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Literature summary for 3.1.3.3 extracted from

  • Peeraer, Y.; Rabijns, A.; Verboven, C.; Collet, J.F.; Van Schaftingen, E.; De Ranter, C.
    High-resolution structure of human phosphoserine phosphatase in open conformation (2003), Acta Crystallogr. Sect. D, 59, 971-977.
    View publication on PubMed
Search for more literature for 3.1.3.3

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour-diffusion method. A resolution of 1.53 A provides a detailed model of the active site in a completely open conformation and the water molecules bound to it Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-O-phosphoserine + H2O Homo sapiens enzyme is responsible for the third and final step of the L-serine biosynthetic pathway L-serine + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-O-phosphoserine + H2O
-
 Homo sapiens L-serine + phosphate
-
 ?
L-O-phosphoserine + H2O enzyme is responsible for the third and final step of the L-serine biosynthetic pathway Homo sapiens L-serine + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
HPSP
-
 Homo sapiens