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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.78 hanging gamma-drop vapor diffusion method, structure of Leishmania major trypanothione synthetase-amidase, determined in three crystal forms, reveals two catalytic domains Leishmania major
6.3.1.9 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
6.3.1.9 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

EC Number General Stability Organism
6.3.1.9 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.1.9 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 ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.78 Leishmania major
-
-
-
6.3.1.9 Leishmania major Q711P7
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.78 trypanothione + H2O
-
 Leishmania major glutathione + glutathionylspermidine
-
 ?
6.3.1.9 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 ?
-
 ?
6.3.1.9 additional information structure modelling of substrate binding to the active site, overview Leishmania major ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.1.9 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

EC Number Synonyms Comment Organism
3.5.1.78 trypanothione synthetase-amidase bifunctional Leishmania major
6.3.1.9 trypanothione synthetase-amidase
-
 Leishmania major
6.3.1.9 trypanothione synthetase-amidase bifunctional Leishmania major
6.3.1.9 TSA
-
 Leishmania major