Literature summary for 2.5.1.65 extracted from

Nakamura, T.; Kawai, Y.; Kunimoto, K.; Iwasaki, Y.; Nishii, K.; Kataoka, M.; Ishikawa, K.
Structural analysis of the substrate recognition mechanism in O-phosphoserine sulfhydrylase from the hyperthermophilic archaeon Aeropyrum pernix K1 (2012), J. Mol. Biol., 422, 33-44.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Aeropyrum pernix

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of the enzyme without acetate, the complex formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with O-phosphoserine, and the complex formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with O-acetylserine, to 2.1 A resolution. No significant difference is seen in the overall structure between the free and complexed forms of the enzyme. The side chains of T152, S153, and Q224 interact with the carboxylate of the substrate. The position of R297 is significantly unchanged in the complex of the K127A mutant with the external Schiff base, allowing enough space for an interaction with O-phosphoserine. The positively charged environment around the entrance of the active site including S153 and R297 is important for accepting negatively charged substrates	Aeropyrum pernix

Crystallization (Comment)

Organism

structures of the enzyme without acetate, the complex formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with O-phosphoserine, and the complex formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with O-acetylserine, to 2.1 A resolution. No significant difference is seen in the overall structure between the free and complexed forms of the enzyme. The side chains of T152, S153, and Q224 interact with the carboxylate of the substrate. The position of R297 is significantly unchanged in the complex of the K127A mutant with the external Schiff base, allowing enough space for an interaction with O-phosphoserine. The positively charged environment around the entrance of the active site including S153 and R297 is important for accepting negatively charged substrates

Aeropyrum pernix

Protein Variants

Protein Variants	Comment	Organism
K127A	mutant is inactive for cysteine synthesis and does not form the alpha-aminoacrylate intermediate	Aeropyrum pernix
Q224A	0.04% of wild-type activity	Aeropyrum pernix
R297A	0.3% of wild-type activity	Aeropyrum pernix
R297E	11% of wild-type activity	Aeropyrum pernix
R297K	0.2% of wild-type activity	Aeropyrum pernix
S153A	0.4% of wild-type activity	Aeropyrum pernix
S153T	0.2% of wild-type activity	Aeropyrum pernix
T152A	0.2% of wild-type activity	Aeropyrum pernix
T152S	71% of wild-type activity	Aeropyrum pernix
T203A	36% of wild-type activity	Aeropyrum pernix
T203M	0.3% of wild-type activity	Aeropyrum pernix

Organism

Organism	UniProt	Comment	Textmining
Aeropyrum pernix	Q9YBL2	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
23	-	pH 7.5, 80°C	Aeropyrum pernix

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme also catalyzes the reaction of EC 2.5.1.47, cysteine synthase	Aeropyrum pernix	?	-	?
O-phospho-L-serine + hydrogen sulfide	-	Aeropyrum pernix	L-cysteine + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
OPSS	-	Aeropyrum pernix

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	crystallization data	Aeropyrum pernix