Information on EC 4.4.1.8 - cystathionine beta-lyase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
4.4.1.8
-
RECOMMENDED NAME
GeneOntology No.
cystathionine beta-lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
elimination
-
-
of RSH, C-S bond cleavage
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Cysteine and methionine metabolism
-
homocysteine and cysteine interconversion
-
Metabolic pathways
-
methionine biosynthesis I
-
methionine biosynthesis II
-
seleno-amino acid biosynthesis
-
Selenocompound metabolism
-
SYSTEMATIC NAME
IUBMB Comments
L-cystathionine L-homocysteine-lyase (deaminating; pyruvate-forming)
A pyridoxal-phosphate protein. The enzyme from some sources also acts on L-cystine, forming pyruvate, ammonia and cysteine persulfide, and a number of related compounds. Possibly identical, in yeast, with EC 4.4.1.6 S-alkylcysteine lyase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
beta-cystathionase
-
-
-
-
beta-cystathionase
-
-
CBL
-
-
-
-
CBL
Clostridium perfringens ATCC13124
-
-
-
CBL
-, A6YH85
-
CBL
B3TNN8, B3TNN9
-
CBL
A2RM21
-
CBL
Saccharomyces cerevisiae EC-1118
E3VL26
-
-
CBS
Streptomyces venezuelae ISP5230
Q9EYM7
-
-
Ctl1
B3TNN8
-
Ctl2
B3TNN9
-
cystathionine beta-lyase
-
-
cystathionine beta-lyase
-
-
cystathionine beta-lyase
-
-
cystathionine beta/gamma-lyase
B3TNN8, B3TNN9
-
cystathionine lyase
-, A6YH85
-
cysteine lyase
-
-
-
-
cystine C-S lyase
-
-
cystine lyase
-
-
-
-
cystine lyase
-
-
L-cystine C-S lyase
-
-
lyase, cystathionine beta-
-
-
-
-
MalY
A6YH85
-
ORF5
-
-
-
-
osteotoxin
-
-
-
-
PatB protein
-
-
Str3p
Saccharomyces cerevisiae EC-1118
E3VL26
-
-
additional information
-
the enzyme belongs to the large family of cysteine-S-conjugate beta-lyases
CAS REGISTRY NUMBER
COMMENTARY
9055-05-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
var. columbia
-
-
Manually annotated by BRENDA team
var. italica
-
-
Manually annotated by BRENDA team
Clostridium perfringens ATCC13124
-
-
-
Manually annotated by BRENDA team
a transducing phage lambda carrying the structural gene for beta-cystathionase; K-12
-
-
Manually annotated by BRENDA team
cystathionine beta- and gamma-lyase Ctl1; strain ATCC 334
UniProt
Manually annotated by BRENDA team
cystathionine beta- and gamma-lyase Ctl2; strain ATCC 334
UniProt
Manually annotated by BRENDA team
gene malY; strain ATCC 334 and several other genotypes, overview, gene malY
UniProt
Manually annotated by BRENDA team
strain ATCC 334 and several other genotypes, overview, gene metC
-
-
Manually annotated by BRENDA team
subsp. bulgaricus
-
-
Manually annotated by BRENDA team
strain MG1363 and strain B78
SwissProt
Manually annotated by BRENDA team
subsp. cremonis B78
-
-
Manually annotated by BRENDA team
Paracoccus denitrificans 8944
strain 8944
-
-
Manually annotated by BRENDA team
Pseudomonas sp. FM518
FM518
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae EC-1118
-
UniProt
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium me-A15
me-A15
-
-
Manually annotated by BRENDA team
L. cv. Desiree
Uniprot
Manually annotated by BRENDA team
a cytosolic and a chloroplastic isoenzyme
-
-
Manually annotated by BRENDA team
strains AX3 and JCSC1435, gene metC or SH2636
-
-
Manually annotated by BRENDA team
strain ISP5230
SwissProt
Manually annotated by BRENDA team
Streptomyces venezuelae ISP5230
strain ISP5230
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Clostridium perfringens ATCC13124
-
expression in cells colonized in mice. CBL appears to be over-expressed in vivo after 2 and 6 h of infection
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-4-(4-methylpentan-2-one)-L-cysteine + H2O
4-mercapto-4-methylpentan-2-one + NH3 + pyruvate
show the reaction diagram
E3VL26
-
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
-
?
cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
A2RM21
-
-
?
cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
1-4% of the activity with L-cysteine, depending on assay method
-
?
cystathionine + H2O
?
show the reaction diagram
-
-
-
-
-
cystathionine + H2O
?
show the reaction diagram
-
the second enzyme unique to methionine biosynthesis
-
-
-
cystathionine + H2O
?
show the reaction diagram
-
enzyme is involved in methionine biosynthesis
-
-
-
cystathionine + H2O
?
show the reaction diagram
-
enzyme is involved in methionine biosynthesis
-
-
-
cystathionine + H2O
?
show the reaction diagram
-
enzyme is involved in methionine biosynthesis
-
-
-
cystine + H2O
pyruvate + NH3 + thiocysteine
show the reaction diagram
-
-
-
-
?
D-Cys + H2O
?
show the reaction diagram
-
-
-
-
?
D-cystine + H2O
?
show the reaction diagram
-
2% of the activity with L-cystine
-
?
DL-homocysteine + H2O
hydrogen sulfide + 2-oxobutyrate + ?
show the reaction diagram
B3TNN8, B3TNN9, -
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 + ?
show the reaction diagram
B3TNN8, B3TNN9, -
Ctl2 degrades DL-homocysteine at pH 5.5, while no activity is detected at pH 6.8 or 9.0
-
-
?
homoserine + H2O
?
show the reaction diagram
-
96% of the activity with L-cystathionine
-
-
?
L-cystathionine
L-homocysteine + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
L-cystathionine
L-homocysteine + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
P06721
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
A6YH85, -
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
alpha,beta-elimination
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
no gamma-cleavage
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
E3VL26
100% activity
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
penultimate step in microbial and plant methionine biosynthesis, 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 + NH3 + pyruvate
show the reaction diagram
B3TNN8, B3TNN9, -
recombinant Ctl1 shows high activity toward the degradation of L-cystathionine
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
B3TNN8, B3TNN9, -
recombinant Ctl2 shows high activity toward the degradation of L-cystathionine
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium me-A15
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
Saccharomyces cerevisiae EC-1118
E3VL26
100% activity
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
Pseudomonas sp. FM518
-
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
Paracoccus denitrificans 8944
-
-
-
?
L-cystathionine + H2O
cysteine + ?
show the reaction diagram
-
alpha,gamma-elimination
-
?
L-cysteine
L-cysteine persulfide + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
?
show the reaction diagram
-
12% of the activity with L-cystathionine
-
-
?
L-cysteine + H2O
?
show the reaction diagram
-
7.5% of the activity with cystathionine
-
-
?
L-cysteine + H2O
?
show the reaction diagram
E3VL26
1.0% activity compared to L-cystathionine
-
-
?
L-cysteine + H2O
?
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium me-A15
-
7.5% of the activity with cystathionine
-
-
?
L-cysteine + H2O
?
show the reaction diagram
Saccharomyces cerevisiae EC-1118
E3VL26
1.0% activity compared to L-cystathionine
-
-
?
L-cysteine + H2O
pyruvate + NH3 + H2S
show the reaction diagram
A6YH85, -
-
-
-
?
L-cysteine + H2O
pyruvate + NH3 + H2S
show the reaction diagram
A6YH85, -
MalY
-
-
?
L-cysteine + H2O
hydrogen sulfide + NH3 + pyruvate
show the reaction diagram
-
very low activity
-
-
?
L-cysteine + H2O
hydrogen sulfide + pyruvate + ?
show the reaction diagram
B3TNN8, B3TNN9, -
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 + ?
show the reaction diagram
B3TNN8, B3TNN9, -
Ctl2 degrades L-cysteine at pH 5.5, while no activity is detected at pH 6.8 or 9.0
-
-
?
L-cysteine S-sulfate + H2O
?
show the reaction diagram
-
11% of the activity with L-cystine
-
?
L-cystine
L-cysteine persulfide + pyruvate + NH4+
show the reaction diagram
-
cystine is preferred over cysteine as substrate
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-, Q84UD0
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
87% of the activity with cystathionine
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
17% of the activity with L-cystathionine
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
28% of the activity with L-cystathionine
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
-
64% of the activity with L-cystathionine
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium me-A15
-
87% of the activity with cystathionine
-
-
?
L-cystine + H2O
thiocysteine + pyruvate + NH3
show the reaction diagram
Paracoccus denitrificans 8944
-
28% of the activity with L-cystathionine
-
-
?
L-cystine + H2O
?
show the reaction diagram
E3VL26
22% activity compared to L-cystathionine
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
-
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
-
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
-
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
-
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
-
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
-
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
-
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
58% of the activity with L-cystathionine
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
79% of the activity with L-cystathionine
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
-
126% of the activity with L-cystathionine
-
-
?
L-djenkolate + H2O
pyruvate
show the reaction diagram
Paracoccus denitrificans 8944
-
79% of the activity with L-cystathionine
-
-
?
L-djenkolate + H2O
pyruvate + NH3 + ?
show the reaction diagram
E3VL26
most effective substrate, 154% activity compared to L-cystathionine
-
-
?
L-djenkolic acid + H2O
?
show the reaction diagram
-
18-24% of the activity with L-cystine, depending on assay method
-
?
L-homocysteine + H2O
?
show the reaction diagram
-
4% of the activity with L-cystathionine
-
-
?
L-homocysteine + H2O
?
show the reaction diagram
Paracoccus denitrificans, Paracoccus denitrificans 8944
-
5% of the activity with L-cystathionine
-
-
?
L-homolanthionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-meso-lanthionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-methionine
methanethiol + (2S)-2-aminobutanoic acid
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
A6YH85, -
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + dimethyl disulfide + dimethyl trisulfide + 2-oxobutyrate
show the reaction diagram
B3TNN8, B3TNN9, -
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
show the reaction diagram
B3TNN8, B3TNN9, -
Ctl2 degrades L-methionine at pH 5.5, while no activity is detected at pH 6.8 or 9.0
-
-
?
L-selenocystathionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-serine + H2O
hydrogen sulfide + pyruvate + NH3
show the reaction diagram
A6YH85, -
MalY
-
-
?
lanthionine + H2O
L-cysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
lanthionine + H2O
L-cysteine + NH3 + pyruvate
show the reaction diagram
-
169% of the activity with L-cystathionine
-
-
?
lanthionine + H2O
L-cysteine + NH3 + pyruvate
show the reaction diagram
Paracoccus denitrificans, Paracoccus denitrificans 8944
-
DL-lanthionine, 136% of the activity with L-cystathionine
-
-
?
O-succinyl-L-homoserine + H2O
2-oxobutyrate + succinate + NH3
show the reaction diagram
A6YH85, -
MetC
-
-
?
S-(1-hydroxyhexan-3-yl)-L-cysteine + H2O
3-mercaptohexan-1-ol + NH3 + pyruvate
show the reaction diagram
E3VL26
-
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-(2-aminoethyl)-L-Cys + H2O
?
show the reaction diagram
-
-
-
-
?
S-ethyl-L-cysteine
?
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae EC-1118
E3VL26
9.0% activity compared to L-cystathionine
-
-
-
S-ethyl-L-cysteine + H2O
?
show the reaction diagram
-
18% of the activity with L-cystine
-
?
S-ethyl-L-cysteine sulfoxide + H2O
?
show the reaction diagram
-
71% of the activity with L-cystine
-
?
S-methyl-L-Cys + H2O
?
show the reaction diagram
-
-
-
-
?
S-methyl-L-cysteine + H2O
?
show the reaction diagram
-
13-29% of the activity with L-cystine, depending on assay method
-
?
S-methyl-L-cysteine + H2O
?
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae EC-1118
E3VL26
7.4% activity compared to L-cystathionine
-
-
?
S-methylcysteine + H2O
?
show the reaction diagram
-
-
-
-
?
S-propyl-L-cysteine + H2O
?
show the reaction diagram
-
29% of the activity with L-cystine
-
?
S-[1-(2-hydroxymethyl)-1-methylbutyl]-L-cysteine + H2O
sulfanylhexanol + ?
show the reaction diagram
-
very low activity
-
-
?
S-[1-(2-hydroxymethyl)-1-methylbutyl]-L-cysteinylglycine + H2O
sulfanylhexanol + ?
show the reaction diagram
-
very low activity
-
-
?
mixed disulfide of L-cysteine and L-homocysteine + H2O
?
show the reaction diagram
-
-
-
-
?
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
?
-
-
two types of cystathionine beta-cleavage enzyme
-
-
-
additional information
?
-
A2RM21
enzyme also is able to catalyze an alpha,gamma-elimination
-
?
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
?
-
P53780
the enzyme catalyzes the penultimate step in de novo biosynthesis of Met in microbes and plants
-
?
additional information
?
-
Q9EYM7, -
the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
-
?
additional information
?
-
-
the enzyme is responsible for off-aroma deterioration in fresh unblanched broccoli
-
?
additional information
?
-
Q9MT31, -
the enzyme plays a central role in methionine biosynthesis
-
?
additional information
?
-
A2RM21
with methionine as substrate the enzyme produces volatile sulfur compounds which are important for flavor formation in Gouda cheese
-
?
additional information
?
-
-
the enzyme catalyzes the penultimate step in methionine biosynthesis. The enzyme is important for bacterial virulence
-
-
-
additional information
?
-
P43623
Irc7p, a putative cystathionine beta-lyase, is one of the main proteins catalyzing the 4-methyl-4-sulfanylpentan-2-one and 3-sulfanylhexan-1-ol, as aromatic compounds, release from inodorous nonvolatile cysteinylated precursors under enological conditions. The two other beta-lyases Ure2p and Gln3p mainly control the bioconversion of volatile thiols by the transcriptional regulation of the IRC7 gene through the general mechanism of nitrogen catabolic repression
-
-
-
additional information
?
-
A6YH85, -
the enzyme is implicated in the degradation of not only cystathionine but also cysteine and methionine
-
-
-
additional information
?
-
P43623
Irc7p is a specifically stereoselective enzyme
-
-
-
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
?
-
A6YH85, -
the enzyme performs a beta-elimination reaction, substrate specificity and product determination, overview
-
-
-
additional information
?
-
Saccharomyces cerevisiae, Saccharomyces cerevisiae EC-1118
E3VL26
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
?
-
Streptomyces venezuelae ISP5230
Q9EYM7
the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cystathionine + H2O
?
show the reaction diagram
-
-
-
-
-
cystathionine + H2O
?
show the reaction diagram
-
the second enzyme unique to methionine biosynthesis
-
-
-
cystathionine + H2O
?
show the reaction diagram
-
enzyme is involved in methionine biosynthesis
-
-
-
cystathionine + H2O
?
show the reaction diagram
-
enzyme is involved in methionine biosynthesis
-
-
-
cystathionine + H2O
?
show the reaction diagram
-
enzyme is involved in methionine biosynthesis
-
-
-
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
A6YH85, -
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
E3VL26
100% activity
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
penultimate step in microbial and plant methionine biosynthesis
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
Saccharomyces cerevisiae EC-1118
E3VL26
100% activity
-
-
?
L-cysteine + H2O
pyruvate + NH3 + H2S
show the reaction diagram
A6YH85, -
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
A6YH85, -
-
-
-
?
additional information
?
-
P53780
the enzyme catalyzes the penultimate step in de novo biosynthesis of Met in microbes and plants
-
?
additional information
?
-
Q9EYM7, -
the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
-
?
additional information
?
-
-
the enzyme is responsible for off-aroma deterioration in fresh unblanched broccoli
-
?
additional information
?
-
Q9MT31, -
the enzyme plays a central role in methionine biosynthesis
-
?
additional information
?
-
A2RM21
with methionine as substrate the enzyme produces volatile sulfur compounds which are important for flavor formation in Gouda cheese
-
?
additional information
?
-
-
the enzyme catalyzes the penultimate step in methionine biosynthesis. The enzyme is important for bacterial virulence
-
-
-
additional information
?
-
P43623
Irc7p, a putative cystathionine beta-lyase, is one of the main proteins catalyzing the 4-methyl-4-sulfanylpentan-2-one and 3-sulfanylhexan-1-ol, as aromatic compounds, release from inodorous nonvolatile cysteinylated precursors under enological conditions. The two other beta-lyases Ure2p and Gln3p mainly control the bioconversion of volatile thiols by the transcriptional regulation of the IRC7 gene through the general mechanism of nitrogen catabolic repression
-
-
-
additional information
?
-
A6YH85, -
the enzyme is implicated in the degradation of not only cystathionine but also cysteine and methionine
-
-
-
additional information
?
-
Streptomyces venezuelae ISP5230
Q9EYM7
the enzyme is involved in generation of sulfur-containing amino acids in streptomycete
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
5.7 mol of pyridoxal 5'-phosphate is bound per mol of enzyme; Km: 0.005 mM
pyridoxal 5'-phosphate
-
required as cofactor
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
required as cofactor
pyridoxal 5'-phosphate
-
required as cofactor
pyridoxal 5'-phosphate
-
the pyridoxal 5'-phosphate binding site shows the tripeptide sequence Thr-Lys(Pxy)-Tyr in their structure
pyridoxal 5'-phosphate
-
each subunit of the tetramer is associated with one molecule of pyridoxal 5'-phosphate. Schiff-base formation between the cofactor and the holoenzyme occurs at Lys278
pyridoxal 5'-phosphate
-
each subunit of the dimer contains one molecule of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
required as cofactor
pyridoxal 5'-phosphate
-
required as cofactor
pyridoxal 5'-phosphate
-
contains 2 mol per mol of enzyme
pyridoxal 5'-phosphate
-
enzyme is dependent on
pyridoxal 5'-phosphate
P53780
dependent on
pyridoxal 5'-phosphate
-
the coenzyme strongly increases the protein stability. It is essential for the step involving dissociation of dimer into monomers and is not required for refolding of single monomers, but it is necessary to attain the native dimeric structure critical for the biological activities of MalY
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
bound by Lys-223 in the active site
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
B3TNN8, B3TNN9, -
;
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
E3VL26
dependent on
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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,-trifluoroalanine
-
irreversible
3,3,3,-trifluoroalanine
-
-
3,3,3-trifluoro-N-(2-methylphenyl)-2-(trifluoromethyl)propanamide
-
reversible inhibition
3,4-dichlorobenzenesulfonohydrazide
-
known to interact with the cofactor of PLP enzymes
3,5-diamino-N-(2-hydrazino-2-oxoethyl)benzamide
-
-
3-amino-N-(2-hydrazino-2-oxoethyl)naphthalene-2-carboxamide
-
only poor inhibitor
3-methyl-2-benzothiazolinone hydrazoone
-
-
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
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
irreversible
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
aminoethoxyvinylglycine
-
irreversible
aminoethoxyvinylglycine
-
-
aminoethoxyvinylglycine
-
-
ammonium sulfate
-
66% inhibition at 4 mM
aromatic disulfide
-
-
-
Beta-cyanoalanine
-
competitive; strong
Beta-cyanoalanine
-
competitive; strong
Beta-cyanoalanine
-
-
Beta-cyanoalanine
-
-
carboxymethoxylamine
-
irreversible
Cys
-
competitive with L-cystathionine
Cys
-
competitive with L-cystathionine
diphenyl 9-(dicyanomethylidene)-4,5-dinitro-9H-fluorene-2,7-disulfonate
-
reversible inhibition
DL-cycloserine
-
irreversible
DL-homocysteine
-
12.5 mM, 70% inhibition, competitive inhibitor
DL-Penicillamine
-
-
DL-propargylglycine
-
irreversible
DL-propargylglycine
-
no inhibition
DTT
-
10 mM, 19% inhibition
glutathione
-
strong
glycine
-
73% inhibition at 4 mM
homocysteine
-
strong
hydroxylamine
-
-
hydroxylamine
-
1 mM, 92% inhibition
hydroxylamine
-
12.5 mM, 97% inhibition
iodoacetamide
-
-
iodoacetamide
-
10 mM, 61% inhibition
iodoacetate
-
-
iodoacetate
-
10 mM, 25% inhibition
KCN
-
1 mM, 84% inhibition
L-alpha-(2-aminoethoxyvinyl)glycine
-
-
L-alpha-(2-aminoethoxyvinyl)glycine
-
-
L-aminoethoxyvinylglycine
-
time-dependent slow-binding, one-step mechanism
L-canaline
-
1 mM, 67% inhibition, 10 mM complete inhibition
L-cystathionine
-
substrate inhibition at concentrations above 6 mM
L-cysteine
-
12 mM, 65% inhibition after 5 min, 1 mM, 29% inhibition after 10 min, linear noncompetitive inhibitor
L-Met
-
competitive
L-methionine
-
40% inhibition at 6 mM
N-(2-hydrazino-2-oxoethyl)-2,6-dimethoxybenzamide
-
-
N-(2-hydrazino-2-oxoethyl)-2-(trifluoromethyl)benzamide
-
-
N-(2-hydrazino-2-oxoethyl)-2-naphthalen-1-ylacetamide
-
-
N-(2-hydrazino-2-oxoethyl)-2-nitrobenzamide
-
known to interact with the cofactor of PLP enzymes
N-(2-hydrazino-2-oxoethyl)-3,5-dinitrobenzamide
-
-
N-(2-hydrazino-2-oxoethyl)-3-(trifluoromethyl)benzamide
-
-
N-(2-hydrazino-2-oxoethyl)-4-(trifluoromethyl)benzamide
-
-
N-(2-hydrazino-2-oxoethyl)-4-nitrobenzamide
-
-
N-hydrazinocarbonylmethyl-2-nitrobenzamide
-
-
N-hydrazinocarbonylmethyl-2-trifluoromethylbenzamide
-
-
N-[4-(hydrazinosulfonyl)benzyl]acetamide
-
known to interact with the cofactor of PLP enzymes
NaCl
A6YH85, -
complete inhibition of MetC at 4%
NaCl
B3TNN8, B3TNN9, -
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
NEM
-
irreversible
NEM
-
1 mM, 94% inhibition
NEM
-
1.25 mM, about 45% inhibition
O-acetylserine
-
strong
p-hydroxymercuribenzoate
-
1 mM, 92% inhibition
phenylhydrazine
-
-
pyridoxal
-
12.5 mM, in presence of 12 mM L-cystine 12% inhibition, in presence of 1 mM L-cystine 37% inhibition
pyruvate
-
12.5 mM, 25% inhibition
rhizobitoxine
-
active-site directed, irreversible
rhizobitoxine
-
in vivo inactivation
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
rhizobitoxine
-
-
S-adenosylmethionine
-
weak
Semicarbazide
-
-
Sodium cyanide
-
12.5 mM, 95% inhibition
L-serine
-
86% inhibition at 4 mM
additional information
-
the enzyme is not inhibited by pyridamine antimicrobial agents (pyrimethanil, cyprodinil or mepanipyrim)
-
additional information
A6YH85, -
no inhibition of MalY by NaCl
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NaCl
B3TNN8, B3TNN9, -
NaCl considerably enhances the reaction rate at pH 6.8; NaCl considerably enhances the reaction rate at pH 6.8
pyridoxal
-
is 23% as effective as pyridoxal 5'-phosphate
TTHA1554
-
when an 8fold excess of TTHA1554 is added to TTHA1620, the cystathionine beta-lyase activity of TTHA1620 increases approximately 2fold
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.38
-
cystathionine
-
-
1.62
-
cystathionine
-
pH 9.0, 30C
4.2
-
cystathionine
-
-
1
-
cystine
-
estimated from steady-state measurements
5.3
-
D-Cys
-
-
1
-
DL-homocysteine
B3TNN8, B3TNN9, -
Ctl2, at pH 5.5 and 37C
1.4
-
DL-homocysteine
B3TNN8, B3TNN9, -
Ctl1, at pH 5.5 and 37C
0.04
-
L-cystathionine
-
-
0.07
-
L-cystathionine
-
-
0.096
-
L-cystathionine
E3VL26
in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37C
0.13
-
L-cystathionine
-
-
0.15
-
L-cystathionine
-
chloroplastic isoenzyme
0.18
-
L-cystathionine
-
wild type enzyme, at 25C
0.3
-
L-cystathionine
-
-
0.33
-
L-cystathionine
B3TNN8, B3TNN9, -
Ctl2, in sodium phosphate buffer, at pH 5.5 and 37C
0.35
-
L-cystathionine
B3TNN8, B3TNN9, -
Ctl1, in sodium phosphate buffer, at pH 5.5 and 37C
0.37
-
L-cystathionine
B3TNN8, B3TNN9, -
Ctl1, in sodium phosphate buffer, at pH 6.8 and 37C
0.41
-
L-cystathionine
B3TNN8, B3TNN9, -
Ctl2, in sodium phosphate buffer, at pH 6.8 and 37C
0.48
-
L-cystathionine
-
-
0.55
-
L-cystathionine
-
mutant enzyme D116N, at 25C
0.67
-
L-cystathionine
-
mutant enzyme D116A, at 25C
1.02
-
L-cystathionine
-
mutant enzyme R59A, at 25C
1.2
-
L-cystathionine
-
pH 8.0, 37C, purified recombinant enzyme
1.3
-
L-cystathionine
-
pH 8.5, 37C, purified recombinant enzyme
1.35
-
L-cystathionine
-
mutant enzyme W340F, at 25C
1.51
-
L-cystathionine
-
mutant enzyme R59K, at 25C
5.1
-
L-cystathionine
-
mutant enzyme R58A, at 25C
15
-
L-cystathionine
-
mutant enzyme R372K, at 25C
0.29
-
L-cysteine
-
in presence of 10 mM dithiothreitol
0.3
-
L-cysteine
B3TNN8, B3TNN9, -
Ctl2, at pH 5.5 and 37C
1
-
L-cysteine
B3TNN8, B3TNN9, -
Ctl1, at pH 5.5 and 37C
0.0812
-
L-cystine
-
-
0.25
-
L-cystine
-
-
2.32
-
L-cystine
-
-
5.4
-
L-cystine
-
-
0.033
-
L-djenkolate
-
-
0.178
-
L-djenkolate
E3VL26
in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37C
0.2
-
L-djenkolate
-
-
0.25
-
L-djenkolate
-
-
0.34
-
L-djenkolate
-
chloroplastic isoenzyme
0.35
-
L-djenkolate
-
-
0.36
-
L-djenkolate
-
-
4.5
-
L-homolanthionine
-
-
0.83
-
L-meso-lanthionine
-
-
32.8
-
L-methionine
B3TNN8, B3TNN9, -
Ctl1, at pH 5.5 and 37C
34.2
-
L-methionine
B3TNN8, B3TNN9, -
Ctl2, at pH 5.5 and 37C
0.35
-
L-selenocystathionine
-
-
0.47
-
S-(2-aminoethyl)-L-Cys
-
-
0.67
-
S-Methyl-L-Cys
-
-
0.104
-
Lanthionine
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetics, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.5
-
cystathionine
-
-
0.91
-
L-cystathionine
E3VL26
in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37C
8.1
-
L-cystathionine
-
mutant enzyme R372K, at 25C
9.7
-
L-cystathionine
-
mutant enzyme R58A, at 25C
34.1
-
L-cystathionine
-
wild type enzyme, at 25C
36.7
-
L-cystathionine
-
mutant enzyme R59K, at 25C
37.9
-
L-cystathionine
-
mutant enzyme D116N, at 25C
41.9
-
L-cystathionine
-
mutant enzyme D116A, at 25C
45.8
-
L-cystathionine
-
mutant enzyme R59A, at 25C
79
-
L-cystathionine
-
mutant enzyme W340F, at 25C
1.27
-
L-djenkolate
E3VL26
in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00009
-
L-cystathionine
-
mutant enzyme R372A, at 25C
12148
0.00023
-
L-cystathionine
-
mutant enzyme R372L, at 25C
12148
0.385
-
L-cystathionine
-
mutant enzyme R58K, at 25C
12148
0.55
-
L-cystathionine
-
mutant enzyme R372K, at 25C
12148
1.92
-
L-cystathionine
-
mutant enzyme R58A, at 25C
12148
24
-
L-cystathionine
-
mutant enzyme R59K, at 25C
12148
45
-
L-cystathionine
-
mutant enzyme R59A, at 25C
12148
59
-
L-cystathionine
-
mutant enzyme W340F, at 25C
12148
62
-
L-cystathionine
-
mutant enzyme D116A, at 25C
12148
69
-
L-cystathionine
-
mutant enzyme D116N, at 25C
12148
190
-
L-cystathionine
-
wild type enzyme, at 25C
12148
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0019
-
aminoethoxyvinylglycine
-
wild type enzyme, at 25C
0.0027
-
aminoethoxyvinylglycine
-
mutant enzyme D116N, at 25C; mutant enzyme R59A, at 25C
0.0039
-
aminoethoxyvinylglycine
-
mutant enzyme D116A, at 25C
0.006
-
aminoethoxyvinylglycine
-
mutant enzyme R58A, at 25C
0.012
-
aminoethoxyvinylglycine
-
mutant enzyme R59K, at 25C
0.04
-
aminoethoxyvinylglycine
-
mutant enzyme W340F, at 25C
0.055
-
aminoethoxyvinylglycine
-
mutant enzyme R58K, at 25C
9.1
-
aminoethoxyvinylglycine
-
mutant enzyme R372K, at 25C
1.5
-
DL-homocysteine
-
-
5
-
L-cysteine
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.016
-
1-(4-chlorophenyl)-3-[4-(6-methyl-1,3-benzothiazol-2-yl)phenyl]urea
-
pH 8.5, 22C
0.00065
-
2,3,5-trifluoro-N-(2-hydrazino-2-oxoethyl)-4-methoxybenzamide
-
pH 8.5, 22C
0.00053
-
2-bromobenzyl (9Z)-9-(hydroxyimino)-2,7-dinitro-9H-fluorene-4-carboxylate
-
pH 8.5, 22C
0.00028
-
3,3,3-trifluoro-N-(2-methylphenyl)-2-(trifluoromethyl)propanamide
-
pH 8.5, 22C
0.0022
-
3,4-dichlorobenzenesulfonohydrazide
-
pH 8.5, 22C
0.082
-
3,5-diamino-N-(2-hydrazino-2-oxoethyl)benzamide
-
pH 8.5, 22C
0.56
-
3-amino-N-(2-hydrazino-2-oxoethyl)naphthalene-2-carboxamide
-
pH 8.5, 22C
0.2
-
4-chloro-N-[4-(6-methyl-1,3-benzothiazol-2-yl)phenyl]benzamide
-
pH 8.5, 22C
0.0018
-
4-methylbenzenesulfonohydrazide
-
pH 8.5, 22C
0.006
-
5-aminonaphthalene-1-sulfonohydrazide
-
pH 8.5, 22C
0.0034
-
5-pyridin-2-ylthiophene-2-sulfonohydrazide
-
pH 8.5, 22C
0.00134
-
aminoethoxyvinylglycine
-
mutant enzyme R59A, at 25C
0.0017
-
aminoethoxyvinylglycine
-
wild type enzyme, at 25C
0.00174
-
aminoethoxyvinylglycine
-
mutant enzyme R58A, at 25C
0.0026
-
aminoethoxyvinylglycine
-
mutant enzyme D116A, at 25C
0.0033
-
aminoethoxyvinylglycine
-
mutant enzyme D116N, at 25C
0.0046
-
aminoethoxyvinylglycine
-
mutant enzyme R59K, at 25C
0.023
-
aminoethoxyvinylglycine
-
mutant enzyme R58K, at 25C
0.043
-
aminoethoxyvinylglycine
-
mutant enzyme W340F, at 25C
3.5
-
aminoethoxyvinylglycine
-
mutant enzyme R372K, at 25C
0.009
-
diphenyl 9-(dicyanomethylidene)-4,5-dinitro-9H-fluorene-2,7-disulfonate
-
pH 8.5, 22C
0.06
-
N-(2-hydrazino-2-oxoethyl)-2,6-dimethoxybenzamide
-
pH 8.5, 22C
0.000079
-
N-(2-hydrazino-2-oxoethyl)-2-(trifluoromethyl)benzamide
-
pH 8.5, 22C
0.5
-
N-(2-hydrazino-2-oxoethyl)-2-naphthalen-1-ylacetamide
-
pH 8.5, 22C
0.0045
-
N-(2-hydrazino-2-oxoethyl)-2-nitrobenzamide
-
pH 8.5, 22C
0.0059
-
N-(2-hydrazino-2-oxoethyl)-3,5-dinitrobenzamide
-
pH 8.5, 22C
0.037
-
N-(2-hydrazino-2-oxoethyl)-3-(trifluoromethyl)benzamide
-
pH 8.5, 22C
0.015
-
N-(2-hydrazino-2-oxoethyl)-4-(trifluoromethyl)benzamide
-
pH 8.5, 22C
0.025
-
N-(2-hydrazino-2-oxoethyl)-4-nitrobenzamide
-
pH 8.5, 22C
0.034
-
N-[4-(hydrazinosulfonyl)benzyl]acetamide
-
pH 8.5, 22C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0091
-
-
-
1.226
-
-
-
1258
-
E3VL26
using L-cystathionine as substrate,in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37C
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
reaction with methionine
5.5
-
B3TNN8, B3TNN9, -
;
6
-
A6YH85, -
MalY
7.5
8.5
-
rapid decrease of activity above pH 8.5
8.3
9
-
with L-cystathionine or L-djenkolate as substrate
8.5
-
-
reaction with L-cystathionine
8.6
8.7
-
-
8.6
-
-
Tris-HCl buffer
8.8
-
-
potassium borate buffer
8.8
-
E3VL26
using L-cystathionine as substrate
9
-
A6YH85, -
MetC
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
6.8
A6YH85, -
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
A6YH85, -
MetC: 15% of maximal activity at pH 5.5, optimal activity at pH 9.0
7
10.5
E3VL26
using L-cystathionine as substrate, no significant activity is observed below pH 7.0 or above pH 10.5
7.2
9
-
pH 7.2: 36% of maximal activity, pH 8.0-9.0: optimum
7.5
9
-
pH 7.5: about 20% of maximal activity, pH 7.5-9.0: optimum
8.4
9.9
-
pH 8.4: about 55% of maximal activity, pH 9.9: about 30% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
A6YH85, -
assay at; assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
90
-
60C: optimum, 90C: 17% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.3
-
-, Q84UD0
calculation from nucleotide sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Streptomyces venezuelae ISP5230
-
-
-
Manually annotated by BRENDA team
additional information
-
expression in cells colonized in mice. CBL appears to be over-expressed in vivo after 2 and 6 h of infection
Manually annotated by BRENDA team
additional information
Clostridium perfringens ATCC13124
-
expression in cells colonized in mice. CBL appears to be over-expressed in vivo after 2 and 6 h of infection
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
50% of the total activity is associated with the chloroplast
Manually annotated by BRENDA team
-
from mesophyll and bundle sheet
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Listeria monocytogenes serotype 4b (strain F2365)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80000
-
-
gel filtration
80000
-
-
gel filtration
100000
-
-
gel filtration
130000
-
-
non-denaturing PAGE
165000
-
-
gel filtration
170000
-
-
chloroplastic isoenzyme, gel filtration
170000
-
-
gel filtration
170000
-
-
recombinant enzyme, gel filtration
195000
-
E3VL26
gel filtration
210000
-
-
gel filtration
280000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q84UD0
x * 47200, calculation from nucleotide sequence
?
A6YH85, -
x * 43000, recombinant His-tagged MetC, SDS-PAGE; x * 47000, recombinant His-tagged MalY, SDS-PAGE
dimer
-
2 * 41000, SDS-PAGE; 2 * 42606, calculation from nucleotide sequence
dimer
-
2 * 48000, SDS-PAGE
hexamer
-
-
homotetramer
E3VL26
4 * 52000, SDS-PAGE; 4 * 53000, estimated from amino acid sequence
homotetramer
Saccharomyces cerevisiae EC-1118
-
4 * 52000, SDS-PAGE; 4 * 53000, estimated from amino acid sequence
-
tetramer
-
4 * 35000-40000, SDS-PAGE
tetramer
-
4 * 44000, chloroplastic isoenzyme, SDS-PAGE
tetramer
-
4 * 46000, SDS-PAGE
tetramer
-
4 * 43000, SDS-PAGE
tetramer
-
4 * 53000, SDS-PAGE
tetramer
-
four equivalent active sites exist within the tetramer
tetramer
-
4 * 46000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 42700, detagged enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
carbohydrate content of 3%
no modification
-
enzyme is not a glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
9
B3TNN8, B3TNN9, -
at pH 6.8 Ctl1 still exhibits high cystathionine lyase activity, no cystathionine lyase activity is detected at pH 9.0; at pH 6.8 cystathionine lyase activity of Ctl2 is strongly reduced, no cystathionine lyase activity is detected at pH 9.0
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
20 h, stable
20
-
-
20 h, stable
20
-
-
room temperature, t1/2: 24 min
25
40
-
stable, rapid decline in activity above 40C
42
57
B3TNN8, B3TNN9, -
Ctl1 does not lose activity after incubation at 42C for 30 min, but activity is lost at 57C; Ctl2 does not lose activity after incubation at 42C for 30 min, but activity is lost at 57C
45
-
-
10 min, completely stable up to
50
-
-
10 min, 20% loss of activity
56
-
A6YH85, -
30 min, inactivation; 30 min, inactivation
60
-
-
10 min, stable up to
60
-
-
15 min, 90% loss of activity
60
-
-
10 min, 75% loss of actrivity
70
-
-
10 min, complete inactivation above
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
no decrease in activity after repeated freezing, -20C, and thawing
-
not stable to lyophilization
-
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
-
repeated freezing, -20C, and thawing has no effect
-
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
E3VL26
rapid loss of activity during dialysis
-
inactivated by repeated freezing and thawing
-
addition of 15% glycerol extends the enzymatic lifetime to several days and permitted freezing of the preparation at -20C
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, stable for several months
-
-20C, stable for 6 months
-
-80C, 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
-
-20C or 4C, 50% glycerol, 4 months, stable
-
-20C, stable for months
-
-15C or 4C, weeks to months, slow loss of activity
-
-10C, stable for 1 month
-
-80C or at 4C, 5 days, 70% loss of activity, partially purified enzyme
-
-80C, 10 mM MOPS buffer, pH 6.5
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation, Toyopearl butyl-650M resin column chromatography, and DEAE column chromatography (untagged enzyme), or Ni-NTA column chromatography (His-tagged enzyme)
-
Ni2+ affinity column chromatography; Ni2+ affinity column chromatography
B3TNN8, B3TNN9, -
recombinant His-tagged MalY from Escherichia coli by nickel affinity chromatography; recombinant His-tagged MetC from Escherichia coli by nickel affinity chromatography
A6YH85, -
Ni-Sepharose column chromatography
E3VL26
chloroplastic isoenzyme
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
-
cocrystallization of wild-type enzyme and mutant enzyme K223A with cystine and cysteine
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
overexpression in Escherichia coli
-
overexpression in Escherichia coli CAG18475
-
expression in Escherichia coli
-
expression in Escherichia coli
-, Q84UD0
construction of an overproducing strain of Escherichia coli
-
mutant enzymes are expressed in Escherichia coli KS1000 cells
-
mutant enzymes are expressed in the Escherichia coli KS1000 metC:cat strain
-
recloning of the gene from a transducing phage lambda carrying the structural gene for beta-cystathionase
-
the deduced amino acid sequence of beta-cystathionase shows extensive homology with that of cystathionine gamma-synthase
-
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
A6YH85, -
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
B3TNN8, B3TNN9, -
expression in Escherichia coli. Overexpression of the enzyme complements the methionine auxotrophy of an Escherichia coli metC mutant
-
expression in Escherichia coli
-
from strain MG1363 and from strain B78
A2RM21
expressed in Saccharomyces cerevisiae strain VIN 13 and in Escherichia coli BL21(DE3) cells
E3VL26
expression in Escherichia coli
Q9MT31
gene metC or SH2636, phylogenetic tree and analysis, cloning from strains AX3 and CSC1435, expression of His-tagged enzyme in Escherichia coli strain BL21
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
E3VL26
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
Saccharomyces cerevisiae EC-1118
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C117G
-
inactive protein, pyridoxal 5'-phosphate is not detectable in the mutant protein, enhanced susceptibility to chymotrypsin digestion
C279
-
activity is comparable with that of the native enzyme
C309A
-
inactive protein, pyridoxal 5'-phosphate is not detectable in the mutant protein, enhanced susceptibility to chymotrypsin digestion
C88A
-
activity is comparable with that of the native enzyme
D116A
-
mutant with reduced catalytic efficiency
D116N
-
mutant with reduced catalytic efficiency
F55D
-
the mutant shows 74fold reduced catalytic efficiency compared to the wild type enzyme
F55D/Y338E
-
the mutant shows 58000fold reduced catalytic efficiency compared to the wild type enzyme
R372A
-
mutant with reduced catalytic efficiency
R372K
-
mutant with reduced catalytic efficiency
R372L
-
mutant with reduced catalytic efficiency
R58A
-
mutant with reduced catalytic efficiency
R58K
-
mutant with reduced catalytic efficiency
R59A
-
mutant with reduced catalytic efficiency
R59K
-
mutant with reduced catalytic efficiency
W340F
-
mutant with reduced catalytic efficiency
Y338E
-
the mutant shows 2850fold reduced catalytic efficiency compared to the wild type enzyme
K223A
-
inactive mutant enzyme
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
P53780
the absence of the enzyme in higher organisms makes it an important target for the development of antibiotics and herbicides
medicine
P53780
the absence of the enzyme in higher organisms makes it an important target for the development of antibiotics and herbicides
nutrition
-
possible essential role of the enzyme in flavor development in cheese is suggested
food industry
E3VL26
improvement of wine aroma during fermentation of a Vitis vinifera cultivar Sauvignon blanc juice
food industry
Saccharomyces cerevisiae EC-1118
-
improvement of wine aroma during fermentation of a Vitis vinifera cultivar Sauvignon blanc juice
-
medicine
-
the enzyme is important for bacterial virulence and is therefor a potential target for antibacterial drug development