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Information on EC 2.5.1.48 - cystathionine gamma-synthase and Organism(s) Arabidopsis thaliana and UniProt Accession P55217

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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:
Arabidopsis thaliana
UNIPROT: P55217
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
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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cystathionine synthase
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cystathionine synthetase
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cystathionine-gamma-synthase
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homoserine O-transsuccinylase
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homoserine transsuccinylase
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O-succinyl-L-homoserine succinate-lyase (adding cysteine)
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O-succinylhomoserine (Thiol)-lyase
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O-succinylhomoserine synthase
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O-succinylhomoserine synthetase
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synthase, cystathionine gamma-
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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
O-succinyl-L-homoserine + L-cysteine
L-cystathionine + succinate
show the reaction diagram
O-succinyl-L-homoserine + CH3SH
L-methionine + succinate
show the reaction diagram
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-
-
-
?
O-succinyl-L-homoserine + L-cysteine
L-cystathionine + succinate
show the reaction diagram
O-succinyl-L-homoserine + L-selenocysteine
selenocystathionine + succinate
show the reaction diagram
additional information
?
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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
O-succinyl-L-homoserine + L-cysteine
L-cystathionine + succinate
show the reaction diagram
O-succinyl-L-homoserine + L-selenocysteine
selenocystathionine + succinate
show the reaction diagram
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first step in conversion of selenocysteine to volatile dimethylselenide
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-
?
additional information
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-methionine
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2 mM, decreases the expression level of CGS
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-threonine
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2 mM, increases the expression level of CGS
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CGS1_ARATH
563
0
59919
Swiss-Prot
Chloroplast (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
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SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CGS1, primer extension studies, wheat germ in vitro translation in presence of S-adenosyl-L-methionine results in a 5'-truncated enzyme
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
co-expression of Arabidopsis thaliana cystathionine gamma-synthase and bacterial feedback-insensitive aspartate kinase in tobacco
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construction of transgenic Brassica juncea plants overexpressing the enzyme
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expressed in Medicago sativa
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expressed in Nicotiana tabacum
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expression in Escherichia coli
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ravanel, S.; Gakiere, B.; Job, D.; Douce, R.
Cystathionine gamma-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli
Biochem. J.
331
639-648
1998
Arabidopsis thaliana
-
Manually annotated by BRENDA team
Kim, J.; Lee, M.; Chalam, R.; Martin, M.N.; Leustek, T.; Boerjan, W.
Constitutive overexpression of cystathionine gamma-synthase in Arabidopsis leads to accumulation of soluble methionine and S-methylmethionine
Plant Physiol.
128
95-107
2002
Arabidopsis thaliana (P55217)
Manually annotated by BRENDA team
Hacham, Y.; Avraham, T.; Amir, R.
The N-terminal region of Arabidopsis cystathionine gamma-synthase plays an important regulatory role in methionine metabolism
Plant Physiol.
128
454-462
2002
Arabidopsis thaliana
Manually annotated by BRENDA team
Van Huysen, T.; Abdel-Ghany, S.; Hale, K.L.; LeDuc, D.; Terry, N.; Pilon-Smits, E.A.
Overexpression of cystathionine-gamma-synthase enhances selenium volatilization in Brassica juncea
Planta
218
71-78
2003
Arabidopsis thaliana
Manually annotated by BRENDA team
Chiba, Y.; Sakurai, R.; Yoshino, M.; Ominato, K.; Ishikawa, M.; Onouchi, H.; Naito, S.
S-adenosyl-L-methionine is an effector in the posttranscriptional autoregulation of the cystathionine gamma-synthase gene in Arabidopsis
Proc. Natl. Acad. Sci. USA
100
10225-10230
2003
Arabidopsis thaliana (P55217), Arabidopsis thaliana
Manually annotated by BRENDA team
Avraham, T.; Amir, R.
The expression level of threonine synthase and cystathionine-gamma-synthase is influenced by the level of both threonine and methionine in Arabidopsis plants
Transgenic Res.
14
299-311
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Avraham, T.; Badani, H.; Galili, S.; Amir, R.
Enhanced levels of methionine and cysteine in transgenic alfalfa (Medicago sativa L.) plants over-expressing the Arabidopsis cystathionine gamma-synthase gene
Plant Biotechnol. J.
3
71-79
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Hacham, Y.; Schuster, G.; Amir, R.
An in vivo internal deletion in the N-terminus region of Arabidopsis cystathionine gamma-synthase results in CGS expression that is insensitive to methionine
Plant J.
45
955-967
2006
Arabidopsis thaliana
Manually annotated by BRENDA team
Hacham, Y.; Matityahu, I.; Schuster, G.; Amir, R.
Overexpression of mutated forms of aspartate kinase and cystathionine gamma-synthase in tobacco leaves resulted in the high accumulation of methionine and threonine
Plant J.
54
260-271
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Loizeau, K.; Gambonnet, B.; Zhang, G.F.; Curien, G.; Jabrin, S.; Van Der Straeten, D.; Lambert, W.E.; Rebeille, F.; Ravanel, S.
Regulation of one-carbon metabolism in Arabidopsis: the N-terminal regulatory domain of cystathionine gamma-synthase is cleaved in response to folate starvation
Plant Physiol.
145
491-503
2007
Arabidopsis thaliana
Manually annotated by BRENDA team