Information on EC 2.5.1.48 - cystathionine gamma-synthase

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

EC NUMBER
COMMENTARY
2.5.1.48
-
RECOMMENDED NAME
GeneOntology No.
cystathionine gamma-synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
O4-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate
show the reaction diagram
-
-
-
-
O4-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate
show the reaction diagram
can also use hydrogen sulfide and methanethiol as substrates producing homocysteine and methionine respectively. In the absence of thiol, the enzyme can also catalyse beta,gamma-elimination to form 2-oxobutanoate, succinate and ammonia
-
O4-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate
show the reaction diagram
ping-pong mechanism
-
O4-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate
show the reaction diagram
ping-pong mechanism
-
O4-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate
show the reaction diagram
enzyme performs an elimination or a replacement reaction, reaction mechanism, formation of an aldimine intermediate, overview
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
elimination
-
-
-
-
gamma-replacement
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Cysteine and methionine metabolism
-
Metabolic pathways
-
methionine biosynthesis I
-
Selenocompound metabolism
-
Sulfur metabolism
-
SYSTEMATIC NAME
IUBMB Comments
O4-succinyl-L-homoserine:L-cysteine S-(3-amino-3-carboxypropyl)transferase
A pyridoxal-phosphate protein. Also reacts with hydrogen sulfide and methanethiol as replacing agents, producing homocysteine and methionine, respectively. In the absence of thiol, can also catalyse beta,gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CGS
-
-
-
-
CS,26
-
-
-
-
cystathionine synthase
-
-
-
-
cystathionine synthetase
-
-
-
-
cystathionine-gamma-synthase
-
-
-
-
EC 4.2.99.9
-
-
formerly
-
homoserine O-transsuccinylase
-
-
-
-
homoserine transsuccinylase
-
-
-
-
homoserine transsuccinylase
-
-
MetB
A0PKT3
gene name
MetB
A0PKT3
gene name
-
O-succinyl-L-homoserine succinate-lyase (adding cysteine)
-
-
-
-
O-succinylhomoserine (Thiol)-lyase
-
-
-
-
O-succinylhomoserine synthase
-
-
-
-
O-succinylhomoserine synthetase
-
-
-
-
synthase, cystathionine gamma-
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9030-70-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
enzyme type I, preference for O-succinyl-L-homoserine + L-cysteine as substrates
-
-
Manually annotated by BRENDA team
enzyme type II, preference for O-acetyl-L-homoserine + L-cysteine as substrates
-
-
Manually annotated by BRENDA team
two enzymes: enzyme type I, preference for O-succinyl-L-homoserine + L-cysteine as substrates and enzyme type II, preference for O-acetyl-L-homoserine + L-cysteine as substrates
-
-
Manually annotated by BRENDA team
enzyme type II, preference for O-acetyl-L-homoserine + L-cysteine as substrates
-
-
Manually annotated by BRENDA team
enzyme type II, preference for O-acetyl-L-homoserine + L-cysteine as substrates
-
-
Manually annotated by BRENDA team
enzyme type I, preference for O-succinyl-L-homoserine + L-cysteine as substrates
-
-
Manually annotated by BRENDA team
strain SS
UniProt
Manually annotated by BRENDA team
Helicobacter pylori SS
strain SS
UniProt
Manually annotated by BRENDA team
enzyme type II, preference for O-acetyl-L-homoserine + L-cysteine as substrates
-
-
Manually annotated by BRENDA team
Neptunia amplexicaulis
-
-
-
Manually annotated by BRENDA team
enzyme type I, preference for O-succinyl-L-homoserine + L-cysteine as substrates
-
-
Manually annotated by BRENDA team
Pseudomonas dacunhae
enzyme type I, preference for O-succinyl-L-homoserine + L-cysteine as substrates
-
-
Manually annotated by BRENDA team
enzyme type I, preference for O-succinyl-L-homoserine + L-cysteine as substrates
-
-
Manually annotated by BRENDA team
enzyme type I, preference for O-succinyl-L-homoserine + L-cysteine as substrates
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-cystathionine + acetate
O-acetyl-L-homoserine + L-cysteine
show the reaction diagram
-
-
-
-
r
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-cystathionine + H2O
L-homocysteine + NH3 + pyruvate
show the reaction diagram
-
beta-elimination
-
?
L-cystathionine + H2O
L-cysteine + NH3 + 2-oxobutyrate
show the reaction diagram
-
beta-elimination
-
?
O-acetyl-L-homoserine + 2-mercaptoethanol
S-hydroxyethyl-L-homocysteine + acetate
show the reaction diagram
-
150% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + 2-mercaptopropionate
S-methylcarboxymethyl-L-homoserine + acetate
show the reaction diagram
-
50% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + 3-mercaptopropionate
S-carboxyethyl-L-homocysteine + acetate
show the reaction diagram
-
65% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + allyl mercaptan
S-allyl-L-homocysteine + acetate
show the reaction diagram
-
4% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + benzyl mercaptan
S-benzyl-L-homocysteine + acetate
show the reaction diagram
-
41% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + CH3SH
L-methionine + acetate
show the reaction diagram
-
11% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + D-Cys
D-allocystathionine + acetate
show the reaction diagram
-
101% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + D-homocysteine
meso-homolanthionine + acetate
show the reaction diagram
-
125% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + ethyl mercaptan
L-thionine + acetate
show the reaction diagram
-
24% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + isobutyl mercaptan
S-isobutyl-L-homocysteine + acetate
show the reaction diagram
-
13% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + isopropyl mercaptan
S-isopropyl-L-homocysteine + acetate
show the reaction diagram
-
1% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + L-Cys ethyl ester
S-(L-2-amino-2-ethoxycarbonyl)-L-homocysteine + acetate
show the reaction diagram
-
15% relative activity to O-acetyl-L-homoserine + L-cysteine
i.e. L-cystathionine monoethyl ester + acetate
?
O-acetyl-L-homoserine + L-Cys methyl ester
S-(L-2-amino-2-methoxycarbonyl)-L-homocysteine + acetate
show the reaction diagram
-
20% relative activity to O-acetyl-L-homoserine + L-cysteine
i.e. L-cystathionine monomethyl ester + acetate
?
O-acetyl-L-homoserine + L-Cys methyl ester
S-(L-2-amino-2-methoxycarbonyl)-L-homocysteine + acetate
show the reaction diagram
-
26% of the activity with L-Cys
-
-
?
O-acetyl-L-homoserine + L-cysteine
L-cystathionine + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-homoserine + L-cysteine
L-cystathionine + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-homoserine + L-cysteine
L-cystathionine + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-homoserine + L-cysteine
L-cystathionine + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-homoserine + L-cysteine
L-cystathionine + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-homoserine + L-cysteine
L-cystathionine + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-homoserine + L-cysteine
L-cystathionine + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-homoserine + L-cysteine
L-cystathionine + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-homoserine + L-cysteine
L-cystathionine + acetate
show the reaction diagram
-
gamma-replacement
-
?
O-acetyl-L-homoserine + L-cysteine
L-cystathionine + acetate
show the reaction diagram
-
gamma-replacement
-
-
r
O-acetyl-L-homoserine + L-homocysteine
L-homolanthionine + acetate
show the reaction diagram
-
92% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + m-thiocresol
S-m-tolyl-L-homocysteine + acetate
show the reaction diagram
-
150% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + N-acetyl-L-Cys
S-(L-acetylamino-2-carboxyethyl)-L-homocysteine + acetate
show the reaction diagram
-
12% relative activity to O-acetyl-L-homoserine + L-cysteine
i.e. mono-N-acetyl-L-cystathionine + acetate
?
O-acetyl-L-homoserine + n-butyl mercaptan
S-n-butyl-L-homocysteine + acetate
show the reaction diagram
-
5% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + n-propyl mercaptan
S-n-propyl-L-homocysteine + acetate
show the reaction diagram
-
13% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + o-thiocresol
S-o-tolyl-L-homocysteine + acetate
show the reaction diagram
-
3% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + p-nitrothiophenol
S-p-nitrophenyl-L-homocysteine + acetate
show the reaction diagram
-
41% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + p-thiocresol
S-p-tolyl-L-homocysteine + acetate
show the reaction diagram
-
25% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + phenyl mercaptan
S-phenyl-L-homocysteine + acetate
show the reaction diagram
-
98% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + S2-
L-homocysteine + acetate
show the reaction diagram
-
163% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + sec-butyl mercaptan
S-sec-butyl-L-homocysteine + acetate
show the reaction diagram
-
5% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + tert-butyl mercaptan
S-tert-butyl-L-homosysteine + acetate
show the reaction diagram
-
2% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + thioacetic acid
S-acetyl-L-homocysteine + acetate
show the reaction diagram
-
3% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + thioglycolate ethyl ester
S-ethoxycarbonyl-L-homocysteine + acetate
show the reaction diagram
-
348% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + thioglycolate n-butyl ester
S-n-butoxycarbonyl-L-homocysteine + acetate
show the reaction diagram
-
274% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-acetyl-L-homoserine + thiosalicylic acid
S-o-carboxyphenyl-L-homocysteine + acetate
show the reaction diagram
-
63% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-malonyl-L-homoserine + L-cysteine
L-cystathionine + malonate
show the reaction diagram
-
14% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-phenyl-L-homoserine + L-cysteine
L-cystathionine + phenol
show the reaction diagram
-
1% relative activity to O-acetyl-L-homoserine + L-cysteine
-
?
O-phospho-L-homoserine + L-cysteine
L-cystathionine + phosphate
show the reaction diagram
-
-
-
?
O-phospho-L-homoserine + L-cysteine
L-cystathionine + phosphate
show the reaction diagram
-
-
-
?
O-phospho-L-homoserine + L-cysteine
L-cystathionine + phosphate
show the reaction diagram
-
-
-
?
O-phospho-L-homoserine + L-cysteine
L-cystathionine + phosphate
show the reaction diagram
-
-
-
?
O-phospho-L-homoserine + L-cysteine
L-cystathionine + phosphate
show the reaction diagram
-
-
-
-
?
O-phospho-L-homoserine + L-cysteine
L-cystathionine + phosphate
show the reaction diagram
Neptunia amplexicaulis, Astragalus hamosus
-
-
-
?
O-phospho-L-homoserine + L-cysteine ethyl ester
S-(L-2-amino-2-ethoxycarbonyl)-L-homocysteine + phosphate
show the reaction diagram
-
1% relative activity to O-phospho-L-homoserine + L-cysteine
-
-
?
O-phospho-L-homoserine + L-cysteine methyl ester
S-(L-2-amino-2-methoxycarbonyl)-L-homocysteine + phosphate
show the reaction diagram
-
15% relative activity to O-phospho-L-homoserine + L-cysteine
-
-
?
O-phospho-L-homoserine + L-selenocysteine
selenocystathionine + phosphate
show the reaction diagram
-
-
-
?
O-phospho-L-homoserine + S2-
L-homocysteine + phosphate
show the reaction diagram
-
-
-
-
?
O-phospho-L-homoserine + S2-
L-homocysteine + phosphate
show the reaction diagram
-
13% relative activity to O-phospho-L-homoserine + L-cysteine
-
?
O-succinyl-L-homoserine
succinate + pyruvate + NH3
show the reaction diagram
-
elimination reaction
-
-
?
O-succinyl-L-homoserine + 2-mercaptoethanol
S-ethyl-L-homocysteine + succinate
show the reaction diagram
-
32% of the activity with L-cysteine
-
-
?
O-succinyl-L-homoserine + beta-mercaptopropionate
S-carboxyethyl-L-homocysteine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + CH3SH
L-methionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + CH3SH
L-methionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + CH3SH
L-methionine + succinate
show the reaction diagram
-
-
-
-
?
O-succinyl-L-homoserine + D-cysteine
?
show the reaction diagram
-
20% of the activity with L-cysteine
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-, Q1M0P5
-
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
gamma-elimination, in absence of L-cysteine
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
gamma-elimination, in absence of L-cysteine
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
gamma-elimination
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
-
gamma-elimination
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
Helicobacter pylori SS
Q1M0P5
-
-
-
?
O-succinyl-L-homoserine + H2S
L-homocysteine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + H2S
L-homocysteine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
Pseudomonas dacunhae
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
enzyme catalyzes the first step in methionine biosynthesis, overview
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
first step in bacterial transsulfuration pathway, replacement reaction
-
-
?
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
-
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
methionine biosynthesis
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
the enzyme catalyzes the first reaction specific for methionine biosynthesis
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
P55217
constitutive overexpression of the enzyme in Arabidopsis leads to accumulation of soluble methionine and S-methylmethionine
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
the expression of the enzyme is light-inducible
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
key intermediate in transsulfuration pathways
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
the second enzyme of the methionine biosynthetic pathway
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
key enzyme of Met biosynthesis
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
essential step in bacterial methionine biosynthesis
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
Q9MT29, -
the enzyme catalyzes a near-equilibrium reaction and does not display features of a pathway-regulating enzyme
-
-
-
O-succinyl-L-homoserine + L-selenocysteine
selenocystathionine + succinate
show the reaction diagram
-
-, first step in conversion of selenocysteine to volatile dimethylselenide
-
-
?
O-succinyl-L-homoserine + sodium sulfide
L-homocysteine + sodium succinate
show the reaction diagram
-
62% of the activity with L-cysteine
-
-
?
O-succinyl-L-serine + H2O
succinate + pyruvate + NH3
show the reaction diagram
-
beta-elimination
-
?
O-succinyl-L-serine + H2O
succinate + pyruvate + NH3
show the reaction diagram
-
beta-elimination
-
?
O-succinyl-L-serine + L-cysteine
lanthionine + succinate
show the reaction diagram
-
-
-
?
O-succinyl-L-serine + L-homocysteine
succinate + L-cystathionine
show the reaction diagram
-
beta-replacement, very low reaction rate
-
?
O-succinyl-L-serine + L-homocysteine
succinate + L-cystathionine
show the reaction diagram
-
beta-replacement, very low reaction rate
-
?
L-cystathionine + L-cysteine
L-cystathionine + L-cysteine
show the reaction diagram
-
-
observed via 35S-exchange
-
additional information
?
-
-
beta-elimination and gamma-elimination barely catalyzed
-
-
-
additional information
?
-
-
catalyzes alpha or beta proton exchange with a number of amino acids and L-allylglycine
-
-
-
additional information
?
-
-
exchange of tritium from water into both alpha and beta positions of a wide variety of amino acids which are otherwise no substrates
-
-
-
additional information
?
-
-
S-adenosyl-L-methionine is an effector in the posttranscriptional autoregulation of the CGS1 gene
-
-
-
additional information
?
-
-
the enzyme might by rate-limiting in selenium volatilization
-
-
-
additional information
?
-
-
enzyme performs an elimination or a replacement reaction
-
-
-
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
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
-
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
enzyme catalyzes the first step in methionine biosynthesis, overview
-
-
?
O-succinyl-L-homoserine + L-cysteine
cystathionine + succinate
show the reaction diagram
-
first step in bacterial transsulfuration pathway
-
-
?
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
-
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
methionine biosynthesis
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
the enzyme catalyzes the first reaction specific for methionine biosynthesis
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
P55217
constitutive overexpression of the enzyme in Arabidopsis leads to accumulation of soluble methionine and S-methylmethionine
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
the expression of the enzyme is light-inducible
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
key intermediate in transsulfuration pathways
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
the second enzyme of the methionine biosynthetic pathway
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
key enzyme of Met biosynthesis
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
-
essential step in bacterial methionine biosynthesis
-
-
-
O-succinyl-L-homoserine + L-cysteine
O-acetyl-L-homocysteine + L-cysteine
show the reaction diagram
Q9MT29, -
the enzyme catalyzes a near-equilibrium reaction and does not display features of a pathway-regulating enzyme
-
-
-
O-succinyl-L-homoserine + L-selenocysteine
selenocystathionine + succinate
show the reaction diagram
-
first step in conversion of selenocysteine to volatile dimethylselenide
-
-
?
additional information
?
-
-
S-adenosyl-L-methionine is an effector in the posttranscriptional autoregulation of the CGS1 gene
-
-
-
additional information
?
-
-
the enzyme might by rate-limiting in selenium volatilization
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
binding site
pyridoxal 5'-phosphate
-
4 mol tightly bound per mol of enzyme
pyridoxal 5'-phosphate
-
4 mol per mol of enzyme, Km: 0.021 mM
pyridoxal 5'-phosphate
-
4 mol per tetrameric holoenzyme
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
enzyme is dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent
pyridoxal 5'-phosphate
-
one molecule is attached to one subunit of the protein, apoenzyme is completely inactive. Unfolding by guanidinium/HCl inactivates the enzyme due to loss of ketoenamine tautomer. Though pyridoxal 5'-phosphate induces difference in secondary structure content, it is unable to provide stabilizing effect during the overall secondary structure unfolding process. It induces tertiary structure stability of the protein thereby counteracting the deleterious effect of denaturant
pyridoxal 5'-phosphate
A0PKT3
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1S,3aS,4R,6aR)-1,4-bis(1,3-benzodioxol-5-yl)hexahydropentalen-3a(1H)-ol
-, Q1M0P5
i.e. paulownin, NPLC604, noncompetitive, significant activity in the inhibition of Helicobacter pylori strain SS1 growth with MIC of 15 mg/ml
(1S,3aS,4S,6aS)-1,4-di(3,4,5-trimethoxy)-phenyloctahydropentalene
-, Q1M0P5
i.e. yangambin, NPLC605, noncompetitive, significant activity in the inhibition of Helicobacter pylori strain SS1 growth with MIC of 10 mg/ml
(Z)-3-(2-phosphonethen-1-yl)pyridine-2-carboxylic acid
-
Ki: 0.04 mM
-
(Z)-3-(2-phosphonoethen-1-yl)pyridine-2-carboxylic acid
-
-
2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-, Q1M0P5
i.e. alpha-lapachone, NPLC518, noncompetitive, significant activity in the inhibition of Helicobacter pylori strain SS1 growth with MIC of 2.6 mg/ml
3-(phosphonomethyl)pyridine-2-carboxylic acid
-
-
3-Methyl-2-benzothiazolinone hydrazone
-
-
4-(phosphonomethyl)pyridine-2-carboxylic acid
-
Ki: 0.045 mM
4-(phosphonomethyl)pyridine-2-carboxylic acid
-
-
6-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-, Q1M0P5
i.e. 9-hydroxy-alpha-lapachone, NPLC519, noncompetitive, significant activity in the inhibition of Helicobacter pylori strain SS1 growth with MIC of 2.5 mg/ml
aminooxyacetic acid
-
-
beta-mercaptopropionate
-
competitive inhibitor of gamma-replacement reaction
beta-mercaptopropionate
-
also a substrate for gamma-replacement reaction
chloromercuriphenylsulfonate
-
inhibition of gamma-elimination
cystathionine
-
competitive, gamma-elimination
D-Cysteine
-
inhibition of gamma-elimination
dithiothreitol
-
10% inhibition of beta-elimination from O-succinyl-L-serine
DL-(E)-2-amino-5-phosphono-3-pentenoic acid
-
Ki: 0.0011 mM
DL-(E)-2-amino-5-phosphono-3-pentenoic acid
-
-
DL-propargylglycine
-
irreversible
hydroxylamine
-
-
L-cysteine
-
complete inhibition of gamma-elimination and beta-elimination
L-cysteine
-
inhibition of beta-elimination
L-homocysteine
-
partial inhibition of beta-elimination and gamma-elimination
N-ethylmaleimide
-
inhibition of gamma-elimination
propargylglycine
-
i.e. 2-amino-4-pentynoate
propargylglycine
-
pseudo-first order inactivation kinetics
propargylglycine
-
-
propargylglycine
-
-
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-methionine
-
0.003 mM, 34% inhibition , 0.1 mM, 96% inhibition, physiological inhibitor
S-adenosyl-L-methionine
-
9.5 mM, 50% inhibition
L-methionine
-
2 mM, decreases the expression level of CGS
additional information
-
not inhibited by p-chloromercuribenzoate, iodoacetate, N-ethylmaleimide, 5,5'-dithiobis(2-nitrobenzoate), NaCN
-
additional information
-
no inhibition by 2-amino-1-hydroxycyclobutane-1-acetic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
L-threonine
-
2 mM, increases the expression level of CGS
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.6
-
2-mercaptoethanol
-
-
100
-
CH3SH
-
pH 7.3, 30C, gamma-replacement reaction
3
-
H2S
-
pH 7.3, 30C, gamma-replacement reaction
0.11
-
L-cystathionine
-
wild-type, 25C, pH 7.8
0.26
-
L-cystathionine
-
mutant E325Y 25C, pH 7.8
2.4
-
L-cystathionine
-
mutant D45F, 25C, pH 7.8
0.1
-
L-cysteine
-
pH 7.8, 25C, replacement reaction, ordered mechanism
0.11
-
L-cysteine
-
pH 7.8, 25C, replacement reaction, modified ping-pong mechanism
0.12
-
L-cysteine
-
mutant R49A, pH 7.8, 25C
0.14
-
L-cysteine
-
-
0.15
-
L-cysteine
-
mutant Y101F, pH 7.8, 25C
0.17
-
L-cysteine
-
mutant E325A, pH 7.8, 25C
0.18
-
L-cysteine
-
pH 7.5, 30C
0.2
-
L-cysteine
-
mutant S326A, pH 7.8, 25C
0.22
-
L-cysteine
-
mutant R361K, pH 7.8, 25C; mutant R48K, pH 7.8, 25C
0.23
-
L-cysteine
-
-
0.24
-
L-cysteine
-
wild-type, pH 7.8, 25C
0.29
-
L-cysteine
-
mutant E325Q, pH 7.8, 25C
0.3
-
L-cysteine
-
mutant N227A, pH 7.8, 25C
0.36
-
L-cysteine
-
mutant R49K, pH 7.8, 25C
0.5
-
L-cysteine
-
pH 7.5, 37C
0.6
-
L-cysteine
-
mutant Y46F, pH 7.8, 25C
0.65
-
L-cysteine
-
mutant R106K, pH 7.8, 25C
0.8
-
L-cysteine
-
mutant D45A, pH 7.8, 25C
0.9
-
L-cysteine
-
mutant D45N, pH 7.8, 25C
3
-
L-cysteine
-
mutant R106A, pH 7.8, 25C
0.89
-
L-cysteine methyl ester
-
-
1.4
-
O-phospho-L-homoserine
-
pH 7.5, 30C
3.6
-
O-phospho-L-homoserine
-
pH 7.5, 37C
7.1
-
O-phospho-L-homoserine
-
-
2.85
-
O-phospho-L-serine
-
-
0.05
-
O-succinyl-L-homoserine
-
pH 7.3, 30C, reaction with H2S
0.07
-
O-succinyl-L-homoserine
-
pH 7.3, 30C, gamma-replacement reaction
0.3
-
O-succinyl-L-homoserine
-
pH 7.3, 30C, gamma-elimination reaction
0.32
-
O-succinyl-L-homoserine
-
pH 7.5, 30C
0.33
-
O-succinyl-L-homoserine
-
pH 8.2, 25C, gamma-elimination reaction
0.7
-
O-succinyl-L-homoserine
-
mutant E325A, pH 7.8, 25C
1.1
-
O-succinyl-L-homoserine
-
mutant E325Q, pH 7.8, 25C
1.2
-
O-succinyl-L-homoserine
-
pH 7.8, 25C, replacement reaction, ordered mechanism
1.3
-
O-succinyl-L-homoserine
-
pH 7.8, 25C, elimination reaction, modified ping-pong mechanism
1.3
-
O-succinyl-L-homoserine
-
wild-type, gamma-elimination, 25C, pH 7.8
1.5
-
O-succinyl-L-homoserine
-
mutant D45F/E325Y, gamma-elimination, 25C, pH 7.8
1.7
-
O-succinyl-L-homoserine
-
mutant E325Y, gamma-elimination, 25C, pH 7.8
1.8
-
O-succinyl-L-homoserine
-
mutant R48K, pH 7.8, 25C
1.9
-
O-succinyl-L-homoserine
-
mutant Y101F, pH 7.8, 25C
2
-
O-succinyl-L-homoserine
-
mutant D45F, gamma-elimination, 25C, pH 7.8
2.1
-
O-succinyl-L-homoserine
-
mutant E325Y, gamma-replacement, 25C, pH 7.8
2.5
-
O-succinyl-L-homoserine
-
pH 7.8, 25C, replacement reaction, modified ping-pong mechanism
2.5
-
O-succinyl-L-homoserine
-
wild-type, gamma-replacement, 25C, pH 7.8
3.02
-
O-succinyl-L-homoserine
-, Q1M0P5
25C, pH 9.0
4
-
O-succinyl-L-homoserine
-
pH 7.3, 30C, gamma-replacement reaction
4.4
-
O-succinyl-L-homoserine
-
wild-type, pH 7.8, 25C
5.4
-
O-succinyl-L-homoserine
-
mutant D45F, gamma-replacement, 25C, pH 7.8
8
-
O-succinyl-L-homoserine
-
mutant N227A, pH 7.8, 25C; mutant R49K, pH 7.8, 25C
9
-
O-succinyl-L-homoserine
-
pH 7.3, 30C, reaction wirh CH3SH
11
-
O-succinyl-L-homoserine
-
mutant R106A, pH 7.8, 25C
13.34
-
O-succinyl-L-homoserine
-
pH 7.5, 30C
19
-
O-succinyl-L-homoserine
-
mutant D45A, pH 7.8, 25C
21
-
O-succinyl-L-homoserine
-
mutant S326A, pH 7.8, 25C
39
-
O-succinyl-L-homoserine
-
mutant D45N, pH 7.8, 25C; mutant R106K, pH 7.8, 25C
90
-
O-succinyl-L-homoserine
-
mutant Y46F, pH 7.8, 25C
0.7
-
O-Succinyl-L-serine
-
final, inhibited reaction phase
1.2
-
O-Succinyl-L-serine
-
initial reaction phase
0.6
-
S2-
-
pH 7.5, 30C
0.55
-
Sodium sulfide
-
-
0.07
-
L-selenocysteine
-
-
additional information
-
additional information
-
kinetic analysis of the reaction O-succinyl-L-homoserine + beta-mercaptopropionate
-
additional information
-
additional information
-
detailed kinetics of elimination and replacement reaction, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.67
-
cystathionine
-
pH 8.2, 25C, 460 mol product formed per mol of subunit
5.6
-
L-cystathionine
-
mutant D45F, 25C, pH 7.8
11.1
-
L-cystathionine
-
mutant E325Y 25C, pH 7.8
121
-
L-cystathionine
-
wild-type, 25C, pH 7.8
117
-
L-cysteine
-
pH 7.8, 25C, replacement reaction, ordered mechanism
121
-
L-cysteine
-
pH 7.8, 25C, replacement reaction, modified ping-pong mechanism
0.15
-
O-succinyl-L-homoserine
-
mutant R48K, pH 7.8, 25C
0.297
-
O-succinyl-L-homoserine
-, Q1M0P5
25C, pH 9.0
0.31
-
O-succinyl-L-homoserine
-
mutant S326A, pH 7.8, 25C
0.5
-
O-succinyl-L-homoserine
-
mutant R361K, pH 7.8, 25C
1.23
-
O-succinyl-L-homoserine
-
mutant D45F/E325Y, gamma-elimination, 25C, pH 7.8
1.39
-
O-succinyl-L-homoserine
-
mutant E325Y, gamma-elimination, 25C, pH 7.8
1.4
-
O-succinyl-L-homoserine
-
mutant D45F, gamma-elimination, 25C, pH 7.8
1.4
-
O-succinyl-L-homoserine
-
mutant R106A, pH 7.8, 25C
1.8
-
O-succinyl-L-homoserine
-
pH 7.8, 25C, elimination reaction, modified ping-pong mechanism
1.8
-
O-succinyl-L-homoserine
-
wild-type, gamma-elimination, 25C, pH 7.8
4
-
O-succinyl-L-homoserine
-
gamma-elimination reaction, pH 7.3, 30C
5.3
-
O-succinyl-L-homoserine
-
mutant R106K, pH 7.8, 25C
5.6
-
O-succinyl-L-homoserine
-
mutant R49A, pH 7.8, 25C
6
-
O-succinyl-L-homoserine
-
mutant Y46F, pH 7.8, 25C
9.6
-
O-succinyl-L-homoserine
-
mutant Y101F, pH 7.8, 25C
12.7
-
O-succinyl-L-homoserine
-
gamma-elimination reaction , pH 8.2, 37C
33
-
O-succinyl-L-homoserine
-
mutant N227A, pH 7.8, 25C
57
-
O-succinyl-L-homoserine
-
mutant E325Q, pH 7.8, 25C
59
-
O-succinyl-L-homoserine
-
mutant E325A, pH 7.8, 25C
63.3
-
O-succinyl-L-homoserine
-
gamma-replacement reaction, pH 8.2, 37C
79
-
O-succinyl-L-homoserine
-
mutant D45A, pH 7.8, 25C
100
-
O-succinyl-L-homoserine
-
mutant D45N, pH 7.8, 25C
112
-
O-succinyl-L-homoserine
-
wild-type, pH 7.8, 25C
117
-
O-succinyl-L-homoserine
-
pH 7.8, 25C, replacement reaction, ordered mechanism
121
-
O-succinyl-L-homoserine
-
pH 7.8, 25C, replacement reaction, modified ping-pong mechanism
130
-
O-succinyl-L-homoserine
-
mutant R49K, pH 7.8, 25C
0.133
-
O-Succinyl-L-serine
-
gamma-replacement reaction, pH 8.2, 37C
1.5
-
O-Succinyl-L-serine
-
gamma-elimination reaction, final, inhibited reaction phase, pH 7.3, 30C
3.83
-
O-Succinyl-L-serine
-
gamma-elimination reaction, initial reaction phase, pH 7.3, 30C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2
-
L-cystathionine
-
mutant D45F, 25C, pH 7.8
12148
41
-
L-cystathionine
-
mutant E325Y 25C, pH 7.8
12148
1060
-
L-cystathionine
-
wild-type, 25C, pH 7.8
12148
0.41
-
L-cysteine
-
mutant R106A, pH 7.8, 25C
12151
0.68
-
L-cysteine
-
mutant R48K, pH 7.8, 25C
12151
1.6
-
L-cysteine
-
mutant S326A, pH 7.8, 25C
12151
2.3
-
L-cysteine
-
mutant R361K, pH 7.8, 25C
12151
8.2
-
L-cysteine
-
mutant R106K, pH 7.8, 25C
12151
11.3
-
L-cysteine
-
mutant Y46F, pH 7.8, 25C
12151
50
-
L-cysteine
-
mutant R49A, pH 7.8, 25C
12151
64
-
L-cysteine
-
mutant Y101F, pH 7.8, 25C
12151
99
-
L-cysteine
-
mutant D45A, pH 7.8, 25C
12151
110
-
L-cysteine
-
mutant N227A, pH 7.8, 25C
12151
113
-
L-cysteine
-
mutant D45N, pH 7.8, 25C
12151
200
-
L-cysteine
-
mutant E325Q, pH 7.8, 25C
12151
350
-
L-cysteine
-
mutant E325A, pH 7.8, 25C
12151
360
-
L-cysteine
-
mutant R49K, pH 7.8, 25C
12151
470
-
L-cysteine
-
wild-type, pH 7.8, 25C
12151
0.002
-
O-succinyl-L-homoserine
-
mutant R48K, pH 7.8, 25C
14728
0.005
-
O-succinyl-L-homoserine
-
mutant R361K, pH 7.8, 25C
14728
0.015
-
O-succinyl-L-homoserine
-
mutant S326A, pH 7.8, 25C
14728
0.071
-
O-succinyl-L-homoserine
-
mutant Y46F, pH 7.8, 25C
14728
0.12
-
O-succinyl-L-homoserine
-
mutant R106A, pH 7.8, 25C
14728
0.14
-
O-succinyl-L-homoserine
-
mutant R106K, pH 7.8, 25C
14728
0.69
-
O-succinyl-L-homoserine
-
mutant D45F, gamma-elimination, 25C, pH 7.8
14728
0.8
-
O-succinyl-L-homoserine
-
mutant D45F/E325Y, gamma-elimination, 25C, pH 7.8; mutant E325Y, gamma-elimination, 25C, pH 7.8
14728
1.35
-
O-succinyl-L-homoserine
-
wild-type, gamma-elimination, 25C, pH 7.8
14728
3
-
O-succinyl-L-homoserine
-
mutant D45F, gamma-replacement, 25C, pH 7.8
14728
3.1
-
O-succinyl-L-homoserine
-
mutant R49A, pH 7.8, 25C
14728
4.2
-
O-succinyl-L-homoserine
-
mutant N227A, pH 7.8, 25C
14728
5.1
-
O-succinyl-L-homoserine
-
mutant Y101F, pH 7.8, 25C
14728
7
-
O-succinyl-L-homoserine
-
mutant E325Y, gamma-replacement, 25C, pH 7.8
14728
16
-
O-succinyl-L-homoserine
-
mutant R49K, pH 7.8, 25C
14728
25
-
O-succinyl-L-homoserine
-
wild-type, pH 7.8, 25C
14728
26
-
O-succinyl-L-homoserine
-
mutant D45N, pH 7.8, 25C
14728
42
-
O-succinyl-L-homoserine
-
mutant D45A, pH 7.8, 25C
14728
49
-
O-succinyl-L-homoserine
-
wild-type, gamma-replacement, 25C, pH 7.8
14728
50
-
O-succinyl-L-homoserine
-
mutant E325Q, pH 7.8, 25C
14728
90
-
O-succinyl-L-homoserine
-
mutant E325A, pH 7.8, 25C
14728
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.06
-
(1S,3aS,4R,6aR)-1,4-bis(1,3-benzodioxol-5-yl)hexahydropentalen-3a(1H)-ol
-, Q1M0P5
25C, pH 9.0
0.031
-
(1S,3aS,4S,6aS)-1,4-di(3,4,5-trimethoxy)-phenyloctahydropentalene
-, Q1M0P5
25C, pH 9.0
0.04
-
(Z)-3-(2-phosphonethen-1-yl)pyridine-2-carboxylic acid
-
pH 7.5, 37C
-
0.45
-
(Z)-3-(2-phosphonoethen-1-yl)pyridine-2-carboxylic acid
-
-
0.019
-
2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-, Q1M0P5
25C, pH 9.0
0.2
-
3-(phosphonomethyl)pyridine-2-carboxylic acid
-
-
0.045
-
4-(phosphonomethyl)pyridine-2-carboxylic acid
-
pH 7.5, 37C
0.3
-
4-(phosphonomethyl)pyridine-2-carboxylic acid
-
-
0.016
-
6-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-, Q1M0P5
25C, pH 9.0
0.0011
-
DL-(E)-2-amino-5-phosphono-3-pentenoic acid
-
pH 7.5, 37C
0.027
-
DL-(E)-2-amino-5-phosphono-3-pentenoic acid
-
-
9.5
-
S-adenosyl-L-methionine
-
pH 7.5, 37C
0.018
-
DL-propargylglycine
-
-
additional information
-
additional information
-
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.019
-
(1S,3aS,4R,6aR)-1,4-bis(1,3-benzodioxol-5-yl)hexahydropentalen-3a(1H)-ol
-, Q1M0P5
25C, pH 9.0
0.027
-
(1S,3aS,4S,6aS)-1,4-di(3,4,5-trimethoxy)-phenyloctahydropentalene
-, Q1M0P5
25C, pH 9.0
0.011
-
2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-, Q1M0P5
25C, pH 9.0
0.009
-
6-hydroxy-2,2-dimethyl-3,4-dihydro-2H-benzo[g]chromene-5,10-dione
-, Q1M0P5
25C, pH 9.0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.403
-
-, Q1M0P5
25C, pH 9.0
3.7
-
-
plasmid pSL109
10.5
-
-
O-succinyl-L-homoserine + L-cysteine, gamma-replacement reaction
18.7
-
-
O-succinyl-L-homoserine + L-cysteine, gamma-replacement reaction
37
-
-
plasmid pSL123
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
elimination reaction
7.5
-
-, Q1M0P5
-
7.8
-
-
replacement reaction
8.2
-
-
O-succinyl-L-homoserine + H2O
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
O-succinyl-L-homoserine + H2O, 12% of the reaction rate at pH 8.2; O-succinyl-L-serine + H2O, 28% of the reaction rate at pH 8.2
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
45
-
-, Q1M0P5
-
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
56000
-
-
SDS-PAGE
160000
-
-
sedimentation equilibrium centrifugation
160000
-
-
gel filtration
160000
-
-
sedimentation equilibrium centrifugation
160000
-
-
gel filtration, both apo- and holoenzyme
165000
-
-
gel filtration
194000
-
-
gel filtration
215000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 41655, SDS-PAGE
tetramer
-
4 * 48000, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
4 * 43000, SDS-PAGE
tetramer
-
4 * 39000, SDS-PAGE; 4 * 41503, calculation from sequence of DNA
tetramer
-
4 * 41200, SDS-PAGE
tetramer
-
4 * 50000 or 2 * 50000 + 2 * 53000, SDS-PAGE
tetramer
-
4 * 41000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
during an initial period of folate starvation, S-adenosyl-Met and Met pools decline, but are further restored to typical levels. Re-establishment of Met and S-adenosyl-Met homeostasis is concomitant with the removal of 92 amino acids at the N terminus of cystathionine gamma-synthase. Processing is specifically associated with perturbation of the folates pool and involves chloroplastic serine-type proteases
proteolytic modification
-
the 50000 Da polypeptide may be derived from the 53000 Da polypeptide by proteolysis
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure at 1.5 A resulution
P00935
in silico modeling and pyridoxal 5'-phosphate cofactor docking study
-
to 1.9 A resolution. Cofactor pyridoxal 5'-phosphate binds tightly to Lys208 with a covalent-bond length ranging between 1.3 and 1.4 A. The cofactor is stabilized by a series of hydrogen bonds from Gly86, Met87, Asn158, Asp183 and Ser205 from one monomer and Tyr56 and Arg58 from the second monomer
A0PKT3
crystals grown by sitting drop vapour diffusion against a reservoir containing 100 mM MES-NaOH
-
to 2.4 A resolution, tetragonal space group I41
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
EDTA and dithiothreitol stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 10 mM potassium phosphate buffer, pH 7.5, 50% glycerol
-
-15C, protein concentration 10 mg/ml, 6-12 months stable
-
-20C, 20 mM MOPS-NaOH, pH 7.5, 1 mM EDTA, 1 mM DTT, 10% v/v glycerol, 5 days, 50% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant protein
-, Q1M0P5
recombinant enzyme
-
simultaneous purification of EC 4.4.1.1 and EC 4.2.99.2
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
co-expression of Arabidopsis thaliana cystathionine gamma-synthase and bacterial feedback-insensitive aspartate kinase in tobacco
-
construction of transgenic Brassica juncea plants overexpressing the enzyme
-
expressed in Medicago sativa
-
expressed in Nicotiana tabacum
-
expression in Escherichia coli
-
gene CGS1, primer extension studies, wheat germ in vitro translation in presence of S-adenosyl-L-methionine results in a 5'-truncated enzyme
-
overexpression of full-length enzyme and its truncated version that lacks the N-terminal region in transgenic Nicotiana tabacum plants. Transgenic plants expressing both types of enzyme have a significant higher level of Met and S-methyl-Met content in their proteins. Plants expressing full-length enzyme show the same phenotype and developmental pattern as wild-type plants, those expressing the truncated length enzyme show a severely abnormal phenotype. The N-terminal region plays a role in protecting plants from a high level of Met catabolic products such as ethylene
-
transgenic plants overexpressing the enzyme under the control of the cauliflower mosaic virus 35S promoter show increased soluble Met and its metabolite S-methyl-Met
-
expression in Escherichia coli
-
cloned from strain JM103, expression in strain DH10B
-
expression in Escherichia coli
-, Q1M0P5
expression in Escherichia coli
A0PKT3
overexpression in Escherichia coli
-
expression of the CYS3 gene in Escherichia coli, the protein shows activities of EC 4.4.1.1, EC 4.4.1.8, and EC 2.5.1.8
-
the truncated cDNA without putative leader peptide, when cloned into a bacterial expression vector, complements the Escherichia coli metB1 mutant strain LE392
-
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D45A
-
decrease in kcat and increase in Km value of succinyl-L-homoserine substrate
D45F
-
reduction in catalytic effciency, without change in reaction specificity
D45F/E325Y
-
reduction in catalytic effciency, without change in reaction specificity
D45N
-
decrease in kcat and increase in Km value of succinyl-L-homoserine substrate
E325A
-
decrease in kcat and increase in Km values of substrates
E325Q
-
kinetic values similar to wild-type
E325Y
-
reduction in catalytic effciency, without change in reaction specificity
N227A
-
decrease in kcat value of succinyl-L-homoserine substrate
R106A
-
the Arg residues at positions 48, 106 and 361 tether the distal and alpha-carboxylate moieties, respectively, of the succinyl-L-homoserine substrate
R106K
-
the Arg residues at positions 48, 106 and 361 tether the distal and alpha-carboxylate moieties, respectively, of the succinyl-L-homoserine substrate
R361A
-
almost complete loss of activity
R361K
-
the Arg residues at positions 48, 106 and 361 tether the distal and alpha-carboxylate moieties, respectively, of the succinyl-L-homoserine substrate
R48A
-
almost complete loss of activity
R48K
-
the Arg residues at positions 48, 106 and 361 tether the distal and alpha-carboxylate moieties, respectively, of the succinyl-L-homoserine substrate
R49A
-
decrease in kcat value
R49K
-
3fold increase in Km value for both succinyl-L-homoserine and L-cysteine
S326A
-
decrease in kcat and increase in Km value of succinyl-L-homoserine substrate
Y101F
-
decrease in kcat value
Y46F
-
large decrease in kcat and increase in Km value of succinyl-L-homoserine substrate
additional information
-
overexpression of full-length enzyme and its truncated version that lacks the N-terminal region in transgenic Nicotiana tobacum plants. Transgenic plants expressing both types of enzyme have a significant higher level of Met and S-methyl-Met content in their proteins. Plants expressing full-length enzyme show the same phenotype and developmental pattern as wild-type plants, those expressing the truncated length enzyme show a severely abnormal phenotype
additional information
-
overexpression of the enzyme in Brassica juncea, 5 transgenic lines with up to 10fold increased enzyme level, enzyme expression enhances selenium volatilization in the transgenic plants compared to the wild-type plants, transgenic plants show increased tolerance against selenite and reduced selenite levels in shoots and roots, overview
additional information
-
co-expression of Arabidopsis thaliana cystathionine gamma-synthase and bacterial feedback-insensitive aspartate kinase in tobacco. Plants co-expressing both enzymes have significantly higher methionine and threonine levels compared with the levels found in wild-type plants, but the methionine level does not increase beyond that found in plants expressing cystathionine gamma-synthase alone. Plants expressing bacterial feedback-insensitive aspartate kinase and one of two mutated forms of cystathionine gamma-synthase in which the domains responsible for the feedback regulation have been deleted, show significantly higher methionine contents and its metabolites levels accumulate in the newly produced plants. The levels of threonine are also significantly higher than in the wild-type plants. The transcript level of the two mutated forms of cystathionine gamma-synthase significantly increases when there is a high content of threonine in the plants, suggesting that threonine modulates, probably indirectly, the transcript level of cystathionine gamma-synthase
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unfolding by guanidinium/HCl inactivates the enzyme due to loss of ketoenamine tautomer. Though pyridoxal 5'-phosphate induces difference in secondary structure content, it is unable to provide stabilizing effect during the overall secondary structure unfolding process. It induces tertiary structure stability of the protein thereby counteracting the deleterious effect of denaturant
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
production of alpha or beta deuterated amino acids
synthesis
-
production of L-cystathionine