Literature summary for 2.5.1.47 extracted from

Fyfe, P.K.; Westrop, G.D.; Ramos, T.; Mueller, S.; Coombs, G.H.; Hunter, W.N.
Structure of Leishmania major cysteine synthase (2012), Acta Crystallogr. Sect. F, 68, 738-743.

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.8 A resolution. The biologically active unit, a dimer, constitutes the asymmetric unit. Subunit A contains residues 3-213 and 241-333, whilst subunit B comprises residues 4-214 and 241-333. A surface loop from residues 214 to 241 is disordered. The subunit contains two domains. The smaller domain I is constructed by residues 51-158, which primarily form a four-stranded beta-sheet surrounded by four alpha-helices. The larger domain II comprises residues 21-50 and 159-306. Domain II contains four alpha-helices and six beta-strands which, together with a beta-strand contributed from the partner-subunit domain I, form a seven-membered beta-sheet. In addition, residues 307-333 at the C-terminus form an extended helix-loop-helix structure that stretches across the surface of the partner subunit	Leishmania major

Crystallization (Comment)

Organism

to 1.8 A resolution. The biologically active unit, a dimer, constitutes the asymmetric unit. Subunit A contains residues 3-213 and 241-333, whilst subunit B comprises residues 4-214 and 241-333. A surface loop from residues 214 to 241 is disordered. The subunit contains two domains. The smaller domain I is constructed by residues 51-158, which primarily form a four-stranded beta-sheet surrounded by four alpha-helices. The larger domain II comprises residues 21-50 and 159-306. Domain II contains four alpha-helices and six beta-strands which, together with a beta-strand contributed from the partner-subunit domain I, form a seven-membered beta-sheet. In addition, residues 307-333 at the C-terminus form an extended helix-loop-helix structure that stretches across the surface of the partner subunit

Leishmania major

Inhibitors

Inhibitors	Comment	Organism	Structure
DYVI	a peptide based on the C-terminus of the partner serine acetyltransferase with which the enzyme forms a complex, competitive inhibition	Leishmania major

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
35600	-	x * 35600, calculated	Leishmania major

Organism

Organism	UniProt	Comment	Textmining
Leishmania major	-	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
180	-	pH 7.8, 22°C	Leishmania major

Subunits

Subunits	Comment	Organism
?	x * 35600, calculated	Leishmania major

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	residue K51 forms a Schiff base with pyridoxal 5'-phosphate, with conserved residues N82 and S274 forming hydrogen bonds to the cofactor. Further residues predicted to orient and hold the pyridoxal 5'-phosphate in position are G186, T182, G183 and T185	Leishmania major

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.004	-	DYVI	pH 7.8, 22°C	Leishmania major