
-
propargylglycine
-
-
propargylglycine
-
-
propargylglycine
-
-
Semicarbazide
-
-
Semicarbazide
-
-
Semicarbazide
-
alpha,beta-elimination L-homoserine as substrate
Semicarbazide
-
11% residual activity at 5 mM
Ser
-
competitive
Sodium bisulfite
-
-
Sodium borohydride
-
-
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
trifluoro-Ala
-
trifluoro-D,L-Ala
trifluoro-Ala
-
-
trifluoroalanine
-
-
Zn2+
-
0.1 mM, weak
Zn2+
-
ZnCl2, alpha,beta-elimination L-homoserine
Mn2+
-
0.1 mM, weak
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
-
not inhibitory: EDTA
-
additional information
-
administration of CSE inhibitors enhances the glucose uptake of adipocytes
-
additional information
P31373
cystathionine gamma-lyase encoded by CYS3 is repressed by addition of cysteine to the growth medium
-
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
-
no or poor inhibition by methylselenocysteine, D-cycloserine, pargyline, and parsalmide
-
additional information
-
no inhibition by 4-hydroxybutyrate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-propargyl-cysteine
-
(S)-propargyl-cysteine increases CSE activity by 1.6fold in myocardial infarction rats
2-mercaptoethanol
-
increases activity
calcium-calmodulin
-
catalytic activity of pure CSE is increased more than 2fold by calcium and calmodulin, but not by either substance alone
-
CYS3
Q96VU7
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
B2LXT6
low concentration of cellular cysteine leads to elevation of cystathionine gamma-lyase
additional information
-
enzyme is stimulated by preincubation with Cys
-
additional information
P31373
cystathionine gamma-lyase encoded by CYS3 is induced by sulfur starvation
-
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
-
glucose (10 or 20 mM) increases the cystathionine-gamma-lyase expression in the beta-cells
-
additional information
-
presence of 10 mM L-cysteine increases H2S production rate. Low oxygen levels increases H2S production rates
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.153
(DL)-homocysteine
-
pH 8.0, 37C
1.417
(DL)-homocysteine
-
pH 8.0, 37C
28.41
3-chloro-DL-alanine
-
pH 8.0, 37C
2.39
beta-chloro-L-Ala
-
-
0.1
beta-chloro-L-alanine
-
Y123F/Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25C
0.17
beta-chloro-L-alanine
-
Y123F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25C
1.21
beta-chloro-L-alanine
-
wild type, 20 mM potassium phosphate buffer, pH 7.4, 25C
3.2
beta-chloro-L-alanine
-
Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25C
1
cystathionine
-
-
0.76
D-alanine
-
racemization, Y123F/Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25C
10
D-alanine
-
racemization, wild type, 20 mM potassium phosphate buffer, pH 7.4, 25C
22.4
D-alanine
-
racemization, Y123F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25C
25.3
D-alanine
-
racemization, Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25C
3.27
DL-cystathionine
-
pH 8.0, 37C
0.209
DL-lanthionine
-
-
5.18
DL-vinylglycine
-
-
1
L-alanine
-
racemization, Y123F/Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25C
10
L-alanine
-
racemization, wild type, 20 mM potassium phosphate buffer, pH 7.4, 25C
14.3
L-alanine
-
racemization, Y123F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25C
20
L-alanine
-
racemization, Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25C
0.029
L-Cys
-
pH 8.0, 37C
0.069
L-Cys
-
pH 8.0, 37C
0.204
L-cystathionine
-
-
0.232
L-cystathionine
-
pH 8.0, 37C
0.236
L-cystathionine
-
pH 8.0, 37C
0.4
L-cystathionine
-
for variante S403
0.42
L-cystathionine
-
His-tagged recombinant wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25C
0.45
L-cystathionine
-
native wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25C
0.5
L-cystathionine
-
-
0.6
L-cystathionine
-
for mutante T67I; for variante I403
0.71
L-cystathionine
-
pH 7.2, 25C, recombinant wild-type enzyme
0.72
L-cystathionine
-
for mutante Q240E
0.76
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E48A
0.81
L-cystathionine
-
-
0.81
L-cystathionine
-
mutant enzyme E48F, in 50 mM potassium phosphate, pH 7.8, at 25C
0.82
L-cystathionine
-
mutant enzyme E48A, in 50 mM potassium phosphate, pH 7.8, at 25C
0.87
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E48D
0.9
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E48Q
1.11
L-cystathionine
-
mutant enzyme E48D, in 50 mM potassium phosphate, pH 7.8, at 25C
5.2
L-cystathionine
-
mutant enzyme E333A, in 50 mM potassium phosphate, pH 7.8, at 25C
8.7
L-cystathionine
-
pH 7.6, 37C
10.6
L-cystathionine
-
pH 7.6, 37C
11.1
L-cystathionine
-
pH 7.6, 37C
11.2
L-cystathionine
-
pH 7.6, 37C
11.8
L-cystathionine
-
pH 7.6, 37C
12
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E333A; pH 7.2, 25C, recombinant mutant E333D
13
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E333Q
25.5
L-cystathionine
-
pH 7.6, 37C
0.09
L-cysteine
-
pH 7.2, 25C, recombinant wild-type enzyme
0.11
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48A
0.18
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48Q
0.4
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48D; pH 7.2, 25C, recombinant mutant E48Q/E333Q
0.46
L-cysteine
-
-
0.5
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48A/E333A; pH 7.2, 25C, recombinant mutant E48D/E333D
0.62
L-cysteine
-
pH 8.0, 37C
0.68
L-cysteine
-
pH 7.6, 37C
0.7
L-cysteine
-
pH 7.2, 25C, recombinant mutant E333Q
0.75
L-cysteine
-
pH 7.6, 37C
0.76
L-cysteine
-
mutant enzyme E339Y, in 50 mM sodium phosphate buffer (pH 8.2) , at 37C
0.88
L-cysteine
-
pH 7.6, 37C
1.08
L-cysteine
-
pH 7.6, 37C
1.16
L-cysteine
-
pH 7.6, 37C
1.2
L-cysteine
-
pH 7.2, 25C, recombinant mutant E333A
1.8
L-cysteine
-
pH 7.2, 25C, recombinant mutant E333D
1.9
L-cysteine
-
wild type enzyme, in 50 mM sodium phosphate buffer (pH 8.2) , at 37C
2.46
L-cysteine
-
pH 7.6, 37C
2.75
L-cysteine
-
-
3.3
L-cysteine
-
mutant enzyme E339K, in 50 mM sodium phosphate buffer (pH 8.2) , at 37C
3.4
L-cysteine
-
for variante I403
3.5
L-cysteine
-
for variante S403
4.1
L-cysteine
-
for mutante T67I
7.7
L-cysteine
-
mutant enzyme E339A, in 50 mM sodium phosphate buffer (pH 8.2) , at 37C
0.032
L-cystine
Neurospora sp.
-
-
1.29
L-cystine
-
pH 8.0, 37C
5.4
L-homocysteine
-
for variante S403
7
L-homocysteine
-
for variante I403
8
L-homocysteine
-
for mutante T67I
12.5
L-homoserine
-
-
0.39
Lanthionine
Neurospora sp.
-
-
0.7
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48D/E333D
0.9
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E333D
1.4
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48D
1.5
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48A; pH 7.2, 25C, recombinant mutant E48Q/E333Q
2.2
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E333A
2.5
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant wild-type enzyme
2.9
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48A/E333A
4.4
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48Q
5.3
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E333Q
2.75
S-(2-aminoethyl)-L-cysteine
-
pH 8.0, 37C
13.13
S-methyl-L-cysteine
-
pH 8.0, 37C
0.12
meso-cystine
Neurospora sp.
-
-
additional information
additional information
Neurospora sp.
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.9
cystathionine
-
-
0.02
L-cystathionine
-
for mutante Q240E
0.39
L-cystathionine
-
mutant enzyme E48F, in 50 mM potassium phosphate, pH 7.8, at 25C
0.45
L-cystathionine
-
for mutante T67I
0.48
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E333Q
0.54
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E48A
0.67
L-cystathionine
-
mutant enzyme E48A, in 50 mM potassium phosphate, pH 7.8, at 25C
0.69
L-cystathionine
-
mutant enzyme E333A, in 50 mM potassium phosphate, pH 7.8, at 25C
0.76
L-cystathionine
-
mutant enzyme E48D, in 50 mM potassium phosphate, pH 7.8, at 25C
0.78
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E333A
0.9
L-cystathionine
-
native wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25C
0.98
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E333D
1.29
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E48Q
1.4
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E48D
1.51
L-cystathionine
-
pH 7.2, 25C, 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 25C
1.9
L-cystathionine
-
for variante I403
7.5
L-cystathionine
-
-
0.029
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48D/E333D
0.09
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48A
0.11
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48A/E333A
0.12
L-cysteine
-
wild type enzyme, in 50 mM sodium phosphate buffer (pH 8.2) , at 37C
0.15
L-cysteine
-
pH 7.2, 25C, recombinant wild-type enzyme
0.16
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48Q/E333Q
0.18
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48Q
0.24
L-cysteine
-
pH 7.2, 25C, recombinant mutant E333D
0.3
L-cysteine
-
for mutante T67I
0.32
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48D
0.34
L-cysteine
-
mutant enzyme E339K, in 50 mM sodium phosphate buffer (pH 8.2) , at 37C
0.4
L-cysteine
-
-
0.5
L-cysteine
-
pH 7.2, 25C, recombinant mutant E333Q
0.67
L-cysteine
-
for variante I403; for variante S403
0.76
L-cysteine
-
mutant enzyme E339Y, in 50 mM sodium phosphate buffer (pH 8.2) , at 37C
1.3
L-cysteine
-
pH 7.2, 25C, recombinant mutant E333A
1.44
L-cysteine
-
mutant enzyme E339A, in 50 mM sodium phosphate buffer (pH 8.2) , at 37C
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, 25C, recombinant mutant E48D/E333D
0.0045
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E333D
0.0047
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48A/E333A
0.0053
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48D
0.0058
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E333A
0.0092
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48Q/E333Q
0.0097
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant wild-type enzyme
0.0102
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E333Q
0.0124
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48Q
0.0142
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48A
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0037
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E48A/E333A
585
0.0088
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E48D/E333D
585
0.0169
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E48Q/E333Q
585
0.036
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E333Q
585
0.065
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E333A
585
0.082
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E333D
585
0.132
L-cystathionine
-
mutant enzyme E333A, in 50 mM potassium phosphate, pH 7.8, at 25C
585
0.147
L-cystathionine
-
mutant enzyme E333Y, in 50 mM potassium phosphate, pH 7.8, at 25C
585
0.49
L-cystathionine
-
mutant enzyme E48F, in 50 mM potassium phosphate, pH 7.8, at 25C
585
0.68
L-cystathionine
-
mutant enzyme E48D, in 50 mM potassium phosphate, pH 7.8, at 25C
585
0.71
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E48A
585
0.82
L-cystathionine
-
mutant enzyme E48A, in 50 mM potassium phosphate, pH 7.8, at 25C
585
1.4
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E48Q
585
1.59
L-cystathionine
-
pH 7.2, 25C, recombinant mutant E48D
585
1.98
L-cystathionine
-
native wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25C
585
2.1
L-cystathionine
-
pH 7.2, 25C, recombinant wild-type enzyme
585
4.3
L-cystathionine
-
His-tagged recombinant wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25C
585
0.06
L-cysteine
-
wild type enzyme, in 50 mM sodium phosphate buffer (pH 8.2) , at 37C
74
0.06
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48D/E333D
74
0.11
L-cysteine
-
mutant enzyme E339K, in 50 mM sodium phosphate buffer (pH 8.2) , at 37C
74
0.13
L-cysteine
-
pH 7.2, 25C, recombinant mutant E333D
74
0.19
L-cysteine
-
mutant enzyme E339A, in 50 mM sodium phosphate buffer (pH 8.2) , at 37C
74
0.21
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48A/E333A
74
0.31
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48Q/E333Q
74
0.43
L-cysteine
-
mutant enzyme E339Y, in 50 mM sodium phosphate buffer (pH 8.2) , at 37C
74
0.49
L-cysteine
-
pH 7.2, 25C, recombinant mutant E333Q
74
0.72
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48D
74
0.8
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48A
74
0.81
L-cysteine
-
pH 7.2, 25C, recombinant mutant E333A
74
1.02
L-cysteine
-
pH 7.2, 25C, recombinant mutant E48Q
74
1.7
L-cysteine
-
pH 7.2, 25C, recombinant wild-type enzyme
74
0.0016
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48A/E333A
680
0.0019
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E333Q
680
0.0026
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E333A
680
0.0028
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48Q
680
0.0038
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant wild-type enzyme and mutant E48D
680
0.005
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E333D; pH 7.2, 25C, recombinant mutant E48D/E333D
680
0.006
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48Q/E333Q
680
0.01
O-acetyl-L-serine
-
pH 7.2, 25C, recombinant mutant E48A
680
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0011
aminooxyacetic acid
-
pH 8.2, 37C
0.014
Beta-cyanoalanine
-
pH 8.2, 37C
0.065
DL-propargylglycine
E9AFE7
pH 7.4, 37C
0.0048
hydroxylamine
-
pH 8.2, 37C
0.001
L-aminoethoxyvinylglycine
-
pH 8.2, 37C
0.04
propargylglycine
-
pH 8.2, 37C
0.289
trifluoroalanine
-
pH 8.2, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.49
E9AFE7
cell-free extract of promastigotes, pH 8.0, 37C
0.49
-
cell-free extract of promastigotes, pH 8.0, 37C
11.5
A2RM21
substrate cystathionine
24
-
purified liver enzyme, pH 7.4, 37C
additional information
Neurospora sp.
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2 - 7.8
-
wild-type enzyme
7.4
-
assay at
7.5
Neurospora sp.
-
-
8
-
0.1 M potassium phosphate buffer
8
-
substrate cystathionine
8
E9AFE7
assay at
8.9
-
Tris-HCl
9
-
alpha,gamma-elimination of L-cystathionine and L-homoserine
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
5
-
20% residual activity
6
-
40% residual 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
6.5
-
substrate cystathionine, no activity below
8 - 9
-
pH 8.0: about 85% of maximal activity, pH 9.0: about 50% of maximal activity
9
-
90% residual activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
0.1 M potassium phosphate buffer
37
-
assay at
37
E9AFE7
assay at
37
-
assay at
50
-
alpha,gamma-elimination of L-cystathionine and L-homoserine
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
-
10C: about 35% of maximal activity, 40C: rapid decrease of activity above
30 - 55
-
0.1 M potassium phosphate buffer, pH 7.8, 0.2 mM pyridoxal-5'-phosphate and 1 mM EDTA
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression of both cystathionine gamma-lyase and 3-mercaptopyruvate sulfurtransferase, the activity of 3-mercaptopyruvate sulfurtransferase is higher than that of cystathionine gamma-lyase
Manually annotated by BRENDA team
-
mainly expressed in airway and vascular smooth muscle cells in rat lung tissue
Manually annotated by BRENDA team
-
cultured human aorta smooth muscle cell
Manually annotated by BRENDA team
-
predominantly localized to the endothelial layer of blood vessels
Manually annotated by BRENDA team
-
with a decreasing activity in tail artery, aorta and mesenteric arteries
Manually annotated by BRENDA team
-
enzyme expression in numerous oval or polygonal cells
Manually annotated by BRENDA team
-
enzyme activity remains low during all stages of development
Manually annotated by BRENDA team
-
acitvity only 1% of activity in liver
Manually annotated by BRENDA team
-
activity in human brain is 100fold higher than that observed in mouse brain
Manually annotated by BRENDA team
-
in the brain, where CSE levels are low, localizations are predominantly in white matter
Manually annotated by BRENDA team
-
mainly in the ventral ganglia
Manually annotated by BRENDA team
Mus musculus C57/BL6
-
-
-
Manually annotated by BRENDA team
Q9M1R1
high expression
Manually annotated by BRENDA team
-
whole cells, cell lysate of a culture broth, cell wall of a subcellular fraction
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Mus musculus C57/BL6
-
-
-
Manually annotated by BRENDA team
-
CSE is localized in the muscular trabeculae and the smooth-muscle component of the penile artery
Manually annotated by BRENDA team
-
only in the anterior- and the postero-lateral areas of the body
Manually annotated by BRENDA team
-
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)
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
-
in neurons and nerve fibers of the lateral nerve cords immediately behind the ventral ganglia
Manually annotated by BRENDA team
-
high enzyme activity from late foetal life to maturity
Manually annotated by BRENDA team
P32929
only in adult tissue, not detectable in fetal, premature and full-term neonatal liver
Manually annotated by BRENDA team
-
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)
Manually annotated by BRENDA team
-
of type 1 diabetic rats
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
of type 1 diabetic rats
-
Manually annotated by BRENDA team
Mus musculus C57/BL6
-
-
-
Manually annotated by BRENDA team
-
mainly expressed in airway and vascular smooth muscle cells in rat lung tissue
Manually annotated by BRENDA team
-
smooth muscle cells
Manually annotated by BRENDA team
-
pregnant myometrium, primarily localized to smooth muscle cells of pregnant myometrium
Manually annotated by BRENDA team
-
of lateral nerve cord and in the area of the cell bodies
Manually annotated by BRENDA team
-
peripheral blood mononuclear cells, PBMC, isolated from healthy subjects and type 1 diabetic patients
Manually annotated by BRENDA team
-
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)
Manually annotated by BRENDA team
-
of the canals of the cerebral organs, enzyme expression
Manually annotated by BRENDA team
-
only trace activity
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
primarily localized to smooth muscle cells of pregnant myometrium
Manually annotated by BRENDA team
Q9M1R1
high expression
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
high expression
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
a pro-monocytic cell line
Manually annotated by BRENDA team
-
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)
Manually annotated by BRENDA team
-
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)
Manually annotated by BRENDA team
-
mainly expressed in airway and vascular smooth muscle cells in rat lung tissue
Manually annotated by BRENDA team
-
expression of both cystathionine gamma-lyase and 3-mercaptopyruvate sulfurtransferase, the activity of 3-mercaptopyruvate sulfurtransferase is higher than that of cystathionine gamma-lyase
Manually annotated by BRENDA team
additional information
-
immunohistochemic analysis
Manually annotated by BRENDA team
additional information
-
no expression in white muscle
Manually annotated by BRENDA team
additional information
Q9M1R1
the enzyme expression levels gradually increases in an age-dependent manner, expression profiling, overview
Manually annotated by BRENDA team
additional information
Arabidopsis thaliana Col-0
-
the enzyme expression levels gradually increases in an age-dependent manner, expression profiling, overview
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39700
-
the 44.5 kDa bands for variant 1 of CSE are detected in all arteries tested with Western blotting. CSE variant 2 is also detected at 39.7 kDa in a few arteries, but the band is not as intense and is not detected in most arteries
693818
40000
-
Western blot
675074
42600
Q5H4T8
SDS-PAGE
690270
43000
-
Western blot analysis, SDS-PAGE
690781
43000
-
Western blot
695079
43000
-
SDS-PAGE
708059
43600
-
calculated from cDNA sequence
663934
43600
-
deduced from SDS-PAGE
710063
44000
-
SDS-PAGE
710627
44500
-
the 44.5 kDa bands for variant 1 of CSE are detected in all arteries tested with Western blotting. CSE variant 2 is also detected at 39.7 kDa in a few arteries, but the band is not as intense and is not detected in most arteries
693818
44500
-
SDS-PAGE
709711
70000
-
Western blot analysis
690352
140000
-
non-denaturing PAGE, gel filtration
34506
156000
-
T67I CGL mutant; wild-type, estimated for CGL from its retention time of 42.8 min
690967
160000
-
light scattering
34498
160000
-
glycerol density gradient centrifugation
34502
160000
-
-
5584
160000
-
gel filtration
652626
162000
-
gel filtration
586904
168000
-
equilibrium sedimentation
586904
170000
-
Q240E CGL mutant
690967
178000
-
wild-type, molecular masses of both the T67I CGL (156 kDa) and the Q240E mutant (170 kDa) are comparable to that of wild-type CGL (167 kDa), indicating that both mutants exist as tetrameric proteins
690967
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 43000, SDS-PAGE
?
-
x * 45000, SDS-PAGE
?
-
x * 44000, SDS-PAGE
?
A2RM21
x * 41000, deduced from gene sequence
?
-
x * 40000, SDS-PAGE, x * 41500, calculated
?
Oenococcus oeni R1105
-
x * 40000, SDS-PAGE, x * 41500, calculated
-
homotetramer
-
In the three-dimensional structure of human CGL, two monomers contribute residues to each of the two active sites in the dimer, and two dimers come together to form a tetramer
octamer
-
8 * 20000, ultracentrifugation in presence of SDS
oligomer
-
-
tetramer
-
-
tetramer
-
4 * 45000, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
4 * 41000, SDS-PAGE
tetramer
-
4 * 35000, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE in presence of a reducing agent
tetramer
-
crystallization data
tetramer
Lactobacillus fermentum DT41
-
4 * 35000, SDS-PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no modification
-
does not contain detectable carbohydrate
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using sitting drop and hanging drop vapor diffusion methods at room temperature
-
crystals of two different shapes, plate-shaped and pyramid-shaped, diffract to 2.9 and 3.2 A resolution and belong to the primitive orthogonal space group P212121 and the tetragonal space group P41 (or P43), with unit-cell parameters a = 73.0, b = 144.9, c = 152.3 A and a = b = 78.2, c = 300.7 A, respectively. For the P212121 crystals, three or four monomers exist in the asymmetric unit with a corresponding VM of 3.02 or 2.26 A3/Da and a solvent content of 59.3 or 45.7%. For the P41 (or P43) crystals, four or five monomers exist in the asymmetric unit with a corresponding VM of 2.59 or 2.09 A3/Da and a solvent content of 52.5 or 40.6%
Q5H4T8
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
-
5 min, enzyme maintains about 50% of activity
652626
20
-
20 h, stable
34506
30 - 55
-
rapid loss of activity at 60C, 0.1 M potassium phosphate buffer, pH 7.8, 0.2 mM pyridoxal-5'-phosphate and 1 mM EDTA
663694
40
-
10 min, stable up to
34509
50
-
10 min, 75% loss of activity
34509
50
-
0.04 mM pyridoxal 5'-phosphate, 10 min, stable
586904
55
-
10 min, complete inactivation
34509
55
-
0.04 mM pyridoxal 5'-phosphate, 10 min, 15% loss of activity
586904
56
-
stable up to
713889
60
-
0.04 mM pyridoxal 5'-phosphate, 10 min, 50% loss of activity
586904
60
-
5 min, complete inactivation
652626
65
-
1 min, complete inactivation
34506
70
-
30 min, complete inactivation
34507
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no loss of activity after repeated freezing at -40C and thawing
-
inactivation by cathepsins at various rates
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
-
not inhibitory up to 15% v/v
Ethanol
Oenococcus oeni R1105
-
not inhibitory up to 15% v/v
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for 90 days
-
-40C, stable for 4 months
-
-50C, potassium phosphate buffer, pH 7.5, enzyme stabilized by pyridoxal 5'-phosphate, EDTA, and dithiothreitol retains full activity for several months
-
-20C, in 45% glycerol solution, containing 10 mM potassium phosphate, pH 7.5, 0.02 mM pyridoxal 5'-phosphate, 0.12 mM EDTA, 0.2 mM DTT, stable for 2 months or more
-
4C, 10 mM potassium phosphate, pH 7.5, containing 0.02 mM pyridoxal phosphate, 0.12 mM EDTA, 0.2 mM dithiothreitol stable for 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Codon Plus by metal affinity chromatography
-
combination of Ni-NTA chromatography, anion exchange chromatography, and gel filtration steps
-
gel filtration
-
glutathione Sepharose bead chromatography, gel filtration
-
Superdex S-200 gel filtration
-
Ni2+ affinity column chromatography, gel filtration
B3TNN8 and B3TNN9
-
Neurospora sp.
-
ammonium sulfate precipitation, butyl-Toyopearl 650M resin column chromatography, and DEAE column chromatography
-
immobilization on aminohexyl-Sepharose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
semi-quantitative reverse transcription-PCR analysis
Q9M1R1
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Codon Plus using expression vector pGEX-4T3/GST-CSE
-
expression in Escherichia coli strain Sure R
-
enzyme expressionin HEK-293 cells, Hep-G2 cells and IMR-90 cells
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli XL-1 cells
-
expression in Escherichia coli
-
quantitative enzyme expression PCR analysis
-
expressed in Escherichia coli BL21(DE3) cells
B3TNN8 and B3TNN9
expressed in Escherichia coli
-
gene LmjF35.3230 or Lmj_CGL, functional complementation of a CGL null mutant strain DELTA CYS3 of Saccharomyces cerevisiae
E9AFE7
gene cys-16+, DNA and amino acid sequence determination and analysis, gene cys-16+ gene encodes a polypeptide of 417 amino acids with a highly conserved pyridoxal 5'-phosphate binding site and substrate-cofactor binding pocket
Q96VU7
expression in Escherichia coli
-
overexpression in HEK-293, overexpression inhibits cell proliferation and DNA synthesis
Q9EQS4
quantitative enzyme expression PCR analysis
-
expression in Escherichia coli
-
the His-tagged enzyme is expressed in Escherichia coli KS1000 cells
-
expression in Escherichia coli
-
site directed mutagenesis mutants, expression in Escherichia coli
-
Y64A mutant
-
expressed in Escherichia coli
Q5H4T8
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression levels gradually increases in an age-dependent manner
Q9M1R1
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
Q9M1R1
the enzyme expression levels gradually increases in an age-dependent manner
Arabidopsis thaliana Col-0
-
-
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
Arabidopsis thaliana Col-0
-
-
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
-
butyrate significantly increases CSE protein expression
-
butyrate upregulates CSE expression
-
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
-
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
-
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
-
CSE activity and protein levels in the colonic tissue do not notably change in the mice with colitis
-
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
-
either the activity or protein expression of pancreatic CSE increase after the development of caerulein-induced pancreatitis in mice
-
higher rate of H2S production corresponds to an up-regulation of CSE expression in liver and kidney
-
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
-
the expression of CSE is increased by NaHS
-
enzyme expression levels are present only at a low level under sulfur sufficient (repressing) conditions
Q96VU7
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
Q96VU7
enzyme expression levels increase under sulfur limiting (derepressing) conditions
Q96VU7
enzyme expression levels are present only at a low level under sulfur sufficient (repressing) conditions
Neurospora crassa 74OR23-1a
-
-
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
Neurospora crassa 74OR23-1a
-
-
enzyme expression levels increase under sulfur limiting (derepressing) conditions
Neurospora crassa 74OR23-1a
-
-
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
-
the expression level and activity of cystathionine gamma-lyase is significantly decreased by methylglyoxal treatment (0.01-0.05 mM)
-
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
-
CSE mRNA and protein expression are upregulated by S-propargyl-cysteine
-
the level of CSE mRNA expression in liver are increased by hepatic ischemia-reperfusion
-
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
Rattus norvegicus Sprague-Dawley
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D187A
-
0.5% of wild-type activity, the mutation results in a loss of enzyme activity
E339A
-
the mutant demonstrates an approximately 6fold enhancement in H2S production, 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
E339K
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
E339Y
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
E349A
-
activity similar to wild-type
E349A
-
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
E349A
-
the mutant displays enzyme activity comparable to that for wild type enzyme
Q240E
-
missense mutation. Exhibits a 70fold decrease in Vmax compared to that of wild-type CGL. The KMs for L-cystathionine are comparable to that of wild type CGL. The pyridoxal 5'-phosphate content of the Q240E mutant is about 80fold lower than that of wild-type enzyme
R197C
-
the mutant shows about 44% activity compared to the wild type enzyme
R375A
-
2% of wild-type activity, the mutation results in a loss of enzyme activity
R62A
-
3% of wild-type activity, the mutation results in a loss of enzyme activity
R62H
-
exchange of Arg62 for His62 shifts the geometry of the active site, decreases the strength of pyridoxal 5'-phosphate binding, and makes this bond pH dependent under physiological conditions
S209A
-
activity similar to wild-type, the mutant displays enzyme activity comparable to that for wild type enzyme
T189A
-
0.5% of wild-type activity, the mutation results in a loss of enzyme activity
T211A
-
activity similar to wild-type, the mutant displays enzyme activity comparable to that for wild type enzyme
T311I
-
the mutant shows wild type activity
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
-
the mutation results in a loss of enzyme activity, 3% of wild-type activity, residue involved in binding of pyridoxal 5'-phosphate
Y114F
-
the mutation leads to significant increase in the production of H2S by CSE
Y60A
-
13% of wild-type activity, the mutation results in a severe decrease of enzyme activity
E333A
-
the mutation leads to 30fold reduction of kcat/Km for L-cystathionine
E333A
-
site-directed mutagenesis of the active-site residue, pH optimum 7.8-8.6, the mutant shows increased KM for L-cystathionine up to 17fold, and 2.5fold for O-acetyl-L-serine
E333D
-
site-directed mutagenesis of the active-site residue, pH optimum 7.2-8.0, the mutant shows increased KM for L-cystathionine up to 17fold, and 2.5fold for O-acetyl-L-serine
E333Q
-
site-directed mutagenesis of the active-site residue, pH optimum 7.6-8.4, the mutant shows increased KM for L-cystathionine up to 17fold, and 2.5fold for O-acetyl-L-serine
E333Y
-
the mutation leads to 30fold reduction of kcat/Km for L-cystathionine
E48A
-
the mutation leads to about 6fold reduction of kcat/Km for L-cystathionine
E48A
-
site-directed mutagenesis of the active-site residue, pH optimum 7.6-8.4
E48A/E333A
-
site-directed mutagenesis of the active-site residues, pH optimum 8.4-9.2
E48D
-
the mutation leads to about 5fold reduction of kcat/Km for L-cystathionine
E48D
-
site-directed mutagenesis of the active-site residue, pH optimum 7.07.8
E48D/E333D
-
site-directed mutagenesis of the active-site residues, pH optimum 7.6-8.4
E48F
-
the mutation leads to about 9fold reduction of kcat/Km for L-cystathionine
E48Q
-
site-directed mutagenesis of the active-site residue, pH optimum 7.4-8.2
K238A
-
mutant with complete loss of lyase and racemase activity
Y123F
-
mutant with decreased activity
Y123F/Y124F
-
mutant with decreased activity
Y124F
-
mutant with 50% of kcat for transamination of L- and D-alanine
Y64A
-
mutant with decreased PLP binding affinity
additional information
-
gene disruption mutants, lower cephalosporin production in Shens defined fermentation medium supplemented with methionine, but not in the same medium without methionine
additional information
Acremonium chrysogenum C10
-
gene disruption mutants, lower cephalosporin production in Shens defined fermentation medium supplemented with methionine, but not in the same medium without methionine
-
additional information
-
the total DES activity in mutants des1-1 and des1-2 plants is reduced by 20% to 25% in both mutants relative to their respective wild types
additional information
B2LXT6
various Aspergillus nidulans mutant strains (sconB, metR, metG, mecB, cysB)
K212A
-
the mutation results in a loss of enzyme activity, 1.3% of wild-type activity, residue involved in binding of pyridoxal 5'-phosphate
additional information
-
loss of enzyme activity in patients with hereditary cystathioninuria can be caused by nonsense mutations or by missense mutations
additional information
-
enzyme silencing by CSE-specific siRNA in HEK-293 cells, Hep-G2 cells, and IMR90 cells with loss of the protein band to at least 90% efficacy in the siRNA-transfected samples as compared with the scrambled-siRNA negative control
additional information
-
enzyme silencing by CSE-specific siRNA, treatment with acetoacetate and high D-glucose of 25 mM causes a significant decrease in enzyme protein expression compared with those in normal controls, while 4-hydroxybutyrate has no effect
Y60A
-
site-directed mutagenesis, inactive mutant, which cannot provide antioxidative activity
additional information
-
PNG902 and PNG903 strains (cgl, cyuC and mlp mutants), constructing a cgl mutant (PNG901) and comparing it to a similarly constructed cyuC mutant (PNG902). The growth defects in aerated cultures of both mutants are alleviated by supplementation with cysteine (and cystine in the cgl mutant) but not methionine, with the cyuC mutant showing a much higher requirement
additional information
Lactobacillus reuteri BR11
-
PNG902 and PNG903 strains (cgl, cyuC and mlp mutants), constructing a cgl mutant (PNG901) and comparing it to a similarly constructed cyuC mutant (PNG902). The growth defects in aerated cultures of both mutants are alleviated by supplementation with cysteine (and cystine in the cgl mutant) but not methionine, with the cyuC mutant showing a much higher requirement
-
additional information
-
CSE-/- mice and CSE-/+ mice, mice genetically deficient in this enzyme display marked hypertension, comparable to that of eNOS-/- mice
additional information
-
enzyme silencing by CSE-specific siRNA
additional information
Rattus norvegicus Sprague-Dawley
-
enzyme silencing by CSE-specific siRNA
-
E48Q/E333Q
-
site-directed mutagenesis of the active-site residues, pH optimum 7.9-8.7
additional information
-
pH optima of the mutant enzymes vary from wild-type enzyme, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
infection with Pyrenopeziza brassicae led to increased LCD activity
medicine
-
molecular basis of cystathioninuria, MIM 219500, revealed by mutations of enzyme
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
-
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
nutrition
-
Lactobacillus fermentum is contained in the natural starter used for producing Parmesan cheese and as adventitious non-starter lactic acid bacteria. It also populates several Italian and Swiss cheeses. EC 4.4.1.1 is stable in the conditions of cheese ripening and may contribute to the biosynthesis of sulfur-containing compounds
nutrition
Lactobacillus fermentum DT41
-
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
-
biotechnology
-
use of strain as adjunct starter in cheese making
medicine
-
inhibition of hydrogen sulfide synthesis attenuates chemokine production and protects mice against acute pancreatitis and associated lung injury
synthesis
-
effective at the end of trans-sulfuration pathway
synthesis
-
effective in detoxification and biotransformation of Se
synthesis
-
effective in metabolism of Se compounds
synthesis
-
effective at the end of trans-sulfuration pathway
medicine
-
physiologic importance of increased expression and activity of enzyme during lactation
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
-
CSE is not associated with dextran sulfate sodium-induced colitis in mice
synthesis
Q9EQS4
effective at the end of trans-sulfuration pathway
analysis
-
use in biosensor for measurement of L-cysteine
agriculture
Q5H4T8
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
-
CSE is not associated with dextran sulfate sodium-induced colitis in mice
additional information
-
H2S is a physiologic vasodilator and regulator of blood pressure
medicine
-
chronical treatment of rats with CGL inhibitor (DL)-propargylglycine or cystathionine beta-synthase inhibitor aminooxyacetic acid or a combination of both. Only the rats with combination therapy show a decrease in urinary sulfate excretion rate, which is associated with an increase in mean arterial pressure. Urine flow and sodium excretion are also increased in combination group as consequent to the increase in mean arterial pressure. Glomerular filtration rate does not alter due to these treatments, renal blood flow is lowered only in the combination group compared to the control group
additional information
-
H2S might be a novel insulin resistance regulator
additional information
-
insulin release is impaired in diabetic animals and inhibition of abnormally increased endogenous pancreatic H2S production in diabetes may represent a novel avenue for diabetes treatment
medicine
-
enzyme participates in hydrogen sulfide production in the oral cavity
additional information
-
H2S donors elicit pharmacological effect on ocular smooth muscle is of great interest and merits further investigation