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Information on EC 2.5.1.48 - cystathionine gamma-synthase and Organism(s) Escherichia coli and UniProt Accession P00935

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IUBMB Comments
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.
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This record set is specific for:
Escherichia coli
UNIPROT: P00935
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cystathionine gamma-synthase, cystathionine synthase, atcgs, cystathionine synthetase, cystathionine-gamma-synthase, o-succinylhomoserine synthetase, o-succinylhomoserine synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CS,26
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-
-
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cystathionine synthase
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-
-
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cystathionine synthetase
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-
-
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cystathionine-gamma-synthase
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-
-
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homoserine O-transsuccinylase
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-
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homoserine transsuccinylase
O-succinyl-L-homoserine succinate-lyase (adding cysteine)
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-
-
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O-succinylhomoserine (Thiol)-lyase
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O-succinylhomoserine synthase
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-
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O-succinylhomoserine synthetase
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synthase, cystathionine gamma-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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gamma-replacement
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-70-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-cystathionine + acetate
O-acetyl-L-homoserine + L-cysteine
show the reaction diagram
-
-
-
-
r
O-acetyl-L-homoserine + L-cysteine
L-cystathionine + acetate
show the reaction diagram
O-succinyl-L-homoserine
succinate + pyruvate + NH3
show the reaction diagram
-
elimination reaction
-
-
?
O-succinyl-L-homoserine + H2O
succinate + 2-oxobutyrate + NH3
show the reaction diagram
O-succinyl-L-homoserine + L-cysteine
L-cystathionine + succinate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
O-succinyl-L-homoserine + L-cysteine
L-cystathionine + succinate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 2.4
L-cystathionine
0.1 - 3
L-cysteine
0.33 - 90
O-succinyl-L-homoserine
additional information
additional information
-
detailed kinetics of elimination and replacement reaction, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.67
cystathionine
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pH 8.2, 25°C, 460 mol product formed per mol of subunit
5.6 - 121
L-cystathionine
117 - 121
L-cysteine
0.15 - 130
O-succinyl-L-homoserine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 1060
L-cystathionine
0.41 - 470
L-cysteine
0.002 - 90
O-succinyl-L-homoserine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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elimination reaction
7.8
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replacement reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
39000
-
4 * 39000, SDS-PAGE
40000
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4 * 40000, SDS-PAGE
41503
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4 * 41503, calculation from sequence of DNA
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 1.5 A resulution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D45A
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decrease in kcat and increase in Km value of succinyl-L-homoserine substrate
D45F
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reduction in catalytic effciency, without change in reaction specificity
D45F/E325Y
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reduction in catalytic effciency, without change in reaction specificity
D45N
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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
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kinetic values similar to wild-type
E325Y
-
reduction in catalytic effciency, without change in reaction specificity
N227A
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decrease in kcat value of succinyl-L-homoserine substrate
R106A
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the Arg residues at positions 48, 106 and 361 tether the distal and alpha-carboxylate moieties, respectively, of the succinyl-L-homoserine substrate
R106K
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the Arg residues at positions 48, 106 and 361 tether the distal and alpha-carboxylate moieties, respectively, of the succinyl-L-homoserine substrate
R361A
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almost complete loss of activity
R361K
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the Arg residues at positions 48, 106 and 361 tether the distal and alpha-carboxylate moieties, respectively, of the succinyl-L-homoserine substrate
R48A
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almost complete loss of activity
R48K
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the Arg residues at positions 48, 106 and 361 tether the distal and alpha-carboxylate moieties, respectively, of the succinyl-L-homoserine substrate
R49A
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decrease in kcat value
R49K
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3fold increase in Km value for both succinyl-L-homoserine and L-cysteine
S326A
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decrease in kcat and increase in Km value of succinyl-L-homoserine substrate
Y101F
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decrease in kcat value
Y46F
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large decrease in kcat and increase in Km value of succinyl-L-homoserine substrate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned from strain JM103, expression in strain DH10B
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
construction of an Escherichia coli strain for production of O-succinyl-L-homoserine. The metJ transcriptional repressor and metI subunit of DL-methionine transporter are deleted, metL (encodes bifunctional aspartate kinase/homoserine dehydrogenase II) is overexpressed and metB (encodes cystathionine gamma-synthase) is inactivated. The O-succinyl-L-homoserine titer thus increases to 7.30 g/l. Release of the feedback regulation leads to production of 9.31 g/l O-succinyl-L-homoserine from 20 g/l glucose in batch fermentation
synthesis
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production of alpha or beta deuterated amino acids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martel, A.; Bouthier de la Tour, C.; le Goffic, F.
Pyridoxal 5 phosphate binding site of Escherichia coli beta cystathionase and cystathionine gamma synthase comparison of their sequences
Biochem. Biophys. Res. Commun.
147
565-571
1987
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Wiebers, J.L.; Garner, H.R.
Acyl derivatives of homoserine as substrates for homocysteine synthesis in Neurospora crassa, yeast and Escherichia coli
J. Biol. Chem.
242
5644-5649
1967
Escherichia coli
Manually annotated by BRENDA team
Tran, S.V.; Schaeffer, E.; Bertrand, O.; Mariuzza, R.; Ferrara, P.
Appendix. Purification, molecular weight, and NH2-terminal sequence of cystathionine gamma-synthase of Escherichia coli
J. Biol. Chem.
258
14872-14873
1983
Escherichia coli
Manually annotated by BRENDA team
Kanzaki, H.; Kobayashi, M.; Nagasawa, T.; Yamada, H.
Distribution to two kinds of cystathionine gamma-synthase in various bacteria
FEMS Microbiol. Lett.
33
65-68
1987
Acinetobacter calcoaceticus, Agrobacterium tumefaciens, Alcaligenes faecalis, Aneurinibacillus aneurinilyticus, Bacillus subtilis, Bacillus pumilus, Lysinibacillus sphaericus, Escherichia coli, Pectobacterium carotovorum, Pseudomonas putida, Pseudomonas dacunhae, Salmonella enterica subsp. enterica serovar Typhimurium
-
Manually annotated by BRENDA team
Litzenberger Holbrook, E.; Greene, R.C.; Heilig Krueger, J.
Purification and properties of cystathionine gamma-synthase from overproducing strains of Escherichia coli
Biochemistry
29
435-442
1990
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Homer, R.J.; Kim, M.S.; LeMaster, D.M.
The use of cystathionine gamma-synthase in the production of alpha and chiral beta deuterated amino acids
Anal. Biochem.
215
211-215
1993
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Clausen, T.; Huber, R.; Prade, L.; Wahl, M.C.; Messerschmidt, A.
Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution
EMBO J.
17
6827-6838
1998
Escherichia coli (P00935), Escherichia coli
Manually annotated by BRENDA team
Aitken, S.M.; Kim, D.H.; Kirsch, J.F.
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for the elimination and substitution reactions
Biochemistry
42
11297-11306
2003
Escherichia coli
Manually annotated by BRENDA team
Ziegler, K.; Noble, S.M.; Mutumanje, E.; Bishop, B.; Huddler, D.P.; Born, T.L.
Identification of catalytic cysteine, histidine, and lysine residues in Escherichia coli homoserine transsuccinylase
Biochemistry
46
2674-2683
2007
Escherichia coli
Manually annotated by BRENDA team
Goudarzi, M.; Born, T.L.
Purification and characterization of Thermotoga maritima homoserine transsuccinylase indicates it is a transacetylase
Extremophiles
10
469-478
2006
Escherichia coli
Manually annotated by BRENDA team
Farsi, A.; Lodha, P.H.; Skanes, J.E.; Los, H.; Kalidindi, N.; Aitken, S.M.
Interconversion of a pair of active-site residues in Escherichia coli cystathionine gamma-synthase, E. coli cystathionine beta-lyase, and Saccharomyces cerevisiae cystathionine gamma-lyase and development of tools for the investigation of their mechanisms
Biochem. Cell Biol.
87
445-457
2009
Escherichia coli
Manually annotated by BRENDA team
Jaworski, A.F.; Lodha, P.H.; Manders, A.L.; Aitken, S.M.
Exploration of the active site of Escherichia coli cystathionine gamma-synthase
Protein Sci.
21
1662-1671
2012
Escherichia coli
Manually annotated by BRENDA team
Huang, J.F.; Zhang, B.; Shen, Z.Y.; Liu, Z.Q.; Zheng, Y.G.
Metabolic engineering of E. coli for the production of O-succinyl-L-homoserine with high yield
3 Biotech
8
310
2018
Escherichia coli (P00935), Escherichia coli K12 (P00935)
Manually annotated by BRENDA team