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Literature summary for 2.6.1.51 extracted from

  • Sayer, C.; Bommer, M.; Isupov, M.; Ward, J.; Littlechild, J.
    Crystal structure and substrate specificity of the thermophilic serine:pyruvate aminotransferase from Sulfolobus solfataricus (2012), Acta Crystallogr. Sect. D, 68, 763-772.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Saccharolobus solfataricus

Crystallization (Commentary)

Crystallization (Comment) Organism
1.8 A resolution. The structure of the Sulfolobus solfataricus enzyme is determined with an amino form of the cofactor pyridoxamine 5'-phosphate bound in the active site and in complex with gabaculine, an aminotransferase inhibitor. These structures show the changes in the enzyme active site during the course of the catalytic reaction Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97VM5
-
-
Saccharolobus solfataricus P2 Q97VM5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine + pyruvate
-
Saccharolobus solfataricus 3-hydroxypyruvate + L-alanine
-
?
L-serine + pyruvate
-
Saccharolobus solfataricus P2 3-hydroxypyruvate + L-alanine
-
?

Subunits

Subunits Comment Organism
homodimer
-
Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
serine:pyruvate aminotransferase
-
Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
assay at Saccharolobus solfataricus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate the structure of the protein is a homodimer that adopts the type I fold of pyridoxal 5'-phosphate-dependent aminotransferases. The structure reveals the PLP cofactor covalently bound in the active site to the active-site lysine in the internal aldimine form Saccharolobus solfataricus