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Information on EC 4.4.1.13 - cysteine-S-conjugate beta-lyase
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EC Tree
4.4.1.13 cysteine-S-conjugate beta-lyaseIUBMB Comments
A pyridoxal-phosphate protein. The enzyme is promiscuous regarding the moiety conjugated to L-cysteine, and can accept both aliphatic and aromatic substitutions. 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. While bacteria and plants have dedicated enzymes, all of the animal enzymes discovered thus far are bifunctional, most of which also act as aminotransferases.
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Word Map
- 4.4.1.13
-
nephrotoxic
-
kynurenic
-
s-conjugates
-
aminooxyacetic
- pyridoxal
- s-1,2-dichlorovinyl-l-cysteine
-
mercapturic
-
halogenated
-
transamination
-
beta-elimination
- aminotransferases
- kynureninase
- l-kynurenine
- alkene
-
haloalkenes
- sevoflurane
- 3-hydroxykynurenine
-
gamma-lyase
-
plp-dependent
- acivicin
- trichloroethylene
-
gamma-synthase
- probenecid
- l-cystathionine
-
transsulfuration
-
hexachlorobutadiene
-
xanthurenic
-
nephrocarcinogenicity
-
5'-phosphate-dependent
- methylselenol
- methanethiol
-
b6-dependent
- se-methylselenocysteine
-
sulfhydrylase
- o-acetylserine
-
thioacylating
-
organ-selective
- alpha-aminoadipate
-
3-monooxygenase
-
3-hydroxyanthranilic
-
beta-replacement
- food industry
- nutrition
- agriculture
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
beta-lyase, kynurenine aminotransferase, cysteine conjugate beta-lyase, c-s lyase, cystathionine beta-lyase, glutamine transaminase k, cysteine s-conjugate beta-lyase, beta-cystathionase, kat iii, c-des, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAR
beta-cystathionase
beta-lyase
C-S lyase
CBL
CBL/ALR
CBS
cystathionine beta-lyase
cysteine conjugate beta-lyase
cysteine conjugate. beta.-lyase
-
-
-
-
cysteine lyase
-
-
-
-
cysteine S-conjugate beta-lyase
cystine lyase
EC 4.4.1.6
-
-
formerly
-
EC 4.4.1.8
-
-
formerly
-
glutamine transaminase K
glutamine transaminase K/cysteine conjugate beta-lyase
-
-
-
-
GTK
KYAT3
kynurenine aminotransferase
-
the enzyme is a multifunctional aminotransferase and also a cysteine S-conjugate beta-lyase
lyase, cystathionine beta-
-
-
-
-
lyase, cysteine conjugate.beta.
-
-
-
-
MalY
MetC
ORF5
-
-
-
-
osteotoxin
-
-
-
-
Str3p
additional information
beta-cystathionase
-
-
-
-
CBL
-
-
-
-
cysteine conjugate beta-lyase
-
-
-
-
cystine lyase
-
-
-
-
glutamine transaminase K
-
exhibits broad specificity both as an aminotransferase and as a cysteine S-conjugate beta-lyase
additional information
-
glutamine transaminase K: beta-lyase activity with S-(1,2-dichlorovinyl)-L-cysteine regulated by concurrent transamination
additional information
-
rat kidney enzyme: identical with rat kidney cytosolic glutamine transaminase K
additional information
-
rat kidney enzyme: identical with rat kidney cytosolic glutamine transaminase K
additional information
-
rat kidney enzyme: identical with rat kidney cytosolic glutamine transaminase K
additional information
-
the enzyme belongs to the large family of cysteine-S-conjugate beta-lyases
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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
stereochemistry
-
an L-cysteine-S-conjugate + H2O = a thiol + NH3 + pyruvate
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
with an amino acid containing a good leaving group in the beta position, beta-elemination is greatly favoured over transamination
-
an L-cysteine-S-conjugate + H2O = a thiol + NH3 + pyruvate
overall reaction
-
-
-
L-cystathionine + H2O = L-homocysteine + pyruvate + NH3
overall reaction
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
transamination
additional information
elimination
-
-
of H2S or RSH, C-S bond cleavage
-
elimination
-
-
of RSH, C-S bond cleavage
-
additional information
-
shows identity with a soluble kynurenine aminotransferase from rat brain
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
Cysteine and methionine metabolism, Cysteine and methionine metabolism, Cysteine and methionine metabolism, Cysteine and methionine metabolism, Cysteine and methionine metabolism, Cysteine and methionine metabolism, Cysteine and methionine metabolism, Cysteine and methionine metabolism, Cysteine and methionine metabolism, Cysteine and methionine metabolism, Cysteine and methionine metabolism, Cysteine and methionine metabolism, methionine metabolism, methionine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-cysteine-S-conjugate thiol-lyase (deaminating; pyruvate-forming)
A pyridoxal-phosphate protein. The enzyme is promiscuous regarding the moiety conjugated to L-cysteine, and can accept both aliphatic and aromatic substitutions. 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. While bacteria and plants have dedicated enzymes, all of the animal enzymes discovered thus far are bifunctional, most of which also act as aminotransferases.
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CAS REGISTRY NUMBER
COMMENTARY
68652-57-3
-
9055-05-4
-
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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 + H2O
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-hydroxyethyl)-1-methylbutyl]-L-cysteine + H2O
sulfanylhexanol + ?
-
very low activity
-
-
?
S-[1-(2-hydroxyethyl)-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
-
-
-
?
2,4-dinitrophenyl-L-cysteine + H2O
2,4-dinitrobenzenethiol + pyruvate + NH3
-
-
-
-
?
2,4-dinitrophenyl-L-cysteine + H2O
2,4-dinitrobenzenethiol + pyruvate + NH3
-
-
-
-
?
2,4-dinitrophenyl-L-cysteine + H2O
2,4-dinitrobenzenethiol + pyruvate + NH3
-
-
-
-
?
2,4-dinitrophenyl-L-cysteine + H2O
2,4-dinitrobenzenethiol + pyruvate + NH3
-
-
-
-
?
2,4-dinitrophenyl-L-cysteine + H2O
2,4-dinitrobenzenethiol + pyruvate + NH3
-
-
-
-
?
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
-
?
cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
?
cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
?
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
-
-
-
?
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
-
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-cystathionine + H2O
L-homocysteine + pyruvate + NH3
overall reaction
-
-
?
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-thiocysteine + pyruvate + NH3
-
64% of the activity with L-cystathionine
-
-
?
L-cystine + H2O
L-thiocysteine + pyruvate + NH3
-
28% of the activity with L-cystathionine
-
-
?
L-cystine + H2O
L-thiocysteine + pyruvate + NH3
-
28% of the activity with L-cystathionine
-
-
?
L-cystine + H2O
L-thiocysteine + pyruvate + NH3
-
87% of the activity with cystathionine
-
-
?
L-cystine + H2O
L-thiocysteine + pyruvate + NH3
-
87% of the activity with cystathionine
-
-
?
L-cystine + H2O
L-thiocysteine + pyruvate + NH3
-
17% of the activity with L-cystathionine
-
-
?
L-cystine + H2O
L-thiocysteine + pyruvate + NH3
-
cystine is preferred over cysteine as substrate
-
-
?
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 + NH3 + 2-oxobutanoate
-
-
-
?
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
?
-
the Pelagibacter ubique cystathionine beta-lyase (CBL) also shows a promiscuous alanine racemase (ALR) activity (cf. EC 5.1.1.1). ALR catalyzes the interconversion of L-alanine and D-alanine. The ALR activity of MBP-PuCBL is 40fold lower than its CBL activity
-
-
-
additional information
?
-
the Pelagibacter ubique cystathionine beta-lyase (CBL) also shows a promiscuous alanine racemase (ALR) activity (cf. EC 5.1.1.1). ALR catalyzes the interconversion of L-alanine and D-alanine. The ALR activity of MBP-PuCBL is 40fold lower than its CBL activity
-
-
-
additional information
?
-
-
not: D-cysteine derivatives, DL-homocysteine derivatives
-
-
?
additional information
?
-
the Escherichia coli cystathionine beta-lyase (CBL) also shows a promiscuous alanine racemase (ALR) activity (cf. EC 5.1.1.1). ALR catalyzes the interconversion of L-alanine and D-alanine
-
-
-
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
?
-
-
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
?
-
Ls-MalY is a bifunctional amino acid racemase with multiple substrate specificity, both the amino acid racemase and beta-lyase reactions of Ls-MalY are catalyzed at the same active site
-
-
?
additional information
?
-
enzyme Ls-MalY shows cystathionine beta-lyase and amino acid racemase activity (EC 5.1.1.10) with various amino acids, such as Ala, Arg, Asn, Glu, Gln, His, Leu, Lys, Met, Ser, Thr, Trp, and Val. The beta-lyase shows activity toward L-Cys, but not toward D-Cys, L-Ser, and D-Ser, substrate specificity, overview. Ls-MalY also shows beta-lyase activity with L-cystine and L-cystathionine. The epsilon-amino group of Lys233 in the primary structure of Ls-MalY likely bound to pyridoxal 5'-phosphate, and Lys233 is an essential residue for Ls-MalY to catalyze both the amino acid racemase and beta-lyase reactions. Tyr123 is a catalytic residue in the amino acid racemase reaction but strongly affects beta-lyase activity
-
-
?
additional information
?
-
-
not: D-cysteine derivatives, DL-homocysteine derivatives
-
-
?
additional information
?
-
substrate docking study. The largest attractive force that stabilizes the amino group of the ethyl chain moiety is contributed by Arg433. The negative charge of the carboxyl group in the ethyl chain is balanced by a hydrogen bond between it and amino group of Lys271. The propyl chain moiety of cystathionine is stabilized by the guanidium groups of two residues, Arg179 and Arg122'. Phosphate group of PLP forms two hydrogen bonds between hydroxy hydrogen of Ser268 and guanidium hydrogen of Arg122'
-
-
?
additional information
?
-
-
substrate docking study. The largest attractive force that stabilizes the amino group of the ethyl chain moiety is contributed by Arg433. The negative charge of the carboxyl group in the ethyl chain is balanced by a hydrogen bond between it and amino group of Lys271. The propyl chain moiety of cystathionine is stabilized by the guanidium groups of two residues, Arg179 and Arg122'. Phosphate group of PLP forms two hydrogen bonds between hydroxy hydrogen of Ser268 and guanidium hydrogen of Arg122'
-
-
?
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, 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
?
-
-
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
?
-
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
?
-
-
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
?
-
the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
-
?
additional information
?
-
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
-
-
?
additional information
?
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
-
-
additional information
?
-
no activity with O-acetylhomoserine or O-succinylhomoserine plus L-cysteine, the cystathionine gamma-synthase (metB, EC 2.5.1.48) activity of the enzyme is negligible
-
-
-
additional information
?
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
-
-
additional information
?
-
the GLR (EC 5.1.1.3) activity of wMelCBL is very weak: approximately 3fold less efficient than cystathionine beta-elimination (EC 4.4.1.13) and 28fold less efficient than alanine racemization (EC 5.1.1.1)
-
-
-
additional information
?
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
-
-
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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
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
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 + pyruvate + NH3
-
-
-
?
cystathionine + H2O
L-homocysteine + pyruvate + NH3
-
-
-
?
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
-
penultimate step in microbial and plant methionine biosynthesis
-
-
?
L-cystathionine + H2O
L-homocysteine + pyruvate + NH3
overall reaction
-
-
?
additional information
?
-
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
?
-
-
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
?
-
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
?
-
Ls-MalY is a bifunctional amino acid racemase with multiple substrate specificity, both the amino acid racemase and beta-lyase reactions of Ls-MalY are catalyzed at the same active site
-
-
?
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, 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
?
-
the enzyme plays a central role in methionine biosynthesis
-
?
additional information
?
-
-
the enzyme plays a central role in methionine biosynthesis
-
?
additional information
?
-
the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
-
?
additional information
?
-
the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
-
?
additional information
?
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
-
-
additional information
?
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
-
-
additional information
?
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
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
-
5.7 mol of pyridoxal 5'-phosphate is bound per mol of enzyme
pyridoxal 5'-phosphate
-
each subunit of the dimer contains one molecule of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
the pyridoxal 5'-phosphate binding site shows the tripeptide sequence Thr-Lys(Pxy)-Tyr in their structure
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
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-aminoethoxyvinylglycine
time-dependent slow-binding, one-step mechanism
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)
-
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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
TTHA1554
-
when an 8fold excess of TTHA1554 is added to TTHA1620, the cystathionine beta-lyase activity of TTHA1620 increases approximately 2fold
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Tryptophan metabolism in relation to amino acid alterations during typhoid fever.
Anemia, Hypochromic
Rhizobitoxine production and symbiotic compatibility of Bradyrhizobium from Asian and North American lineages of amphicarpaea.
Basal Ganglia Diseases
Immunocytochemical localization of kynurenine aminotransferase in the rat striatum: a light and electron microscopic study.
Carcinogenesis
Upregulation of the Glutaminase II Pathway Contributes to Glutamate Production upon Glutaminase 1 Inhibition in Pancreatic Cancer.
Carcinoma, Hepatocellular
A Novel mRNA-Mediated and MicroRNA-Guided Approach to Specifically Eradicate Drug-Resistant Hepatocellular Carcinoma Cell Lines by Se-Methylselenocysteine.
Cataract
Presence and distribution of l-kynurenine aminotransferases immunoreactivity in human cataractous lenses.
Central Nervous System Neoplasms
Inhibitors of the kynurenine pathway as neurotherapeutics: a patent review (2012-2015).
Diphtheria
Characterization of C-S Lyase from C. diphtheriae: A Possible Target for New Antimicrobial Drugs.
Herpes Simplex
Effect of urethral wall injection of replication-defective herpes simplex virus-mediated gene transfer of kynurenine aminotransferase on urethral pressure in spinal cord-injured rats.
Herpes Simplex
Herpes simplex virus vector-mediated gene transfer of kynurenine aminotransferase improves detrusor overactivity in spinal cord-injured rats.
Huntington Disease
An investigation of the activities of 3-hydroxykynureninase and kynurenine aminotransferase in the brain in Huntington's disease.
Huntington Disease
Characterization of kynurenine aminotransferase III, a novel member of a phylogenetically conserved KAT family.
Huntington Disease
Inhibitors of the kynurenine pathway as neurotherapeutics: a patent review (2012-2015).
Hyperoxaluria
Metabolism of Oxalate in Humans: A Potential Role Kynurenine Aminotransferase/Glutamine Transaminase/Cysteine Conjugate Beta-lyase Plays in Hyperoxaluria.
Ischemic Stroke
Serum indoleamine 2,3-dioxygenase and kynurenine aminotransferase enzyme activity in patients with ischemic stroke.
Melanoma
Presence and distribution of l-kynurenine aminotransferases immunoreactivity in human cataractous lenses.
Melanoma
Presence of L-kynurenine aminotransferase III in retinal ganglion cells and corpora amylacea in the human retina and optic nerve.
Neoplasms
High Levels of Glutaminase II Pathway Enzymes in Normal and Cancerous Prostate Suggest a Role in 'Glutamine Addiction'.
Neoplasms
Inhibitors of the kynurenine pathway as neurotherapeutics: a patent review (2012-2015).
Neoplasms
Perchloroethylene-induced rat kidney tumors: an investigation of the mechanisms involved and their relevance to humans.
Neoplasms
Upregulation of the Glutaminase II Pathway Contributes to Glutamate Production upon Glutaminase 1 Inhibition in Pancreatic Cancer.
Nervous System Diseases
Characterization of kynurenine aminotransferase III, a novel member of a phylogenetically conserved KAT family.
Neuralgia
Kynurenine, Tetrahydrobiopterin, and Cytokine Inflammatory Biomarkers in Individuals Affected by Diabetic Neuropathic Pain.
Neurodegenerative Diseases
Inhibitors of the kynurenine pathway as neurotherapeutics: a patent review (2012-2015).
Osteosarcoma
Toxicity of Bordetella avium beta-cystathionase toward MC3T3-E1 osteogenic cells.
Overweight
TSH levels, overweight, BMI, and skin expression levels of DCT and CCBL2 genes are related to vitiligo treatment response with narrow band UVB phototherapy.
Proteinuria
Nephrotoxicity of sevoflurane compound A [fluoromethyl-2,2-difluoro-1-(trifluoromethyl)vinyl ether] in rats: evidence for glutathione and cysteine conjugate formation and the role of renal cysteine conjugate beta-lyase.
Renal Insufficiency, Chronic
Long-Term Clinical Outcomes and Optimal Stent Strategy in Left Main Coronary Bifurcation Stenting.
Seizures
Differential expression of the astrocytic enzymes 3-hydroxyanthranilic acid oxygenase, kynurenine aminotransferase and glutamine synthetase in seizure-prone and non-epileptic mice.
Seizures
Electrical kindling is associated with a lasting increase in the extracellular levels of kynurenic acid in the rat hippocampus.
Seizures
Proconvulsive effects of the mitochondrial respiratory chain inhibitor--3-nitropropionic acid.
Starvation
Expression in Lactococcus lactis of functional genes related to amino acid catabolism and cheese aroma formation is influenced by branched chain amino acids.
Tuberculosis
Serum Small Extracellular Vesicles Proteome of Tuberculosis Patients Demonstrated Deregulated Immune Response.
Vitamin B 6 Deficiency
Multiple roles of haem in cystathionine ?-synthase activity: implications for hemin and other therapies of acute hepatic porphyria.
Vitiligo
TSH levels, overweight, BMI, and skin expression levels of DCT and CCBL2 genes are related to vitiligo treatment response with narrow band UVB phototherapy.
Yellow Fever
Isolation, characterization, and functional expression of kynurenine aminotransferase cDNA from the yellow fever mosquito, Aedes aegypti(1).
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
cystathionine
recombinant His-tagged enzyme, pH 8.0, 37°C, Tris buffer
0.7
cystathionine
recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer
1.3
cystathionine
recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer
2.1
cystathionine
recombinant MBP-tagged enzyme, pH 8.0, 37°C
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
1.8
L-cystathionine
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
11.5
L-cysteine
pH 10.0, 35°C, recombinant His-tagged enzyme
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
steady-state kinetics
-
additional information
additional information
-
kinetic parameters for differentially substituted cysteine-S-conjugates and selenocysteine Se-conjugates
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetics, overview
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
930
L-cysteine
pH 10.0, 35°C, recombinant His-tagged enzyme
1.27
L-djenkolate
in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37°C
1
cystathionine
recombinant MBP-tagged enzyme, pH 8.0, 37°C
2.3
cystathionine
recombinant His-tagged enzyme, pH 8.0, 37°C, Tris buffer
3.3
cystathionine
recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer
9.2
cystathionine
recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer
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
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
80.87
L-cysteine
pH 10.0, 35°C, recombinant His-tagged enzyme
0.476
cystathionine
recombinant MBP-tagged enzyme, pH 8.0, 37°C
4.71
cystathionine
recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer
5.75
cystathionine
recombinant His-tagged enzyme, pH 8.0, 37°C, Tris buffer
7.08
cystathionine
recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer
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
320
L-cystathionine
pH 8.5, 25°C, recombinant mutant W131FF/W230FF/W276F
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016
1-(4-chlorophenyl)-3-[4-(6-methyl-1,3-benzothiazol-2-yl)phenyl]urea
Escherichia coli
pH 8.5, 22°C
0.00065
2,3,5-trifluoro-N-(2-hydrazino-2-oxoethyl)-4-methoxybenzamide
Escherichia coli
pH 8.5, 22°C
0.00053
2-bromobenzyl (9Z)-9-(hydroxyimino)-2,7-dinitro-9H-fluorene-4-carboxylate
Escherichia coli
pH 8.5, 22°C
0.00028
3,3,3-trifluoro-N-(2-methylphenyl)-2-(trifluoromethyl)propanamide
Escherichia coli
pH 8.5, 22°C
0.56
3-amino-N-(2-hydrazino-2-oxoethyl)naphthalene-2-carboxamide
Escherichia coli
pH 8.5, 22°C
0.2
4-chloro-N-[4-(6-methyl-1,3-benzothiazol-2-yl)phenyl]benzamide
Escherichia coli
pH 8.5, 22°C
0.009
diphenyl 9-(dicyanomethylidene)-4,5-dinitro-9H-fluorene-2,7-disulfonate
Escherichia coli
pH 8.5, 22°C
0.000079
N-(2-hydrazino-2-oxoethyl)-2-(trifluoromethyl)benzamide
Escherichia coli
pH 8.5, 22°C
0.5
N-(2-hydrazino-2-oxoethyl)-2-naphthalen-1-ylacetamide
Escherichia coli
pH 8.5, 22°C
0.037
N-(2-hydrazino-2-oxoethyl)-3-(trifluoromethyl)benzamide
Escherichia coli
pH 8.5, 22°C
0.015
N-(2-hydrazino-2-oxoethyl)-4-(trifluoromethyl)benzamide
Escherichia coli
pH 8.5, 22°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1258
using L-cystathionine as substrate,in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37°C
additional information
additional information
-
approximately between 0.6 and 6.4 with S-(1,2-dichlorovinyl)-L-cysteine or S-(1,1,2,2-tetrafluoroethyl)-L-cysteine as substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
5.5
7.4 - 8.5
7.5 - 8
8 - 9
8.5
8.6
8.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6.8
MalY: 55% of maximal activity at pH 5.5, optimal activity at pH 6.0, reduced activity at pH 6.8, no activity at pH 9.0
5.5 - 9
MetC: 15% of maximal activity at pH 5.5, optimal activity at pH 9.0
7 - 10.5
using L-cystathionine as substrate, no significant activity is observed below pH 7.0 or above pH 10.5
8.4 - 9.9
-
pH 8.4: about 55% of maximal activity, pH 9.9: about 30% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional cystine C-S lyase and alanine aminotransferase, EC 2.6.1.2
-
-
brenda
a transducing phage lambda carrying the structural gene for beta-cystathionase
-
-
brenda
cystathionine beta- and gamma-lyase Ctl1; strain ATCC 334
UniProt
brenda
cystathionine beta- and gamma-lyase Ctl2; strain ATCC 334
UniProt
brenda
gene malY; strain ATCC 334 and several other genotypes, overview, gene malY
UniProt
brenda
strain ATCC 334 and several other genotypes, overview, gene metC
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
-
34541, 34544, 34545, 34547, 34548, 34549, 34555, 34556, 34557, 34558, 34559, 34562, 640183, 660687, 661038, 695201, 707092, 715070
brenda
additional information
-
expression in cells colonized in mice. CBL appears to be over-expressed in vivo after 2 and 6 h of infection
brenda
additional information
strain LK-145 is isolated from a Japanese sake seller as a high D-amino acid producer, and strain LT-13 is isolated from Moto, a starter of sake, as a low D-amino acid producer, using a medium of amylase digested rice as a carbon source
brenda
additional information
Latilactobacillus sakei LT-13
-
strain LK-145 is isolated from a Japanese sake seller as a high D-amino acid producer, and strain LT-13 is isolated from Moto, a starter of sake, as a low D-amino acid producer, using a medium of amylase digested rice as a carbon source
-
brenda
additional information
-
expressed in all plant tissues, with relatively low levels in the latex and pedicel
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
50% of the total activity is associated with the chloroplast
brenda
-
50% of the total activity is associated with the chloroplast
brenda
additional information
the enzyme sequence contains a signal peptide
-
brenda
additional information
-
the enzyme sequence contains a signal peptide
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL
-
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
-
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
-
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
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
metabolism
molecular relationship between cystathionine beta-lyase and mimosinase (UniProt ID U6BYK3, EC 3.5.1.61). The recombinant Mp mimosinase degrades both mimosine and cystathionine with a much higher turnover number for mimosine compared with cystathionine, and Mp CBL utilizes only cystathionine as a substrate
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
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
physiological function
enzyme catalyzes the transamination of kynurenine to kynurenic acid, and is identical to cysteine conjugate beta-lyase 2 and glutamine transaminase L. It is more efficient in transamination of glutamine with indo-3-pyruvate or oxaloacetate as aminogroup acceptor than the mouse KAT1
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
additional information
structural modeling of Ls-MalY, structure comparisons, overview
additional information
homology modeling and molecular dynamics simulations of Mp CBL. Active site structure
additional information
-
homology modeling and molecular dynamics simulations of Mp CBL. Active site structure
additional information
comparisons of structure and function of CBL and ALR, overview
additional information
Latilactobacillus sakei LT-13
-
structural modeling of Ls-MalY, structure comparisons, overview
-
Show AA Sequence and Transmembrane Helices (11201 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
170000
200000
-
enzyme from rat kidney mitochondrion, some activity is present in the high-molecular weight fraction, gel filtration
330000
37000
42700
-
4 * 46000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 42700, detagged enzyme, SDS-PAGE
43000
46000
53000
70000
80000
93000
-
enzyme from rat kidney mitochondrion, most of the activity is present in the low-molecular weight fraction, gel filtration
330000
-
high molecular weight lyase, in rat kidney mitochondria and cytosol
46000
-
4 * 46000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 42700, detagged enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homohexamer
homotetramer
tetramer
additional information
dimer
the Escherichia coli ALR dimer (PDB entry 2RJG) adopts a fold type III
homohexamer
6 * 46000, recombinant His6-tagged enzyme, SDS-PAGE
tetramer
the Escherichia coli CBL tetramer (PDB entry 1CL1) adopts a fold type I
tetramer
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4 * 46000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 42700, detagged enzyme, SDS-PAGE
additional information
structural modeling of Ls-MalY, structure comparisons, overview
additional information
Latilactobacillus sakei LT-13
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structural modeling of Ls-MalY, structure comparisons, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, with 2 M ammonium sulfate and 0.1 M Tris at pH 8.5
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cocrystallization with inhibitor N-(2-hydrazino-2-oxoethyl)-2-nitrobenzamide as well as with N-(2-hydrazino-2-oxoethyl)-2,6-dimethoxybenzamide
sitting drop vapor diffusion method. Crystal structure of the lyase and of a complex with the reaction products of cystine cleavage at 1.8 A and 1.55 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C117G
-
inactive protein, pyridoxal 5'-phosphate is not detectable in the mutant protein, enhanced susceptibility to chymotrypsin digestion
C309A
-
inactive protein, pyridoxal 5'-phosphate is not detectable in the mutant protein, enhanced susceptibility to chymotrypsin digestion
F55D
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the mutant shows 74fold reduced catalytic efficiency compared to the wild type enzyme
F55D/Y338E
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the mutant shows 58000fold reduced catalytic efficiency compared to the wild type enzyme
K42A
site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme
S32A
site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme
S33A
site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme
W131F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W188F/W230F/W276F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W188F/W230F/W276F/W300F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W188F/W230F/W276F/W340F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W188F/W230F/W300F/W340F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W188F/W276F/W300F/W340F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W230F/W276F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W230F/W276F/W300F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W230F/W276F/W300F/W340F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W230F/W276F/W340F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W188F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by 4.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W188F/W230F/W276F/W300F/W340F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W230F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W276F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W300F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W340F
Y338E
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the mutant shows 2850fold reduced catalytic efficiency compared to the wild type enzyme
K233A
site-directed mutagenesis, the mutant is only active with D-Ser, but inactive with L- or D-Cys, and L-Ser, in contrast to the wild-type enzyme
Y123A
site-directed mutagenesis, the mutant shows highly reduced activity with L-Cys compared to the wild-type enzyme, and is active with L-Ser in contrast to wild-type
K233A
Latilactobacillus sakei LT-13
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site-directed mutagenesis, the mutant is only active with D-Ser, but inactive with L- or D-Cys, and L-Ser, in contrast to the wild-type enzyme
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Y123A
Latilactobacillus sakei LT-13
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site-directed mutagenesis, the mutant shows highly reduced activity with L-Cys compared to the wild-type enzyme, and is active with L-Ser in contrast to wild-type
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additional information
construction of 12 chimeric mutants of cystathionine gamma-synthase, EC 2.5.1.48, and cystathionine beta-lyase to probe the roles of two structurally distinct, about 25-residue segments situated in proximity to the amino and carboxy termini and located at the entrance of the active-site. The exchange of the targeted regions impairs the activity of the resulting enzymes, but does not produce a corresponding interchange of reaction specificity, catalytic efficiency of the native reactions is reduced by at least 95fold, and alpha,beta versus alpha,gamma-elimination specificity is not modified. The chimeric enzymes adopt a stable folded structure
W340F
site-directed mutagenesis, 8fold ncrease in KM for L-cystathionine compared to the wild-type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8 - 9
6.8 - 9
at pH 6.8 Ctl1 still exhibits high cystathionine lyase activity, no cystathionine lyase activity is detected at pH 9.0
708517
6.8 - 9
at pH 6.8 cystathionine lyase activity of Ctl2 is strongly reduced, no cystathionine lyase activity is detected at pH 9.0
708517
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
42 - 57
60
70
additional information
Tm values of wild-type and mutant enzymes, overview
42 - 57
Ctl1 does not lose activity after incubation at 42°C for 30 min, but activity is lost at 57°C
42 - 57
Ctl2 does not lose activity after incubation at 42°C for 30 min, but activity is lost at 57°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of 15% glycerol extends the enzymatic lifetime to several days and permitted freezing of the preparation at -20°C
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pyridoxal 5'-phosphate stabilizes
rapid loss of activity during dialysis
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the buffer exchange conditions to stabilize the isolated protein and maintain its enzymatic activity include 500 mM KCl and 20 mM EDTA. By including 10% (w/v) glycerol in the buffer, less than 6% of the activity is lost in a freeze-thaw cycle, compared to the 56% loss in the presence of 10 mM imidazole
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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C or 4°C, weeks to months, slow loss of activity
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-20°C, 10 mM potassium phospate buffer, pH 7.2, with 50% glycerol, 0.01 mM pyridoxal 5'-phosphate and 0.01% 2-mercaptoethanol, 1 month without loss of activity
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-20°C, 50 mM Tris-HCl, pH 8.0, 2 years, no significant decrease in activity
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-80°C, 25 mM Tris-HCl, pH 7.8, 30 mM KCl, 1 mM DTT, 0.5 mM EDTA, 5% ethanediol, less than 5% loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Toyopearl butyl-650M resin column chromatography, and DEAE column chromatography (untagged enzyme), or Ni-NTA column chromatography (His-tagged enzyme)
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cocrystallization of wild-type enzyme and mutant enzyme K223A with cystine and cysteine
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recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
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recombinant His-tagged MalY from Escherichia coli by nickel affinity chromatography
recombinant His-tagged MetC from Escherichia coli by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain ER1821 metC::cat by nickel affinity chromatography
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis, to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of His-tagged MalY in Escherichia coli
DNA and amino acid sequence determination and analysis, expression of His-tagged MetC in Escherichia coli
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)
expressed in Saccharomyces cerevisiae strain VIN 13 and in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli. Overexpression of the enzyme complements the methionine auxotrophy of an Escherichia coli metC mutant
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expression of wild-type and chimeric mutant enzymes in Escherichia coli strain ER1821, in vivo complementation of methionine-auxotrophic Escherichia coli strains, lacking the genes encoding cystathionine gamma-synthase and cystathionine beta-lyase, with chimeric mutants
gene malY, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene met-2+, DNA and amino acid sequence determination and analysis, presence of CYS3 activator binding sites on the met-2+ promoter, quantitative enzyme expression analysis
gene metC or SH2636, phylogenetic tree and analysis, cloning from strains AX3 and CSC1435, expression of His-tagged enzyme in Escherichia coli strain BL21
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gene metC, phylogenetic analysis, the recombinant His6-tagged enzyme TmCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Recombinant production of His6-tagged enzyme in a soluble form
gene metC, phylogenetic analysis, the recombinant His6-tagged enzyme wMelCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Recombinant production of His6-tagged enzyme in a soluble form
gene metC, phylogenetic analysis, the recombinant MBP-tagged enzyme PuCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it partially. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Attempts to optimize recombinant production of the Pelagibacter ubique enzyme (PuCBL) in a soluble form are unsuccessful
gene metC, phylogenetic analysis. The recombinant enzyme EcCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it partially
mutant enzymes are expressed in the Escherichia coli KS1000 metC:cat strain
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overexpression of cysteine-S-conjugate beta-lyase gene from Escherichia coli in a commercial wine yeast strain
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recloning of the gene from a transducing phage lambda carrying the structural gene for beta-cystathionase
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recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain ER1821 metC::cat
the deduced amino acid sequence of beta-cystathionase shows extensive homology with that of cystathionine gamma-synthase
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of met-2+ in wild-type Neurspora crassa increases 3.1fold under sulfur-limiting growth conditions as compared to the transcript levels seen under high sulfur growth conditions, i.e., repressing conditions
in a activator knockout DELTAcys-3 mutant strain, the met-2+ transcript levels are substantially reduced under either low- or high-sulfur growth conditions
STR3 transcript levels in the modified strain VIN 13 are 18fold higher at day 5 but only 50% higher by the end of grape juice fermentation. In the VIN 13 control strain, the level of STR3 transcript under the control of its native promoter increase 12.3fold between day 5 and day 15 of fermentation
STR3 transcript levels in the modified strain VIN 13 are 18fold higher at day 5 but only 50% higher by the end of grape juice fermentation. In the VIN 13 control strain, the level of STR3 transcript under the control of its native promoter increase 12.3fold between day 5 and day 15 of fermentation
STR3 transcript levels in the modified strain VIN 13 are 18fold higher at day 5 but only 50% higher by the end of grape juice fermentation. In the VIN 13 control strain, the level of STR3 transcript under the control of its native promoter increase 12.3fold between day 5 and day 15 of fermentation
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
urea-induced unfolding, unfolding proceeds in at least three stages.The first transition, occurring between 0 and 1 M urea, gives rise to a partially active dimeric species that binds pyridoxal 5'-phosphate. The second equilibrium transition involving dimer dissociation, release of pyridoxal 5'-phosphate and loss of lyase activity leads to the formation of a monomeric equilibrium intermediate. It is a partially unfolded molecule that retains most of the native-state secondary structure, binds significant amounts of 8-anilino-1-naphthalenesulfonic acid (a probe for exposed hydro-phobic surfaces) and tends to self-associate. The self-associated aggregates predominate at urea concentrations of 24 M for holoMalY. The third step represents the complete unfolding of the enzyme. Both holo-and apo-MalY can be successfully refolded into the active enzyme with an 85% yield. Large misfolded soluble aggregates cannot be refolded and can be responsible for the incomplete reactivation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
the absence of the enzyme in higher organisms makes it an important target for the development of antibiotics and herbicides
food industry
medicine
nutrition
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possible essential role of the enzyme in flavor development in cheese is suggested
food industry
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transformed wine yeast strain has a 10fold higher activity of cysteine-S-conjugate beta-lyase
food industry
improvement of wine aroma during fermentation of a Vitis vinifera cultivar Sauvignon blanc juice
food industry
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improvement of wine aroma during fermentation of a Vitis vinifera cultivar Sauvignon blanc juice
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medicine
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considerable interindividual variability in enzyme catalyzed step of degradation of the anesthetic sevoflurane
medicine
the absence of the enzyme in higher organisms makes it an important target for the development of antibiotics and herbicides
medicine
-
possible beneficial or useful consequences of cysteine S-conjugate beta-lyase activity include targeting of prodrugs. They can unmask suitably designed prodrugs in target tumors/tissues. Other favorable beta-lyase reactions are associated with activation of S-cysteine conjugates derived from allium foods into reactive persulfide or sulfane sulfur progenitors. Allium-derived S-allylcysteinyl constituents are effective inhibitors of the cancer process. Thus the study of the biochemistry of allium-derived cysteine S-conjugates may lead to new avenues for cancer treatment
medicine
-
several cysteine S-conjugates that occur in extracts of garlic and other plants of the Allium family possess anti-oxidant properties and are promising anti-cancer agents
medicine
-
the enzyme is important for bacterial virulence and is therefor a potential target for antibacterial drug development
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EXTERNAL LINKS (specific for EC-Number 4.4.1.13)
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Release 2023.1 (January 2023)
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