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

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

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

Crystallization

Crystallization on EC 6.3.1.8 - glutathionylspermidine synthase

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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