4.4.1.1: cystathionine gamma-lyase
This is an abbreviated version!
For detailed information about cystathionine gamma-lyase, go to the full flat file.
Word Map on EC 4.4.1.1
-
4.4.1.1
-
sulfide
-
h2s
-
nahs
-
beta-synthase
-
sulfur
-
homocysteine
-
transsulfuration
-
pyridoxal
-
propargylglycine
-
dl-propargylglycine
-
gasotransmitter
-
cystathionine-beta-synthase
-
sulfurtransferase
-
gaseous
-
3-mercaptopyruvate
-
sulfur-containing
-
hydrosulfide
-
treponema
-
hyperhomocysteinemia
-
adenosyltransferase
-
l-methionine
-
desulfuration
-
glibenclamide
-
beta-lyase
-
denticola
-
vasorelaxation
-
hypotaurine
-
rhodanese
-
persulfide
-
alpha-ketobutyrate
-
d-cysteine
-
ppg
-
s-sulfhydration
-
h2s-producing
-
h2s-generating
-
medicine
-
cowden
-
gamma-synthase
-
synthesis
-
sulfhydrylase
-
analysis
-
aminooxyacetic
-
o-acetylserine
-
h2s-induced
-
remethylation
-
agriculture
-
cysteinesulfinate
-
nutrition
-
l-homoserine
-
biotechnology
-
cys3
-
aldimine
- 4.4.1.1
- sulfide
- h2s
- nahs
- beta-synthase
- sulfur
- homocysteine
-
transsulfuration
- pyridoxal
- propargylglycine
- dl-propargylglycine
-
gasotransmitter
- cystathionine-beta-synthase
- sulfurtransferase
-
gaseous
- 3-mercaptopyruvate
-
sulfur-containing
- hydrosulfide
- treponema
- hyperhomocysteinemia
-
adenosyltransferase
- l-methionine
-
desulfuration
- glibenclamide
-
beta-lyase
- denticola
-
vasorelaxation
- hypotaurine
- rhodanese
- persulfide
- alpha-ketobutyrate
- d-cysteine
- ppg
-
s-sulfhydration
-
h2s-producing
-
h2s-generating
- medicine
-
cowden
-
gamma-synthase
- synthesis
-
sulfhydrylase
- analysis
-
aminooxyacetic
- o-acetylserine
-
h2s-induced
-
remethylation
- agriculture
-
cysteinesulfinate
- nutrition
- l-homoserine
- biotechnology
- cys3
-
aldimine
Reaction
Synonyms
AFUA_8G04340, C-S-lyase, C-S-lyase1, C-S-lyase2, C-S-lyase3, C-S-lyase4, cgl, CGL like protein, CS-LIKE, CSE, CSEgamma, CTH, CTT, cystalysin, cystathionase, cystathioninase, cystathionine beta/gamma-lyase, cystathionine gamma lyase, cystathionine gamma-lyase, cystathionine gamma-lyase-like protein, cystathionine-gamma-lyase, cysteine desulfhydrase, cysteine lyase, cystine desulfhydrase, dehydratase, homoserine, DES1, desulfhydrase, cysteine, EC 4.2.1.15, gamma-CTL, gamma-CTLase, gamma-cystathionase, hCSE, homoserine deaminase, homoserine deaminase-cystathionase, homoserine dehydratase, human cystathionine-gamma-lyase, L-Cys desulfhydrase, L-cysteine desulfhydrase, L-cysteine desulphydrase, L-cysteine-desulfhydrase, LCD, lyase, cystathionine gamma-, PRB-RA, Probasin-related antigen, TGME49_112930, XometC, yCGL
ECTree
4.4.1.1 cystathionine gamma-lyaseAdvanced search results
results (
results (Engineering
Engineering on EC 4.4.1.1 - cystathionine gamma-lyase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D187A
E339A
E339K
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
E339Y
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
E349A
E59N/R119L/E339V
mutant engineered as an L-Met-degrading enzyme based on the human cystathionine-gamma-lyase
K212A
Q240E
missense mutation. Exhibits a 70fold decrease in Vmax compared to that of wild-type CGL. The KMs for L-cystathionine are comparable to that of wild type CGL. The pyridoxal 5'-phosphate content of the Q240E mutant is about 80fold lower than that of wild-type enzyme
R197C
the mutant shows about 44% activity compared to the wild type enzyme
R375A
R62A
R62H
exchange of Arg62 for His62 shifts the geometry of the active site, decreases the strength of pyridoxal 5'-phosphate binding, and makes this bond pH dependent under physiological conditions
S209A
T189A
T211A
T67I
Y114A
Y114F
-
the mutation leads to significant increase in the production of H2S by CSE
Y60A
E333A
E333D
-
site-directed mutagenesis of the active-site residue, pH optimum 7.2-8.0, the mutant shows increased KM for L-cystathionine up to 17fold, and 2.5fold for O-acetyl-L-serine
E333Q
-
site-directed mutagenesis of the active-site residue, pH optimum 7.6-8.4, the mutant shows increased KM for L-cystathionine up to 17fold, and 2.5fold for O-acetyl-L-serine
E333Y
-
the mutation leads to 30fold reduction of kcat/Km for L-cystathionine
E48A
E48A/E333A
-
site-directed mutagenesis of the active-site residues, pH optimum 8.4-9.2
E48D
E48D/E333D
-
site-directed mutagenesis of the active-site residues, pH optimum 7.6-8.4
E48F
-
the mutation leads to about 9fold reduction of kcat/Km for L-cystathionine
E48Q
-
site-directed mutagenesis of the active-site residue, pH optimum 7.4-8.2
E48Q/E333Q
-
site-directed mutagenesis of the active-site residues, pH optimum 7.9-8.7
N360S
mutation does not alter enzyme conformation, but leads to a 56fold decrease in catalyic efficiency for L-cystathionine
N360S
-
mutation does not alter enzyme conformation, but leads to a 56fold decrease in catalyic efficiency for L-cystathionine
-
additional information
E339A
-
the mutant demonstrates an approximately 6fold enhancement in H2S production
E339A
site-directed mutagenesis, the hyperactive mutant displays a 4fold greater H2S production compared to the wild-type enzyme
E349A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
E349A
-
the mutant displays enzyme activity comparable to that for wild type enzyme
K212A
-
1.3% of wild-type activity, residue involved in binding of pyridoxal 5'-phosphate
S209A
-
the mutant displays enzyme activity comparable to that for wild type enzyme
T211A
-
the mutant displays enzyme activity comparable to that for wild type enzyme
T67I
missense mutation. Exhibits a 3.5fold decrease in Vmax compared to that of wild-type CGL. The KMs for L-cystathionine are comparable to that of wild type CGL. The pyridoxal 5'-phosphate content of the T67I mutant is about 4fold lower than that of wild-type enzyme
T67I
the mutant shows about 13% activity compared to the wild type enzyme
Y114A
-
3% of wild-type activity, residue involved in binding of pyridoxal 5'-phosphate
Y60A
site-directed mutagenesis, inactive mutant, which cannot provide antioxidative activity
E333A
-
the mutation leads to 30fold reduction of kcat/Km for L-cystathionine
E333A
-
site-directed mutagenesis of the active-site residue, pH optimum 7.8-8.6, the mutant shows increased KM for L-cystathionine up to 17fold, and 2.5fold for O-acetyl-L-serine
E48A
-
the mutation leads to about 6fold reduction of kcat/Km for L-cystathionine
E48A
-
site-directed mutagenesis of the active-site residue, pH optimum 7.6-8.4
E48D
-
the mutation leads to about 5fold reduction of kcat/Km for L-cystathionine
E48D
-
site-directed mutagenesis of the active-site residue, pH optimum 7.07.8
additional information
-
gene disruption mutants, lower cephalosporin production in Shens defined fermentation medium supplemented with methionine, but not in the same medium without methionine
additional information
Acremonium chrysogenum C10 / ATCC 48272
-
gene disruption mutants, lower cephalosporin production in Shens defined fermentation medium supplemented with methionine, but not in the same medium without methionine
-
additional information
-
the total DES activity in mutants des1-1 and des1-2 plants is reduced by 20% to 25% in both mutants relative to their respective wild types
additional information
various Aspergillus nidulans mutant strains (sconB, metR, metG, mecB, cysB)
additional information
-
various Aspergillus nidulans mutant strains (sconB, metR, metG, mecB, cysB)
additional information
-
loss of enzyme activity in patients with hereditary cystathioninuria can be caused by nonsense mutations or by missense mutations
additional information
enzyme silencing by CSE-specific siRNA in HEK-293 cells, Hep-G2 cells, and IMR90 cells with loss of the protein band to at least 90% efficacy in the siRNA-transfected samples as compared with the scrambled-siRNA negative control
additional information
-
enzyme silencing by CSE-specific siRNA, treatment with acetoacetate and high D-glucose of 25 mM causes a significant decrease in enzyme protein expression compared with those in normal controls, while 4-hydroxybutyrate has no effect
additional information
-
PNG902 and PNG903 strains (cgl, cyuC and mlp mutants), constructing a cgl mutant (PNG901) and comparing it to a similarly constructed cyuC mutant (PNG902). The growth defects in aerated cultures of both mutants are alleviated by supplementation with cysteine (and cystine in the cgl mutant) but not methionine, with the cyuC mutant showing a much higher requirement
additional information
-
PNG902 and PNG903 strains (cgl, cyuC and mlp mutants), constructing a cgl mutant (PNG901) and comparing it to a similarly constructed cyuC mutant (PNG902). The growth defects in aerated cultures of both mutants are alleviated by supplementation with cysteine (and cystine in the cgl mutant) but not methionine, with the cyuC mutant showing a much higher requirement
-
additional information
-
CSE-/- mice and CSE-/+ mice, mice genetically deficient in this enzyme display marked hypertension, comparable to that of eNOS-/- mice
additional information
-
pH optima of the mutant enzymes vary from wild-type enzyme, overview
