Literature summary for 2.5.1.65 extracted from

Mino, K.; Oda, Y.; Ataka, M.; Ishikawa, K.
Crystallization and preliminary X-ray diffraction analysis of O-acetylserine sulfhydrylase from Aeropyrum pernix K1 (2003), Acta Crystallogr. Sect. D, 59, 338-340.

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli	Aeropyrum pernix
overexpression in Escherichia coli Rosetta (DE3)	Aeropyrum pernix

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapor-diffusion method	Aeropyrum pernix
purified recombinant enzyme, optimization of crystallization method, hanging drop vapour diffusion method, enzyme in 50 mM potassium phosphate buffer pH 7.5, containing 0.2 mM pyridoxal 5'-phosphate and 0.05% sodium azide, 0.0015 ml of enzyme and reservoir solution, containing 0.1 M sodium cacodylate pH 7.4, 0.1 M sodium acetate and 30% v/v PEG 8000, are equilibrated against 0.5 ml of reservoir solution at 295°C, 2 weeks, cryoprotection by 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution	Aeropyrum pernix

Crystallization (Comment)

Organism

hanging-drop vapor-diffusion method

Aeropyrum pernix

purified recombinant enzyme, optimization of crystallization method, hanging drop vapour diffusion method, enzyme in 50 mM potassium phosphate buffer pH 7.5, containing 0.2 mM pyridoxal 5'-phosphate and 0.05% sodium azide, 0.0015 ml of enzyme and reservoir solution, containing 0.1 M sodium cacodylate pH 7.4, 0.1 M sodium acetate and 30% v/v PEG 8000, are equilibrated against 0.5 ml of reservoir solution at 295°C, 2 weeks, cryoprotection by 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution

Aeropyrum pernix

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
additional information	Aeropyrum pernix	L-cysteine biosynthesis	?	-	?
O-acetyl-L-serine + hydrogen sulfide	Aeropyrum pernix	-	L-cysteine + acetate	-	?
O-phospho-L-serine + hydrogen sulfide	Aeropyrum pernix	-	L-cysteine + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Aeropyrum pernix	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli	Aeropyrum pernix
recombinant OASS	Aeropyrum pernix

Reaction

Reaction	Comment	Organism	Reaction ID
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate	a pyridoxal-phosphate protein, the enzyme from Aeropyrum pernix acts on both O-phospho-L-serine and O3-acetyl-L-serine, in contrast with EC 2.5.1.47, cysteine synthase, which acts only on O3-acetyl-L-serine	Aeropyrum pernix	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	L-cysteine biosynthesis	Aeropyrum pernix	?	-	?
O-acetyl-L-serine + hydrogen sulfide	-	Aeropyrum pernix	L-cysteine + acetate	-	?
O-acetyl-L-serine + sulfide	-	Aeropyrum pernix	L-cysteine + acetic acid	-	?
O-phospho-L-serine + hydrogen sulfide	-	Aeropyrum pernix	L-cysteine + phosphate	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Aeropyrum pernix

Synonyms

Synonyms	Comment	Organism
APE1586	Aeropyrum pernix K1, open reading frame	Aeropyrum pernix
O-acetyl-L-serine sulfhydrylase	-	Aeropyrum pernix
O-acetylserine sulfhydrylase	-	Aeropyrum pernix
O-phosphoserine(thiol)-lyase	-	Aeropyrum pernix
OASS	-	Aeropyrum pernix

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	required	Aeropyrum pernix