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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.47
-
 Aeropyrum pernix
2.5.1.65
-
 Aeropyrum pernix

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.47 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
2.5.1.65 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

EC Number Protein Variants Comment Organism
2.5.1.47 K127A mutant is inactive for cysteine synthesis and does not form the alpha-aminoacrylate intermediate Aeropyrum pernix
2.5.1.47 Q224A 0.2% of wild-type activity Aeropyrum pernix
2.5.1.47 R297A 61% of wild-type activity Aeropyrum pernix
2.5.1.47 R297E 52% of wild-type activity Aeropyrum pernix
2.5.1.47 R297K 48% of wild-type activity Aeropyrum pernix
2.5.1.47 S153A 117% of wild-type activity Aeropyrum pernix
2.5.1.47 S153T 8% of wild-type activity Aeropyrum pernix
2.5.1.47 T152A 2% of wild-type activity Aeropyrum pernix
2.5.1.47 T152S 93% of wild-type activity Aeropyrum pernix
2.5.1.47 T203A 41% of wild-type activity Aeropyrum pernix
2.5.1.47 T203M 20% of wild-type activity Aeropyrum pernix
2.5.1.65 K127A mutant is inactive for cysteine synthesis and does not form the alpha-aminoacrylate intermediate Aeropyrum pernix
2.5.1.65 Q224A 0.04% of wild-type activity Aeropyrum pernix
2.5.1.65 R297A 0.3% of wild-type activity Aeropyrum pernix
2.5.1.65 R297E 11% of wild-type activity Aeropyrum pernix
2.5.1.65 R297K 0.2% of wild-type activity Aeropyrum pernix
2.5.1.65 S153A 0.4% of wild-type activity Aeropyrum pernix
2.5.1.65 S153T 0.2% of wild-type activity Aeropyrum pernix
2.5.1.65 T152A 0.2% of wild-type activity Aeropyrum pernix
2.5.1.65 T152S 71% of wild-type activity Aeropyrum pernix
2.5.1.65 T203A 36% of wild-type activity Aeropyrum pernix
2.5.1.65 T203M 0.3% of wild-type activity Aeropyrum pernix

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.47 Aeropyrum pernix Q9YBL2
-
-
2.5.1.65 Aeropyrum pernix Q9YBL2
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5.1.47 46
-
 pH 7.5, 60°C Aeropyrum pernix
2.5.1.65 23
-
 pH 7.5, 80°C Aeropyrum pernix

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.47 additional information the enzyme also catalyzes the reaction of EC 2.5.1.65, O-phosphoserine hydrolase Aeropyrum pernix ?
-
 ?
2.5.1.47 O3-acetyl-L-serine + hydrogen sulfide
-
 Aeropyrum pernix L-cysteine + acetate
-
 ?
2.5.1.65 additional information the enzyme also catalyzes the reaction of EC 2.5.1.47, cysteine synthase Aeropyrum pernix ?
-
 ?
2.5.1.65 O-phospho-L-serine + hydrogen sulfide
-
 Aeropyrum pernix L-cysteine + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.47 OPSS
-
 Aeropyrum pernix
2.5.1.65 OPSS
-
 Aeropyrum pernix

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.47 pyridoxal 5'-phosphate crystallization data Aeropyrum pernix
2.5.1.65 pyridoxal 5'-phosphate crystallization data Aeropyrum pernix