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6.3.1.8: glutathionylspermidine synthase

This is an abbreviated version!
For detailed information about glutathionylspermidine synthase, go to the full flat file.

Word Map on EC 6.3.1.8

Reaction

glutathione
+
spermidine
 +
ATP
=
glutathionylspermidine
 +
ADP
 +
phosphate

Synonyms

bifunctional glutathionylspermidine synthetase/amidase, Gen Bank AE000381-derived protein GI 1789361, GenBank U66520-derived protein GI 1813514, Glutathione:spermidine ligase (ADP-forming), Glutathione:spermidine ligase [ADP-forming], glutathionylspermidine synthetase, Glutathionylspermidine synthetase (Crithidia fasciculata strain HS6 gene Cf-GSS), Glutathionylspermidine synthetase (Crithidia fasciculata), Glutathionylspermidine synthetase/amidase, Gsp synthetase, GspS, GspSA, LiGSPS, Protein (Escherichia coli strain K12-MG1655 gene gsp), Synthetase, glutathionylspermidine, Synthetase, glutathionylspermidine (Crithidia fasciculata fragment), Synthetase, glutathionylspermidine (Crithidia fasciculata strain HS6 gene Cf-GSS), Synthetase, glutathionylspermidine (Crithidia fasciculata), Synthetase, glutathionylspermidine (Escherichia coli clone pJBM1 gene gsp), TryS

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.1 Acid—ammonia (or amine) ligases (amide synthases)
                6.3.1.8 glutathionylspermidine synthase

Reference

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Reference on EC 6.3.1.8 - glutathionylspermidine synthase

Please use the Reference Search for a specific query.
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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
-
Manually annotated by BRENDA team
Nadeau, K.C.
Biochemical studies on protein folding chaperones (HSP90 and cyclophilin) and on trypanosomal enzymes (trypanothione and glutathionylspermidine synthetases) (heat shock protein)
Diss. Abstr. Int. B
56
3744
1995
Crithidia fasciculata
-
Manually annotated by BRENDA team
Smith, K.; Nadeau, K.; Bradley, M.; Walsh, C.; Fairlamb, A.H.
Purification of glutathionylspermidine and trypanothione synthetase from Crithidia fasciculata
Protein Sci.
1
874-883
1992
Crithidia fasciculata
Manually annotated by BRENDA team
Tetaud, E.; Manai, F.; Barrett, M.P.; Nadeau, K.; Walsh, C.T.; Fairlamb, A.H.
Cloning and characterization of the two enzymes responsible for trypanothione biosynthesis in Crithidia fasciculata
J. Biol. Chem.
273
19383-19390
1998
Crithidia fasciculata, Crithidia fasciculata (P90518)
Manually annotated by BRENDA team
De Craecker, S.; Verbruggen, C.; Rajan, P.; Smith, K.; Haemers, A.; Fairlamb, A.H.
Characterization of the peptide substrate specificity of glutathionylspermidine synthetase from Crithidia fasciculata
Mol. Biochem. Parasitol.
84
25-32
1997
Crithidia fasciculata
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
Oza, S.L.; Ariyanayagam, M.R.; Fairlamb, A.H.
Characterization of recombinant glutathionylspermidine synthetase/amidase from Crithidia fasciculata
Biochem. J.
364
679-686
2002
Crithidia fasciculata (P90518), Crithidia fasciculata
Manually annotated by BRENDA team
Amssoms, K.; Oza, S.L.; Augustyns, K.; Yamani, A.; Lambeir, A.M.; Bal, G.; Van der Veken, P.; Fairlamb, A.H.; Haemers, A.
Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 2: Substitution of the glycine part
Bioorg. Med. Chem. Lett.
12
2703-2705
2002
Crithidia fasciculata
Manually annotated by BRENDA team
Ariyanayagam, M.R.; Oza, S.L.; Guther, M.L.S.; Fairlamb, A.H.
Phenotypic analysis of trypanothione synthetase knockdown in the African trypanosome
Biochem. J.
391
425-432
2005
Trypanosoma brucei
Manually annotated by BRENDA team
Comini, M.A.; Guerrero, S.A.; Haile, S.; Menge, U.; Lunsdorf, H.; Flohe, L.
Valdiation of Trypanosoma brucei trypanothione synthetase as drug target
Free Radic. Biol. Med.
36
1289-1302
2004
Trypanosoma brucei
Manually annotated by BRENDA team
Comini, M.; Menge, U.; Wissing, J.; Flohe, L.
Trypanothione synthesis in Crithidia revisited
J. Biol. Chem.
280
6850-6860
2005
Crithidia fasciculata (P90518), Crithidia fasciculata (Q5DM89), Crithidia fasciculata
Manually annotated by BRENDA team
Oza, S.L.; Shaw, M.P.; Wyllie, S.; Fairlamb, A.H.
Trypanothione biosynthesis in Leishmania major
Mol. Biochem. Parasitol.
139
107-116
2005
Leishmania major (AJ748279), Leishmania major
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
Oza, S.L.; Chen, S.; Wyllie, S.; Coward, J.K.; Fairlamb, A.H.
ATP-dependent ligases in trypanothione biosynthesis - kinetics of catalysis and inhibition by phosphinic acid pseudopeptides
FEBS J.
275
5408-5421
2008
Crithidia fasciculata (P90518), Crithidia fasciculata
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
Chattopadhyay, M.K.; Chen, W.; Tabor, H.
Escherichia coli glutathionylspermidine synthetase/amidase: phylogeny and effect on regulation of gene expression
FEMS Microbiol. Lett.
338
132-140
2013
Escherichia coli K-12 (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
Sousa, A.F.; Gomes-Alves, A.G.; Benitez, D.; Comini, M.A.; Flohe, L.; Jaeger, T.; Passos, J.; Stuhlmann, F.; Tomas, A.M.; Castro, H.
Genetic and chemical analyses reveal that trypanothione synthetase but not glutathionylspermidine synthetase is essential for Leishmania infantum
Free Radic. Biol. Med.
73
229-238
2014
Leishmania infantum (A4I1T8), Leishmania infantum, Leishmania infantum MHOM / MA / 67 / ITMAP263 (A4I1T8)
Manually annotated by BRENDA team