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Information on EC 6.3.1.8 - glutathionylspermidine synthase and Organism(s) Escherichia coli and UniProt Accession P0AES0

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EC Tree
IUBMB Comments
Requires magnesium ions. Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine amidase (EC 3.5.1.78) reaction, resulting in a net hydrolysis of ATP.
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This record set is specific for:
Escherichia coli
UNIPROT: P0AES0
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
glutathionylspermidine synthetase, gsp synthetase, ligsps, glutathionylspermidine synthase, bifunctional glutathionylspermidine synthetase/amidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bifunctional glutathionylspermidine synthetase/amidase
UniProt
Gen Bank AE000381-derived protein GI 1789361
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GenBank U66520-derived protein GI 1813514
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Glutathione:spermidine ligase (ADP-forming)
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Glutathione:spermidine ligase [ADP-forming]
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glutathionylspermidine synthetase
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Glutathionylspermidine synthetase (Crithidia fasciculata strain HS6 gene Cf-GSS)
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Glutathionylspermidine synthetase (Crithidia fasciculata)
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Glutathionylspermidine synthetase/amidase
Gsp synthetase
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Protein (Escherichia coli strain K12-MG1655 gene gsp)
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Synthetase, glutathionylspermidine
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Synthetase, glutathionylspermidine (Crithidia fasciculata fragment)
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Synthetase, glutathionylspermidine (Crithidia fasciculata strain HS6 gene Cf-GSS)
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Synthetase, glutathionylspermidine (Crithidia fasciculata)
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Synthetase, glutathionylspermidine (Escherichia coli clone pJBM1 gene gsp)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid amide formation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming) [spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule]
Requires magnesium ions. Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine amidase (EC 3.5.1.78) reaction, resulting in a net hydrolysis of ATP.
CAS REGISTRY NUMBER
COMMENTARY hide
168257-36-1
synthetase, glutathionylspermidine (Escherichia coli clone pJBM1 gene gsp), GenBank AE000381-derived protein GI 1789361, protein (Escherichia coli strain K12-MG1655 gene gsp)
190209-90-6
synthetase, glutathionylspermidine (Crithidia fasciculata), glutathionylspermidine synthetase (Crithidia fasciculata)
209273-40-5
synthetase, glutathionylspermidine (Crithidia fasciculata fragment)
213260-31-2
synthetase, glutathionylspermidine (Crithidia fasciculata strain HS6 gene Cf-GSS), genBank U66520-derived protein GI 1813514, glutathionylspermidine synthetase (Crithidia fasciculata strain HS6 gene Cf-GSS)
9077-09-2
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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
gamma-L-Glu-L-Cys-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
show the reaction diagram
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
?
show the reaction diagram
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key enzyme that participates in the first of two similar steps of trypanothione biosynthesis
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?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
show the reaction diagram
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?
additional information
?
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Escherichia coli proteins YgiC and YjfC, encoded by genes ygiC and yjfC, cannot synthesize G-Sp, GSH, or GSH intermediates, they are no glutathionylspermidine synthetase/amidases, but show ATP-hydrolysis activity
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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
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
?
show the reaction diagram
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key enzyme that participates in the first of two similar steps of trypanothione biosynthesis
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?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
show the reaction diagram
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?
additional information
?
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Escherichia coli proteins YgiC and YjfC, encoded by genes ygiC and yjfC, cannot synthesize G-Sp, GSH, or GSH intermediates, they are no glutathionylspermidine synthetase/amidases, but show ATP-hydrolysis activity
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2-[[([2-[(4-amino-4-carboxybutanoyl)amino]propanoyl]amino)methyl](hydroxy)phosphoryl]ethyl)(hydroxy)dioxophosphate(1-)
inhibits the reaction in the presence of spermidine
4-[(14-ammonio-5-hydroxy-1-methyl-5-oxido-2-oxo-6-oxa-3,10-diaza-5-phosphatetradec-1-yl)amino]-1-carboxy-4-oxobutan-1-aminium
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4-[[2-([[[4-[(4-ammoniobutyl)amino]butyl](hydroxy)phosphoryl]methyl]amino)-1-methyl-2-oxoethyl]amino]-1-carboxy-4-oxobutan-1-aminium
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gamma-glutamyl-N-[[(3-aminopropoxy)(2-phosphonoethyl)phosphoryl]methyl]alaninamide
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Hydrogen O-[3-[N-(4-Aminobutyl)amino]propyl][[(gamma-glutamylalanyl)amino]methyl]phosphonate
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N1-glutathionylspermidine analogs
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selective inhibitors against EC 6.3.1.8 and EC 3.5.1.78 activities provide evidence of interdomain communication in the bifunctional enzyme
Non-polyamine-containing phosphoamidate
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Polyamine-containing phosphapeptides
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potent and selective
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0224 - 7.298
glutathione
0.076 - 4.522
spermidine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
4-[(14-ammonio-5-hydroxy-1-methyl-5-oxido-2-oxo-6-oxa-3,10-diaza-5-phosphatetradec-1-yl)amino]-1-carboxy-4-oxobutan-1-aminium
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0.0000078
4-[[2-([[[4-[(4-ammoniobutyl)amino]butyl](hydroxy)phosphoryl]methyl]amino)-1-methyl-2-oxoethyl]amino]-1-carboxy-4-oxobutan-1-aminium
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
hypersensitivities of the GspSA/glutaredoxin null mutants to H2O2 support the idea that GspSA and Grx synergistically defend against oxidative damage
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
138000
analytical ultracentrifugation
70000
2 * 70000, analytical ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 70000, analytical ultracentrifugation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method generating crystals of GspS in 0.1M Tris–HCl (pH 8.5) containing 12% (v/v) PEG3350 and 0.5 M MgCl2
mutant C59A lacking amidase activity, in complex with amidase substrate gluthionylspermidine and ADP. Homodimer, and each monomer contains the N-terminal amidase and C-terminal synthetase domains connected by a linker in between
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C338A
increased Km compared to the wild type enzyme
E391A
increased Km compared to the wild type enzyme
E392A
increased Km compared to the wild type enzyme
K607A
increased Km compared to the wild type enzyme
R316E
no activity
R538A
increased Km compared to the wild type enzyme
R598A
decreased Km compared to the wild type enzyme
S335A
increased Km compared to the wild type enzyme
S337A
increased Km compared to the wild type enzyme
T441A
increased Km compared to the wild type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
purified recombinant GspSA C59A, 3 min, inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel affinity column chromatography
recombinant enzyme mutant GspSA C59A from Escherichia coli strain BL21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
expression of enzyme mutant GspSA C59A in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tabor, H.; Tabor, C.W.
Glutathionylspermidine synthetase
Methods Enzymol.
17
815-817
1971
Escherichia coli
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Manually annotated by BRENDA team
Lin, C.H.; Chen, S.; Kwon, D.S.; Coward, J.K.; Walsh, C.T.
Aldehyde and phosphinate analogs of glutathione and glutathionylspermidine: potent, selective binding inhibitors of the E. coli bifunctional glutathionylspermidine synthetase/amidase
Chem. Biol.
4
859-866
1997
Escherichia coli
Manually annotated by BRENDA team
Chen, S.; Lin, C.H.; Kwon, D.S.; Walsh, C.T.; Coward, J.K.
Design, synthesis, and biochemical evaluation of phosphonate and phosphonamidate analogs of glutathionylspermidine as inhibitors of glutathionylspermidine synthetase/amidase from Escherichia coli
J. Med. Chem.
40
3842-3850
1997
Escherichia coli
Manually annotated by BRENDA team
Bollinger, J.M.; Kwon, D.S.; Huisman, G.W.; Kolter, R.; Walsh, C.T.
Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase
J. Biol. Chem.
270
14031-14041
1995
Escherichia coli
Manually annotated by BRENDA team
Pai, C.H.; Chiang, B.Y.; Ko, T.P.; Chou, C.C.; Chong, C.M.; Yen, F.J.; Chen, S.; Coward, J.K.; Wang, A.H.; Lin, C.H.
Dual binding sites for translocation catalysis by Escherichia coli glutathionylspermidine synthetase
EMBO J.
25
5970-5982
2006
Escherichia coli (P0AES0), Escherichia coli
Manually annotated by BRENDA team
Chiang, B.Y.; Chen, T.C.; Pai, C.H.; Chou, C.C.; Chen, H.H.; Ko, T.P.; Hsu, W.H.; Chang, C.Y.; Wu, W.F.; Wang, A.H.; Lin, C.H.
Protein S-thiolation by Glutathionylspermidine (Gsp): the role of Escherichia coli Gsp synthetase/amidase in redox regulation
J. Biol. Chem.
285
25345-25353
2010
Escherichia coli (P0AES0)
Manually annotated by BRENDA team
Pai, C.H.; Wu, H.J.; Lin, C.H.; Wang, A.H.
Structure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of cysteine; histidine-dependent amidohydrolases/peptidases
Protein Sci.
20
557-566
2011
Escherichia coli (P0AES0)
Manually annotated by BRENDA team
Sui, L.; Warren, J.C.; Russell, J.P.; Stourman, N.V.
Comparison of the functions of glutathionylspermidine synthetase/amidase from E. coli and its predicted homologues YgiC and YjfC
Int. J. Biochem. Mol. Biol.
3
302-312
2012
Escherichia coli (P0AES0)
Manually annotated by BRENDA team