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Enzyme Nomenclature
Information on EC 4.4.1.13 - cysteine-S-conjugate beta-lyase
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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
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAR
beta-cystathionase
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
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
MetaCyc
glucosinolate biosynthesis from dihomomethionine, glucosinolate biosynthesis from hexahomomethionine, glucosinolate biosynthesis from homomethionine, glucosinolate biosynthesis from pentahomomethionine, glucosinolate biosynthesis from phenylalanine, glucosinolate biosynthesis from tetrahomomethionine, glucosinolate biosynthesis from trihomomethionine, glucosinolate biosynthesis from tryptophan, glucosinolate biosynthesis from tyrosine, glutathione-mediated detoxification II, homocysteine and cysteine interconversion, L-methionine biosynthesis I, S-(6-hydroxy-4-methylhexan-4-yl)-L-cysteinylglycine degradation, seleno-amino acid biosynthesis (plants)
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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-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
-
-
-
?
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-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 + 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-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
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
?
-
-
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
-
-
?
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
?
-
-
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
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.
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
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
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