Literature summary for 6.3.1.9 extracted from

Fyfe, P.K.; Oza, S.L.; Fairlamb, A.H.; Hunter, W.N.
Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities (2008), J. Biol. Chem., 283, 17672-17680.

Crystallization (Commentary)

Crystallization (Comment)	Organism
determination of three crystal forms, 18°C, hanging drop vapor diffusion method, 0.001 ml of protein solution is mixed with 0.001 ml of reservoir solution, for crystal form I were optimized to a reservoir of 1.4 M (NH4)2SO4, 100 mM HEPES, pH 7.0, 200 mM NaBr, crystal form II to 1.6 M (NH4)2SO4, 100 mM HEPES, pH 7.0, and 200 mM NaBr, and crystal form III to 14% polyethylene glycol 8000, 15% glycerol and 100 mM KCl, within 2 days, X-ray diffraction structure determination and analysis at 2.3-3.6 A resolution, modelling	Leishmania major
hanging gamma-drop vapor diffusion method, structure of Leishmania major trypanothione synthetase-amidase, determined in three crystal forms, reveals two catalytic domains	Leishmania major

Crystallization (Comment)

Organism

determination of three crystal forms, 18°C, hanging drop vapor diffusion method, 0.001 ml of protein solution is mixed with 0.001 ml of reservoir solution, for crystal form I were optimized to a reservoir of 1.4 M (NH4)2SO4, 100 mM HEPES, pH 7.0, 200 mM NaBr, crystal form II to 1.6 M (NH4)2SO4, 100 mM HEPES, pH 7.0, and 200 mM NaBr, and crystal form III to 14% polyethylene glycol 8000, 15% glycerol and 100 mM KCl, within 2 days, X-ray diffraction structure determination and analysis at 2.3-3.6 A resolution, modelling

Leishmania major

hanging gamma-drop vapor diffusion method, structure of Leishmania major trypanothione synthetase-amidase, determined in three crystal forms, reveals two catalytic domains

Leishmania major

General Stability

General Stability	Organism
the C-terminal segment of the protein contributes to the amidase domain structure, and its loss likely destabilizes the fold	Leishmania major

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Leishmania major	the bifunctional trypanothione synthetase-amidase catalyzes biosynthesis and hydrolysis of the glutathione-spermidine adduct trypanothione, the principal intracellular thiolredox metabolite in parasitic trypanosomatids	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Leishmania major	Q711P7	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the bifunctional trypanothione synthetase-amidase catalyzes biosynthesis and hydrolysis of the glutathione-spermidine adduct trypanothione, the principal intracellular thiolredox metabolite in parasitic trypanosomatids	Leishmania major	?	-	?
additional information	structure modelling of substrate binding to the active site, overview	Leishmania major	?	-	?

Subunits

Subunits	Comment	Organism
More	secondary, tertiary, and domain structures, determined from three crystal forms, revealing two catalytic domains. The N-terminal domain, a cysteine, histidine-dependent amidohydrolase/peptidase amidase, is a papain-like cysteine protease, and the C-terminal synthetase domain displays an ATP-grasp family fold common to C:N ligases	Leishmania major

Synonyms

Synonyms	Comment	Organism
trypanothione synthetase-amidase	-	Leishmania major
trypanothione synthetase-amidase	bifunctional	Leishmania major
TSA	-	Leishmania major