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Information on EC 4.4.1.1 - cystathionine gamma-lyase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P31373
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4.4.1.1 cystathionine gamma-lyaseIUBMB Comments
A multifunctional pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing L-cysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also catalyses the conversion of L-homoserine to 2-oxobutanoate and ammonia, of L-cystine to thiocysteine, pyruvate and ammonia, and of L-cysteine to pyruvate, hydrogen sulfide and ammonia.
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Word Map
- 4.4.1.1
- sulfide
- h2s
- nahs
- beta-synthase
- sulfur
- homocysteine
-
transsulfuration
- pyridoxal
- propargylglycine
- dl-propargylglycine
-
gasotransmitter
- cystathionine-beta-synthase
- sulfurtransferase
-
gaseous
- 3-mercaptopyruvate
-
sulfur-containing
- hydrosulfide
- treponema
- hyperhomocysteinemia
-
adenosyltransferase
- l-methionine
-
desulfuration
- glibenclamide
-
beta-lyase
- denticola
-
vasorelaxation
- hypotaurine
- rhodanese
- persulfide
- alpha-ketobutyrate
- d-cysteine
- ppg
-
s-sulfhydration
-
h2s-producing
-
h2s-generating
- medicine
-
cowden
-
gamma-synthase
- synthesis
-
sulfhydrylase
- analysis
-
aminooxyacetic
- o-acetylserine
-
h2s-induced
-
remethylation
- agriculture
-
cysteinesulfinate
- nutrition
- l-homoserine
- biotechnology
- cys3
-
aldimine
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
cystathionine gamma-lyase, cystathionase, gamma-cystathionase, cystathionine-gamma-lyase, cs-like, cysteine desulfhydrase, l-cysteine desulfhydrase, cystalysin, cystathionine gamma lyase, prb-ra, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cystalysin
-
-
-
-
cystathionase
-
-
-
-
cystathioninase
-
-
-
-
cystathionine gamma-lyase
cysteine desulfhydrase
-
-
-
-
cysteine lyase
-
-
-
-
cystine desulfhydrase
-
-
-
-
dehydratase, homoserine
-
-
-
-
desulfhydrase, cysteine
-
-
-
-
gamma-CTL
-
-
-
-
gamma-cystathionase
-
-
-
-
homoserine deaminase
-
-
-
-
homoserine deaminase-cystathionase
-
-
-
-
homoserine dehydratase
-
-
-
-
lyase, cystathionine gamma-
-
-
-
-
PRB-RA
-
-
-
-
Probasin-related antigen
-
-
-
-
cystathionine gamma-lyase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-cystathionine + H2O = L-cysteine + 2-oxobutanoate + NH3
mechanism
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY
9012-96-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutanoate
-
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
cystathionine gamma-lyase encoded by CYS3 is repressed by addition of cysteine to the growth medium
-
additional information
-
cystathionine gamma-lyase encoded by CYS3 is repressed by addition of cysteine to the growth medium
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
cystathionine gamma-lyase encoded by CYS3 is induced by sulfur starvation
-
additional information
-
cystathionine gamma-lyase encoded by CYS3 is induced by sulfur starvation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.42
L-cystathionine
-
His-tagged recombinant wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.45
L-cystathionine
-
native wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.81
L-cystathionine
-
mutant enzyme E48F, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.82
L-cystathionine
-
mutant enzyme E48A, in 50 mM potassium phosphate, pH 7.8, at 25°C
1.11
L-cystathionine
-
mutant enzyme E48D, in 50 mM potassium phosphate, pH 7.8, at 25°C
5.2
L-cystathionine
-
mutant enzyme E333A, in 50 mM potassium phosphate, pH 7.8, at 25°C
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.39
L-cystathionine
-
mutant enzyme E48F, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.67
L-cystathionine
-
mutant enzyme E48A, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.69
L-cystathionine
-
mutant enzyme E333A, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.76
L-cystathionine
-
mutant enzyme E48D, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.9
L-cystathionine
-
native wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
1.81
L-cystathionine
-
His-tagged recombinant wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.0035
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48D/E333D
0.0047
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48A/E333A
0.0092
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48Q/E333Q
0.0097
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0037
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48A/E333A
0.0088
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48D/E333D
0.0169
L-cystathionine
-
pH 7.2, 25°C, recombinant mutant E48Q/E333Q
0.132
L-cystathionine
-
mutant enzyme E333A, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.147
L-cystathionine
-
mutant enzyme E333Y, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.49
L-cystathionine
-
mutant enzyme E48F, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.68
L-cystathionine
-
mutant enzyme E48D, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.82
L-cystathionine
-
mutant enzyme E48A, in 50 mM potassium phosphate, pH 7.8, at 25°C
1.98
L-cystathionine
-
native wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
4.3
L-cystathionine
-
His-tagged recombinant wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C
0.0016
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48A/E333A
0.0038
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant wild-type enzyme and mutant E48D
0.005
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48D/E333D
0.006
O-acetyl-L-serine
-
pH 7.2, 25°C, recombinant mutant E48Q/E333Q
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
-
0.1 M potassium phosphate buffer, pH 7.8, 0.2 mM pyridoxal-5'-phosphate and 1 mM EDTA
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
-
pH optima of the mutant enzymes vary from wild-type enzyme, overview
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
-
rapid loss of activity at 60°C, 0.1 M potassium phosphate buffer, pH 7.8, 0.2 mM pyridoxal-5'-phosphate and 1 mM EDTA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, butyl-Toyopearl 650M resin column chromatography, and DEAE column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the His-tagged enzyme is expressed in Escherichia coli KS1000 cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamagata, S.; D'Andrea, R.J.; Fujisaki, S.; Isaji, M.; Nakamura, K.
Cloning and bacterial expression of the CYS3 gene encoding cystathionine gamma-lyase of Saccharomyces cerevisiae and the physicochemical and enzymatic properties of the protein
J. Bacteriol.
175
4800-4808
1993
Saccharomyces cerevisiae
Messerschmidt, A.; Worbs, M.; Steegborn, C.; Wahl, M.C.; Huber, R.; Laber, B.; Clausen, T.
Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: crystal structure of cystathionine gamma-lyase from yeast and intrafamiliar structure comparison
Biol. Chem.
384
373-386
2003
Saccharomyces cerevisiae
Yamagata, S.; Isaji, M.; Yamane, T.; Iwama, T.
Substrate inhibition of L-cysteine alpha,beta-elimination reaction catalyzed by L-cystathionine gamma-lyase of Saccharomyces cerevisiae
Biosci. Biotechnol. Biochem.
66
2706-2709
2002
Saccharomyces cerevisiae
Yamagata, S.; Yasugahira, T.; Okuda, Y.; Iwama, T.
Conversion of the aminocrotonate intermediate limits the rate of gamma-elimination reaction catalyzed by L-cystathionine gamma-lyase of the yeast Saccharomyces cerevisiae
J. Biochem.
134
607-613
2003
Saccharomyces cerevisiae
Yamagata, S.; Akamatsu, T.; Iwama, T.
Immobilization of Saccharomyces cerevisiae cystathionine gamma-lyase and application of the product to cystathionine synthesis
Appl. Environ. Microbiol.
70
3766-3768
2004
Saccharomyces cerevisiae
Gente, S.; La Carbona, S.; Gueguen, M.
Levels of cystathionine gamma lyase production by Geotrichum candidum in synthetic media and correlation with the presence of sulphur flavours in cheese
Int. J. Food Microbiol.
114
136-142
2007
Saccharomyces cerevisiae, Geotrichum candidum, Limosilactobacillus fermentum, Limosilactobacillus reuteri, Lactococcus lactis
Hiraishi, H.; Miyake, T.; Ono, B.
Transcriptional regulation of Saccharomyces cerevisiae CYS3 encoding cystathionine gamma-lyase
Curr. Genet.
53
225-234
2008
Saccharomyces cerevisiae (P31373), Saccharomyces cerevisiae
Farsi, A.; Lodha, P.H.; Skanes, J.E.; Los, H.; Kalidindi, N.; Aitken, S.M.
Interconversion of a pair of active-site residues in Escherichia coli cystathionine gamma-synthase, E. coli cystathionine beta-lyase, and Saccharomyces cerevisiae cystathionine gamma-lyase and development of tools for the investigation of their mechanisms
Biochem. Cell Biol.
87
445-457
2009
Saccharomyces cerevisiae
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