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Enzyme Nomenclature
Information on EC 4.4.1.13 - cysteine-S-conjugate beta-lyase
for references in articles please use BRENDA:EC4.4.1.13
Word Map on EC 4.4.1.13
- 4.4.1.13
- renal
-
nephrotoxic
-
s-conjugates
-
aminooxyacetic
-
kynurenic
- pyridoxal
- s-1,2-dichlorovinyl-l-cysteine
-
mercapturic
-
transamination
-
halogenated
-
beta-elimination
-
alkene
- l-kynurenine
-
aminotransferases
-
haloalkenes
- kynureninase
- probenecid
- acivicin
- trichloroethylene
-
sevoflurane
- 3-hydroxykynurenine
-
xanthurenic
-
plp-dependent
-
hexachlorobutadiene
-
nephrocarcinogenicity
-
3-hydroxyanthranilic
- alpha-aminoadipate
-
5'-phosphate-dependent
- se-methylselenocysteine
- methylselenol
-
b6-dependent
-
thioacylating
- l-cystathionine
-
organ-selective
- agriculture
- nutrition
- medicine
- food industry
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
4.4.1.13
-
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RECOMMENDED NAME
GeneOntology No.
cysteine-S-conjugate beta-lyase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-aminoprop-2-enoate = 2-iminopropanoate
spontaneous
-
-
-
2-iminopropanoate + H2O = pyruvate + NH3
spontaneous
-
-
-
an L-cysteine-S-conjugate = a thiol + 2-aminoprop-2-enoate
(1a)
-
-
-
L-cystathionine = L-homocysteine + 2-aminoprop-2-enoate
(1a)
-
-
-
an L-cysteine-S-conjugate + H2O = a thiol + NH3 + pyruvate
overall reaction; R may represent aromatic compounds such as 4-bromobenzene and 2,4-dinitorbenzene
-
-
-
an L-cysteine-S-conjugate + H2O = a thiol + NH3 + pyruvate
activation energy for reaction with L-djenkolate is 53.1 kJ/mol
-
an L-cysteine-S-conjugate + H2O = a thiol + NH3 + pyruvate
stereochemistry
-
an L-cysteine-S-conjugate + H2O = a thiol + NH3 + pyruvate
with an amino acid containing a good leaving group in the beta position, beta-elemination is greatly favoured over transamination
-
L-cystathionine + H2O = L-homocysteine + pyruvate + NH3
overall reaction
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
of H2S or RSH, C-S bond cleavage; of RSH, C-S bond cleavage
-
transamination
additional information
additional information
-
shows identity with a soluble kynurenine aminotransferase from rat brain
additional information
-
identical with glutamine transaminase K
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-cysteine-S-conjugate thiol-lyase (deaminating; pyruvate-forming)
A pyridoxal-phosphate protein. The enzyme can act on a broad range of L-cysteine-S-conjugates, including aromatic conjugates such as 4-bromobenzene and 2,4-dinitrobenzene. The enzyme cleaves a carbon-sulfur bond, releasing a thiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase.
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CAS REGISTRY NUMBER
COMMENTARY
68652-57-3
-
9055-05-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional cystine C-S lyase and alanine aminotransferase, EC 2.6.1.2
-
-
-
-
-
a transducing phage lambda carrying the structural gene for beta-cystathionase; K-12
-
-
gene malY; strain ATCC 334 and several other genotypes, overview, gene malY
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
malfunction
-
the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
malfunction
-
the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
malfunction
-
the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
malfunction
-
enzyme inhibition reduces renal injuries due to cisplatin in rats. The cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
malfunction
-
the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
-
malfunction
-
the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
-
malfunction
-
the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
-
malfunction
-
enzyme inhibition reduces renal injuries due to cisplatin in rats. The cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
-
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
metabolism
cystathionine beta-lyase is part of the CYS3-controlled regulatory network
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
-
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
-
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
-
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
-
physiological function
-
expression in cells colonized in mice. CBL appears to be over-expressed in vivo after 2 and 6 h of infection
physiological function
cystathionine beta-lyase performs an essential role in the transsulfuration pathway by its primary reaction of forming homocysteine from cystathionine. It allows for the utilization of the intracellular pool of cystathionine for the synthesis of homocysteine which serves as the immediate precursor to methionine
physiological function
-
RNAi knockdown of the enzyme has no effect on phenotype
additional information
-
conserved residues W188 and W340 are situated at the core of the domain interface that forms the active-site cleft, W188 is a useful probe of subtle conformational changes at the domain interface and active site. The active site, containing the pyridoxal 5'-phosphate cofactor is situated at the interface between the catalytic (residues 61-256) and C-terminal (residues 257-395) domains. The N-terminal domain (residues 1-60) contributes to the active site of the neighboring subunit
additional information
-
cystathionine gamma-synthase, EC 2.5.1.48, and cystathionine beta-lyase sequence and structure comparison, both belonging to the gamma-subfamily of fold-type I, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-2-benzothiazolyl-L-cysteine + H2O
pyruvate + NH3 + 2-mercaptobenzothiazole
-
-
-
-
?
(S)-4-(4-methylpentan-2-one)-L-cysteine + H2O
4-mercapto-4-methylpentan-2-one + NH3 + pyruvate
-
Str3p is able to release 0.0123 mM 4-mercapto-4-methylpentan-2-one from 2 mM concentration of its precursor S-(2-methyl-4-oxopentan-2-yl)-L-cysteine
-
?
2-(2-(S)-L-cysteinylpentyl)-1,3-thiazolidine-4-carboxylic acid
3-mercaptohexanal + ?
-
-
-
?
alpha-keto-gamma-methiobutyric acid + L-aspartate
?
Monieza expansa
-
transamination reaction
-
?
L-cysteine S-sulfate + H2O
?
-
11% of the activity with L-cystine
-
?
L-cystine + H2O
?
22% activity compared to L-cystathionine
-
-
?
L-djenkolate + H2O
pyruvate + NH3 + ?
most effective substrate, 154% activity compared to L-cystathionine
-
-
?
L-djenkolic acid + H2O
?
-
18-24% of the activity with L-cystine, depending on assay method
-
?
L-methionine + H2O
methanethiol + dimethyl disulfide + dimethyl trisulfide + 2-oxobutyrate
O-succinyl-L-homoserine + H2O
2-oxobutyrate + succinate + NH3
MetC
-
-
?
S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
NH3 + pyruvate + 1,1,2,2-tetrafluoroethanethiol
-
-
-
-
?
S-(1,1,2,2-tetrafluoroethyl)-L-cysteine + H2O
NH3 + pyruvate + 1,1,2,2-tetrafluoroethanethiol
-
-
-
-
ir
S-(1,2-dichloroethenyl)-L-cysteine
pyruvate + NH3 + dichlorovinyl mercaptane
-
-
-
-
?
S-(1-hydroxyhexan-3-yl)-L-cysteine + H2O
3-mercaptohexan-1-ol + NH3 + pyruvate
-
Str3p is able to release 0.0021 mM 3-mercaptohexan-1-ol from 2 mM concentrations of its precursor (S)-3-(hexan-1-ol)-L-cysteine
-
?
S-1,2-dichlorovinyl-L-cysteine + H2O
dichlorovinyl mercaptane + NH3 + pyruvate
-
-
-
-
?
S-1,2-dichlorovinyl-L-cysteine + H2O
pyruvate + NH3 + dichlorovinyl mercaptane
-
-
-
-
?
S-4-(4-methylpentan-2-one)-L-cysteine + H2O
4-mercapto-4-methylpentan-2-one + NH3 + pyruvate
-
-
-
-
?
S-allyl-L-cysteine + H2O
NH3 + pyruvate + prop-2-ene-1-thiol
-
-
-
-
ir
S-allylmercapto-L-cysteine + H2O
NH3 + pyruvate + allyl hydrodisulfide
-
-
-
-
ir
S-ethyl-L-cysteine sulfoxide + H2O
?
-
71% of the activity with L-cystine
-
?
S-methylmercapto-L-cysteine + H2O
NH3 + pyruvate + methanethiol
-
-
-
-
ir
S-penta-1,3-dienylmercapto-L-cysteine + H2O
NH3 + pyruvate + penta-1,3-dien-1-yl hydrodisulfide
-
-
-
-
ir
S-propyl-L-cysteine + H2O
?
-
29% of the activity with L-cystine
-
?
S-propylmercapto-L-cysteine + H2O
NH3 + pyruvate + propyl hydrodisulfide
-
-
-
-
ir
S-[1-(2-hydroxymethyl)-1-methylbutyl]-L-cysteine + H2O
sulfanylhexanol + ?
-
very low activity
-
-
?
S-[1-(2-hydroxymethyl)-1-methylbutyl]-L-cysteinylglycine + H2O
sulfanylhexanol + ?
-
very low activity
-
-
?
S-[2-(fluoromethoxy)-1,1,3,3,3-pentafluoropropyl]-L-cysteine
pyruvate + ?
-
-
-
?
S-[2-(fluoromethoxy)-1,3,3,3-tetrafluoropropyl]-L-cysteine
pyruvate + ?
-
-
-
?
Se-(hydroselenomethyl)selenocysteine
bis(hydroseleno)methane + pyruvate + NH3
-
-
-
ir
Te-phenyl-L-tellurocysteine + H2O
NH3 + pyruvate + phenyltelluride
-
-
-
-
ir
(H2N)2Pt(Cl)SCH2CH(NH3+)CO2- + H2O
CH3C(O)CO2- + NH4+ + (NH2)2Pt(Cl)SH
-
-
-
-
?
(H2N)2Pt(Cl)SCH2CH(NH3+)CO2- + H2O
CH3C(O)CO2- + NH4+ + (NH2)2Pt(Cl)SH
-
-
-
-
?
(S)-2,4-dinitrophenyl-L-cysteine
2,4-dinitrobenzenethiol + pyruvate + NH3
-
-
-
-
?
(S)-2,4-dinitrophenyl-L-cysteine
2,4-dinitrobenzenethiol + pyruvate + NH3
-
-
-
?
(S)-2-benzothiazolyl-L-cysteine
pyruvate + NH3 + 2-mercaptobenzothiazole
-
-
-
-
?
(S)-2-benzothiazolyl-L-cysteine
pyruvate + NH3 + 2-mercaptobenzothiazole
-
-
-
?
(S)-4-bromophenyl-L-cysteine
p-bromobenzenethiol + NH3 + pyruvate
-
-
-
-
3-cysteinylhexanol
3-mercaptohexanal + ?
-
-
S-configuration of product preferred
?
3-cysteinylhexanol
3-mercaptohexanal + ?
-
-
R-configuration of product preferred
?
3-S-(N-acetyl-L-cysteinyl)-hexanal
3-mercaptohexanal + ?
-
-
S-configuration of product preferred
?
3-S-(N-acetyl-L-cysteinyl)-hexanal
3-mercaptohexanal + ?
-
-
R-configuration of product preferred
?
cystathionine + H2O
?
-
enzyme is involved in methionine biosynthesis
-
-
-
cystathionine + H2O
?
-
the second enzyme unique to methionine biosynthesis
-
-
-
cystathionine + H2O
?
-
enzyme is involved in methionine biosynthesis
-
-
-
cystathionine + H2O
?
-
enzyme is involved in methionine biosynthesis
-
-
-
cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
1-4% of the activity with L-cysteine, depending on assay method
-
?
DL-homocysteine + H2O
hydrogen sulfide + 2-oxobutyrate + ?
Ctl1 degrades DL-homocysteine at pH 5.5, while no activity is detected at pH 6.8 or 9.0
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + 2-oxobutyrate + ?
Ctl2 degrades DL-homocysteine at pH 5.5, while no activity is detected at pH 6.8 or 9.0
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
recombinant Ctl1 shows high activity toward the degradation of L-cystathionine
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
recombinant Ctl2 shows high activity toward the degradation of L-cystathionine
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
alpha,beta-elimination
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
100% activity
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
100% activity
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
no gamma-cleavage
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
penultimate step in microbial and plant methionine biosynthesis
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
the enzyme catalyzes the split of the a C-N and of the beta C-S bonds through a beta-elimination
-
-
?
L-cysteine + H2O
?
1.0% activity compared to L-cystathionine
-
-
?
L-cysteine + H2O
?
1.0% activity compared to L-cystathionine
-
-
?
L-cysteine + H2O
?
-
7.5% of the activity with cystathionine
-
-
?
L-cysteine + H2O
?
-
7.5% of the activity with cystathionine
-
-
?
L-cysteine + H2O
hydrogen sulfide + pyruvate + ?
Ctl1 degrades L-cysteine at pH 5.5, while no activity is detected at pH 6.8 or 9.0
-
-
?
L-cysteine + H2O
hydrogen sulfide + pyruvate + ?
Ctl2 degrades L-cysteine at pH 5.5, while no activity is detected at pH 6.8 or 9.0
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
very low activity
-
-
?
L-cystine + H2O
L-cysteine persulfide + pyruvate + NH4+
-
cystine is preferred over cysteine as substrate
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
-
64% of the activity with L-cystathionine
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
-
28% of the activity with L-cystathionine
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
-
28% of the activity with L-cystathionine
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
-
87% of the activity with cystathionine
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
-
87% of the activity with cystathionine
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
-
17% of the activity with L-cystathionine
-
-
?
L-djenkolate
pyruvate + NH3 + S-(mercaptomethyl)cysteine
-
-
-
-
?
L-djenkolate
pyruvate + NH3 + S-(mercaptomethyl)cysteine
-
-
-
-
?
L-djenkolate + H2O
pyruvate
-
58% of the activity with L-cystathionine
-
-
?
L-djenkolate + H2O
pyruvate
-
79% of the activity with L-cystathionine
-
-
?
L-djenkolate + H2O
pyruvate
-
79% of the activity with L-cystathionine
-
-
?
L-djenkolate + H2O
pyruvate
-
126% of the activity with L-cystathionine
-
-
?
L-homocysteine + H2O
?
-
5% of the activity with L-cystathionine
-
-
?
L-homocysteine + H2O
?
-
5% of the activity with L-cystathionine
-
-
?
L-methionine + H2O
methanethiol + dimethyl disulfide + dimethyl trisulfide + 2-oxobutyrate
Ctl1 degrades L-methionine at pH 5.5, while no activity is detected at pH 6.8 or 9.0
-
-
?
L-methionine + H2O
methanethiol + dimethyl disulfide + dimethyl trisulfide + 2-oxobutyrate
Ctl2 degrades L-methionine at pH 5.5, while no activity is detected at pH 6.8 or 9.0
-
-
?
L-Selenodjenkolate
Se-(hydroselenomethyl)selenocysteine + pyruvate + NH3
-
-
-
-
?
L-Selenodjenkolate
Se-(hydroselenomethyl)selenocysteine + pyruvate + NH3
-
-
-
-
?
L-Selenodjenkolate
Se-(hydroselenomethyl)selenocysteine + pyruvate + NH3
-
-
-
ir
lanthionine + H2O
L-cysteine + NH3 + pyruvate
-
169% of the activity with L-cystathionine
-
-
?
lanthionine + H2O
L-cysteine + NH3 + pyruvate
-
DL-lanthionine, 136% of the activity with L-cystathionine
-
-
?
lanthionine + H2O
L-cysteine + NH3 + pyruvate
-
DL-lanthionine, 136% of the activity with L-cystathionine
-
-
?
RSH-CH2-CH(NH3+)COO-
RSH + NH3 + pyruvate
-
R may represent aromatic compounds such as 4-bromobenzene and 2,4-dinitorbenzene
-
?
RSH-CH2-CH(NH3+)COO-
RSH + NH3 + pyruvate
-
R may represent aromatic compounds such as 4-bromobenzene and 2,4-dinitorbenzene
-
?
RSH-CH2-CH(NH3+)COO-
RSH + NH3 + pyruvate
-
R may represent aromatic compounds such as 4-bromobenzene and 2,4-dinitorbenzene
-
?
RSH-CH2-CH(NH3+)COO-
RSH + NH3 + pyruvate
-
R may represent aromatic compounds such as 4-bromobenzene and 2,4-dinitorbenzene
-
?
RSH-CH2-CH(NH3+)COO-
RSH + NH3 + pyruvate
-
R may represent aromatic compounds such as 4-bromobenzene and 2,4-dinitorbenzene
-
-
RSH-CH2-CH(NH3+)COO-
RSH + NH3 + pyruvate
-
R may represent aromatic compounds such as 4-bromobenzene and 2,4-dinitorbenzene
-
-
-
RSH-CH2-CH(NH3+)COO-
RSH + NH3 + pyruvate
-
R may represent aromatic compounds such as 4-bromobenzene and 2,4-dinitorbenzene
-
ir
S-(1,2-dichlorovinyl)-L-cysteine + H2O
NH3 + pyruvate + 1,2-dichloroethylenethiol
-
-
-
-
-
S-(1,2-dichlorovinyl)-L-cysteine + H2O
NH3 + pyruvate + 1,2-dichloroethylenethiol
-
-
-
-
ir
S-ethyl-L-cysteine
?
9.0% activity compared to L-cystathionine
-
-
-
S-ethyl-L-cysteine
?
9.0% activity compared to L-cystathionine
-
-
-
S-methyl-L-cysteine
methyl mercaptane + pyruvate + NH3
-
-
-
-
?
S-methyl-L-cysteine + H2O
?
-
13-29% of the activity with L-cystine, depending on assay method
-
?
S-methyl-L-cysteine + H2O
?
7.4% activity compared to L-cystathionine
-
-
?
S-methyl-L-cysteine + H2O
?
7.4% activity compared to L-cystathionine
-
-
?
S-methyl-L-cysteine sulfoxide
methyl methanethiolsulfinate + pyruvate + NH3
-
-
-
-
-
S-methyl-L-cysteine sulfoxide
methyl methanethiolsulfinate + pyruvate + NH3
-
-
-
-
Se-4-methoxybenzylselenocysteine + H2O
HSe(4-(CH3O)C6H4CH2) + pyruvate + NH3
-
-
-
-
?
Se-4-methoxybenzylselenocysteine + H2O
HSe(4-(CH3O)C6H4CH2) + pyruvate + NH3
-
-
-
-
?
Se-4-methoxybenzylselenocysteine + H2O
HSe(4-(CH3O)C6H4CH2) + pyruvate + NH3
-
-
-
-
?
Se-4-methoxybenzylselenocysteine + H2O
HSe(4-(CH3O)C6H4CH2) + pyruvate + NH3
-
-
-
-
?
Se-4-methoxybenzylselenocysteine + H2O
HSe(4-(CH3O)C6H4CH2) + pyruvate + NH3
-
-
-
-
?
Se-4-methoxybenzylselenocysteine + H2O
HSe(4-(CH3O)C6H4CH2) + pyruvate + NH3
-
-
-
-
?
Se-4-methoxybenzylselenocysteine + H2O
HSe(4-(CH3O)C6H4CH2) + pyruvate + NH3
-
-
-
-
?
thioethers
?
-
of L-cysteine, in which the amino acid's amino and carboxyl groups remain free
-
-
?
thioethers
?
-
of L-cysteine, in which the amino acid's amino and carboxyl groups remain free
-
-
?
thioethers
?
-
of L-cysteine, in which the amino acid's amino and carboxyl groups remain free
-
-
?
thioethers
?
-
of L-cysteine, in which the amino acid's amino and carboxyl groups remain free
-
-
?
thioethers
?
-
of L-cysteine, in which the amino acid's amino and carboxyl groups remain free
-
-
?
additional information
?
-
the enzyme catalyzes the penultimate step in de novo biosynthesis of Met in microbes and plants
-
?
additional information
?
-
-
two types of cystathionine beta-cleavage enzyme
-
-
-
additional information
?
-
-
osteotoxin is lethal for MC3T3-E1 osteogenic cells, fetal bovine trabecular cells, UMR106-01(BSP) rat osteosarcoma cells and embryonic bovine tracheal cells. The cytotoxicity can be attributed to: 1. beta-cystathionase-catalyzed cleavage of L-cystine in the medium and formation of reactive sulfane-containing derivatives, 2. Transfer of sulfane sulfur to metabolically sensitive or structurally important proteins in the osteogenic cells
-
-
-
additional information
?
-
-
the enzyme is responsible for off-aroma deterioration in fresh unblanched broccoli
-
?
additional information
?
-
-
not: D-cysteine derivatives, DL-homocysteine derivatives
-
-
-
additional information
?
-
-
stereochemical ananlyses of product
-
?
additional information
?
-
-
intestinal microflora: formation of methylthio-containing metabolites
-
-
-
additional information
?
-
-
enzyme shows transaminase activity against L-aspartate and L-alanine
-
?
additional information
?
-
-
cisplatin is bioactivated by the enzyme, renal toxicity of cisplatin results from enzyme activity, in contrast, carboplatin is not bioactivated
-
?
additional information
?
-
-
beta-lyase reactions with S-(1,1,2,2-tetrafluoroethyl)-L-cysteine, S-(1,2-dichlorovinyl)-L-cysteine, and Se-methyl-L-selenocysteine are more favorable than the GTK-catalyzed aminotransferase reactions with these amino acids
-
-
-
additional information
?
-
human KAT III/CCBL2, EC 2.6.1.7, possesses cysteine S-conjugate beta-lyase activity. KAtT III and glutamine transaminase L are identical enzymes
-
-
-
additional information
?
-
the enzyme is implicated in the degradation of not only cystathionine but also cysteine and methionine
-
-
-
additional information
?
-
-
the enzyme is implicated in the degradation of not only cystathionine but also cysteine and methionine
-
-
-
additional information
?
-
the enzyme performs a beta-elimination reaction, substrate specificity and product determination, overview
-
-
-
additional information
?
-
-
the enzyme performs a beta-elimination reaction, substrate specificity and product determination, overview
-
-
-
additional information
?
-
enzyme also is able to catalyze an alpha,gamma-elimination
-
?
additional information
?
-
-
enzyme also is able to catalyze an alpha,gamma-elimination
-
?
additional information
?
-
with methionine as substrate the enzyme produces volatile sulfur compounds which are important for flavor formation in Gouda cheese
-
?
additional information
?
-
-
with methionine as substrate the enzyme produces volatile sulfur compounds which are important for flavor formation in Gouda cheese
-
?
additional information
?
-
-
not: D-cysteine derivatives, DL-homocysteine derivatives
-
-
-
additional information
?
-
-
not: D-cysteine derivatives, DL-homocysteine derivatives
-
-
-
additional information
?
-
-
not: D-cysteine derivatives, DL-homocysteine derivatives
-
-
-
additional information
?
-
-
the 4-nitrophenylethyl, benzyl, methyl, 2-chloroethyl, butyl thioethers of cysteine
-
-
-
additional information
?
-
-
not: D-cysteine derivatives, DL-homocysteine derivatives
-
-
-
additional information
?
-
-
kinetic analyses and comparison of beta-elimination reaction and transamination reaction for differentially substituted cysteine-S-conjugates and selenocysteine Se-conjugates
-
?
additional information
?
-
-
no reaction with S-benzothiazolyl-L-cysteine
-
-
-
additional information
?
-
-
cysteine S-conjugate beta-lyases catalyze beta-elimination reactions with cysteine S-conjugates that possess a good leaving group in the beta-position. The end products are aminoacrylate and a sulfur-containing fragment. The aminoacrylate tautomerizes and hydrolyzes to pyruvate and ammonia.
-
-
-
additional information
?
-
Irc7p, a putative cystathionine beta-lyase, is one of the main proteins catalyzing the 4-methyl-4-sulfanylpentan-2-one and 3-sulfanylhexan-1-ol, as aromatic compounds, release from inodorous nonvolatile cysteinylated precursors under enological conditions. The two other beta-lyases Ure2p and Gln3p mainly control the bioconversion of volatile thiols by the transcriptional regulation of the IRC7 gene through the general mechanism of nitrogen catabolic repression
-
-
-
additional information
?
-
Irc7p is a specifically stereoselective enzyme
-
-
-
additional information
?
-
no alpha-ketobutyrate is detected with any of the substrates susceptible for beta-lyase activity, confirming that Str3p has only beta-lyase activity. L-methionine is no substrate for Str3p
-
-
-
additional information
?
-
no alpha-ketobutyrate is detected with any of the substrates susceptible for beta-lyase activity, confirming that Str3p has only beta-lyase activity. L-methionine is no substrate for Str3p
-
-
-
additional information
?
-
-
the enzyme catalyzes the penultimate step in methionine biosynthesis. The enzyme is important for bacterial virulence
-
-
-
additional information
?
-
the enzyme plays a central role in methionine biosynthesis
-
?
additional information
?
-
-
no activity with cysteine, cysteinyl, or cysteinylglycine-S-precursors (S-[1-(2-hydroxymethyl)-1-methylbutyl]-lcysteinylglycine and S-[1-(2-hydroxymethyl)-1-methylbutyl]-l-cysteine)
-
-
-
additional information
?
-
Q9EYM7
the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
-
?
additional information
?
-
Q9EYM7
the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
-
?
additional information
?
-
-
the catalytic mechanism is proposed involving interactions between cystine and active site residues Arg360, Arg369, and Trp251. These residues reorient during beta-elimination reaction, leading to the formation of a hydrophobic pocket that stabilizes the enolimine tautomer of the aminoacrylate and the cysteine persulfide product
-
?
additional information
?
-
-
enzyme displays both cystine C-S lyase activity and alanine aminotransferase activity, Ec 2.6.1.2. No in vitro tyrosine aminotransferase activity is detetced
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
cystathionine + H2O
?
-
enzyme is involved in methionine biosynthesis
-
-
-
cystathionine + H2O
?
-
the second enzyme unique to methionine biosynthesis
-
-
-
cystathionine + H2O
?
-
enzyme is involved in methionine biosynthesis
-
-
-
cystathionine + H2O
?
-
enzyme is involved in methionine biosynthesis
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
E3VL26
100% activity
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
E3VL26
100% activity
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
-
penultimate step in microbial and plant methionine biosynthesis
-
-
?
additional information
?
-
P53780
the enzyme catalyzes the penultimate step in de novo biosynthesis of Met in microbes and plants
-
?
additional information
?
-
-
the enzyme is responsible for off-aroma deterioration in fresh unblanched broccoli
-
?
additional information
?
-
-
intestinal microflora: formation of methylthio-containing metabolites
-
-
-
additional information
?
-
-
cisplatin is bioactivated by the enzyme, renal toxicity of cisplatin results from enzyme activity, in contrast, carboplatin is not bioactivated
-
?
additional information
?
-
A6YH85
the enzyme is implicated in the degradation of not only cystathionine but also cysteine and methionine
-
-
-
additional information
?
-
-
the enzyme is implicated in the degradation of not only cystathionine but also cysteine and methionine
-
-
-
additional information
?
-
A2RM21
with methionine as substrate the enzyme produces volatile sulfur compounds which are important for flavor formation in Gouda cheese
-
?
additional information
?
-
-
with methionine as substrate the enzyme produces volatile sulfur compounds which are important for flavor formation in Gouda cheese
-
?
additional information
?
-
-
cysteine S-conjugate beta-lyases catalyze beta-elimination reactions with cysteine S-conjugates that possess a good leaving group in the beta-position. The end products are aminoacrylate and a sulfur-containing fragment. The aminoacrylate tautomerizes and hydrolyzes to pyruvate and ammonia.
-
-
-
additional information
?
-
P43623
Irc7p, a putative cystathionine beta-lyase, is one of the main proteins catalyzing the 4-methyl-4-sulfanylpentan-2-one and 3-sulfanylhexan-1-ol, as aromatic compounds, release from inodorous nonvolatile cysteinylated precursors under enological conditions. The two other beta-lyases Ure2p and Gln3p mainly control the bioconversion of volatile thiols by the transcriptional regulation of the IRC7 gene through the general mechanism of nitrogen catabolic repression
-
-
-
additional information
?
-
-
the enzyme catalyzes the penultimate step in methionine biosynthesis. The enzyme is important for bacterial virulence
-
-
-
additional information
?
-
Q9MT31
the enzyme plays a central role in methionine biosynthesis
-
?
additional information
?
-
Q9EYM7
the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
-
?
additional information
?
-
Q9EYM7
the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
5.7 mol of pyridoxal 5'-phosphate is bound per mol of enzyme; Km: 0.005 mM
pyridoxal 5'-phosphate
-
the pyridoxal 5'-phosphate binding site shows the tripeptide sequence Thr-Lys(Pxy)-Tyr in their structure
pyridoxal 5'-phosphate
-
each subunit of the tetramer is associated with one molecule of pyridoxal 5'-phosphate. Schiff-base formation between the cofactor and the holoenzyme occurs at Lys278
pyridoxal 5'-phosphate
-
each subunit of the dimer contains one molecule of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
the coenzyme strongly increases the protein stability. It is essential for the step involving dissociation of dimer into monomers and is not required for refolding of single monomers, but it is necessary to attain the native dimeric structure critical for the biological activities of MalY
pyridoxal 5'-phosphate
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(4-chlorophenyl)-3-[4-(6-methyl-1,3-benzothiazol-2-yl)phenyl]urea
-
reversible inhibition
1-[3-(3,4-dichlorophenyl)isoxazol-5-yl]-2-[(4-thiophen-2-ylpyrimidin-2-yl)sulfanyl]ethanone
-
reversible inhibition
2,3,5-trifluoro-N-(2-hydrazino-2-oxoethyl)-4-methoxybenzamide
-
only poor inhibitor
2-bromobenzyl (9Z)-9-(hydroxyimino)-2,7-dinitro-9H-fluorene-4-carboxylate
-
hydrolysis of the oxime to generate hydroxylamine in situ that interacted with the PLP cofactor
3,3,3-trifluoro-N-(2-methylphenyl)-2-(trifluoromethyl)propanamide
-
reversible inhibition
3,4-dichlorobenzenesulfonohydrazide
-
known to interact with the cofactor of PLP enzymes
3-amino-N-(2-hydrazino-2-oxoethyl)naphthalene-2-carboxamide
-
only poor inhibitor
4-chloro-N-[4-(6-methyl-1,3-benzothiazol-2-yl)phenyl]benzamide
-
reversible inhibition
4-methylbenzenesulfonohydrazide
-
known to interact with the cofactor of PLP enzymes
5-aminonaphthalene-1-sulfonohydrazide
-
known to interact with the cofactor of PLP enzymes
5-chlorothiophene-2-sulfonohydrazide
-
known to interact with the cofactor of PLP enzymes
5-pyridin-2-ylthiophene-2-sulfonohydrazide
-
known to interact with the cofactor of PLP enzymes
diphenyl 9-(dicyanomethylidene)-4,5-dinitro-9H-fluorene-2,7-disulfonate
-
reversible inhibition
L-cystathionine
-
substrate inhibition at concentrations above 6 mM
L-cysteine
-
12 mM, 65% inhibition after 5 min, 1 mM, 29% inhibition after 10 min, linear noncompetitive inhibitor
N-(2-hydrazino-2-oxoethyl)-2-nitrobenzamide
-
known to interact with the cofactor of PLP enzymes
N-[4-(hydrazinosulfonyl)benzyl]acetamide
-
known to interact with the cofactor of PLP enzymes
pyridoxal
-
12.5 mM, in presence of 12 mM L-cystine 12% inhibition, in presence of 1 mM L-cystine 37% inhibition
S-methyl-L-cysteine
-
substrate inhibition, when concentration exceeds 10 mM
NaCl
in the presence of 4% (w/v) NaCl the reaction rate of Ctl1 is decreased to 40% of the original rate at pH 5.5; in the presence of 4% (w/v) NaCl the reaction rate of Ctl2 is decreased to 40% of the original rate at pH 5.5
rhizobitoxine
-
complete inhibition at 0.001 mM
rhizobitoxine
-
reactivation by incubation with pyridoxal 5'-phosphate, the substrates cystathionine and djenkolate, as well as the competitive inhibitor beta-cyanoalanine protects
additional information
-
the enzyme is not inhibited by pyridamine antimicrobial agents (pyrimethanil, cyprodinil or mepanipyrim)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CYS3
a bZIP transcriptional activator, is the key regulator and necessary for regulation expression of the sulfur-related genes, binds on a consensus sequence for CYS3 binding
-
NaCl
NaCl considerably enhances the reaction rate at pH 6.8; NaCl considerably enhances the reaction rate at pH 6.8
TTHA1554
-
when an 8fold excess of TTHA1554 is added to TTHA1620, the cystathionine beta-lyase activity of TTHA1620 increases approximately 2fold
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.096
L-cystathionine
in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37°C
0.148
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F/W300F
0.171
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131FF/W230FF/W276F
0.27
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F
0.31
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W230F/W276F/W300F
0.33
L-cystathionine
Ctl2, in sodium phosphate buffer, at pH 5.5 and 37°C
0.35
L-cystathionine
Ctl1, in sodium phosphate buffer, at pH 5.5 and 37°C
0.37
L-cystathionine
Ctl1, in sodium phosphate buffer, at pH 6.8 and 37°C
0.41
L-cystathionine
Ctl2, in sodium phosphate buffer, at pH 6.8 and 37°C
1
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W230F/W276F/W340F
1.05
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W276F/W300F/W340F
1.26
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W230F/W276F/W300F/W340F
1.8
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F/W300F/W340F; pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F/W340F
2
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W188F/W230F/W276F/W300F/W340F
2.1
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W300F/W340F
3.8
L-cystathionine
-
pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sC-eCBL
0.29
L-cysteine
-
in presence of 10 mM dithiothreitol
0.178
L-djenkolate
in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37°C
additional information
additional information
-
kinetic parameters for differentially substituted cysteine-S-conjugates and selenocysteine Se-conjugates
-
additional information
additional information
-
kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.27
L-djenkolate
in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37°C
0.91
L-cystathionine
in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37°C
6.8
L-cystathionine
-
pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sC-eCBL
25.4
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F
31.7
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F/W300F
35.1
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W276F/W300F/W340F
38
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W300F/W340F
40
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F/W340F
42
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W188F/W230F/W276F/W300F/W340F
46
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F/W300F/W340F
54
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W230F/W276F/W300F/W340F
54.5
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131FF/W230FF/W276F; pH 8.5, 25°C, recombinant wild-type enzyme
65
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W230F/W276F/W340F
74
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W230F/W276F/W300F
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.76
L-cystathionine
-
pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sC-eCBL
9.8
L-cystathionine
-
pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sN-eCBL
18
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W300F/W340F
21
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W188F/W230F/W276F/W300F/W340F
23
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F/W340F
25
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F/W300F/W340F
33
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W276F/W300F/W340F
43
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W230F/W276F/W300F/W340F
66
L-cystathionine
-
pH 8.5, 25°C, recombinant mutants W340F and W131F/W230F/W276F/W340F
94
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F
213
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F/W300F
240
L-cystathionine
-
pH 8.5, 25°C, recombinant mutant W131F/W230F/W276F/W300F