4.4.1.13: cysteine-S-conjugate beta-lyase
This is an abbreviated version!
For detailed information about cysteine-S-conjugate beta-lyase, go to the full flat file.
Word Map on EC 4.4.1.13
-
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
- 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
Reaction
Synonyms
AAR, beta-cystathionase, beta-lyase, C-DES, C-S lyase, CBL, CBL/ALR, CBS, CCBL2, Ctl1, Ctl2, cystathionine beta-lyase, cystathionine beta/gamma-lyase, cystathionine lyase, cysteine conjugate beta-lyase, cysteine conjugate. beta.-lyase, cysteine lyase, cysteine S-conjugate beta-lyase, cysteine-S-conjugate beta-lyase, cystine C-S lyase, cystine lyase, EC 4.4.1.6, EC 4.4.1.8, EcCBL, glutamine transaminase K, glutamine transaminase K/cysteine conjugate beta-lyase, GTK, Irc7p, KAT, KAT III, KYAT3, kynurenine aminotransferase, kynurenine-oxoglutarate transaminase 3, L-cystine C-S lyase, LACBS_00576, lyase, cystathionine beta-, lyase, cysteine conjugate.beta., MalY, MetC, More, Mp CBL, ORF5, osteotoxin, patB, PatB protein, Str3p, TmCBL, TTHA1620, wMelCBL
ECTree
4.4.1.13 cysteine-S-conjugate beta-lyaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 4.4.1.13 - cysteine-S-conjugate beta-lyase
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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
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additional information
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stereochemical ananlyses of product
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additional information
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intestinal microflora: formation of methylthio-containing metabolites
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additional information
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enzyme shows transaminase activity against L-aspartate and L-alanine
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additional information
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cisplatin is bioactivated by the enzyme, renal toxicity of cisplatin results from enzyme activity, in contrast, carboplatin is not bioactivated
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the enzyme is implicated in the degradation of not only cystathionine but also cysteine and methionine
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additional information
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the enzyme is implicated in the degradation of not only cystathionine but also cysteine and methionine
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additional information
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the enzyme performs a beta-elimination reaction, substrate specificity and product determination, overview
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additional information
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the enzyme performs a beta-elimination reaction, substrate specificity and product determination, overview
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enzyme also is able to catalyze an alpha,gamma-elimination
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additional information
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enzyme also is able to catalyze an alpha,gamma-elimination
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with methionine as substrate the enzyme produces volatile sulfur compounds which are important for flavor formation in Gouda cheese
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additional information
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with methionine as substrate the enzyme produces volatile sulfur compounds which are important for flavor formation in Gouda cheese
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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
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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
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not: D-cysteine derivatives, DL-homocysteine derivatives
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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'
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additional information
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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'
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not: D-cysteine derivatives, DL-homocysteine derivatives
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not: D-cysteine derivatives, DL-homocysteine derivatives
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the 4-nitrophenylethyl, benzyl, methyl, 2-chloroethyl, butyl thioethers of cysteine
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not: D-cysteine derivatives, DL-homocysteine derivatives
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kinetic analyses and comparison of beta-elimination reaction and transamination reaction for differentially substituted cysteine-S-conjugates and selenocysteine Se-conjugates
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no reaction with S-benzothiazolyl-L-cysteine
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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.
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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
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additional information
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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
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Irc7p is a specifically stereoselective enzyme
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Irc7p is a specifically stereoselective enzyme
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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
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additional information
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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
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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
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additional information
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the enzyme catalyzes the penultimate step in methionine biosynthesis. The enzyme is important for bacterial virulence
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the enzyme plays a central role in methionine biosynthesis
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the enzyme plays a central role in methionine biosynthesis
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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)
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the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
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the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
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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
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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
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additional information
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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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additional information
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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
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additional information
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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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additional information
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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)
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additional information
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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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