Literature summary for 3.1.3.1 extracted from

Hoylaerts, M.F.; Ding, L.; Narisawa, S.; Van Kerckhoven, S.; Millan, J.L.
Mammalian alkaline phosphatase catalysis requires active site structure stabilization via the N-terminal amino acid microenvironment (2006), Biochemistry, 45, 9756-9766.

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Protein Variants

Protein Variants	Comment	Organism
additional information	deletion of five and nine N-terminal amino acis in TNAP reduced and abolished AP activity, respectively. The N-terminal amino acid deletions affects the rate of substrate catalysis (kcat), with a minor effect on the Michaelis constant	Homo sapiens
additional information	deletion of nine N-terminal amino acid residues in PLAP reducs its AP activity and heat stability, while deletion of 25 amino acids results in an inactive enzyme. The N-terminal amino acid deletions affect the rate of substrate catalysis (kcat), with a minor effect on the Michaelis constant	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P05187	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
placenta	-	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
PLAP	-	Homo sapiens
TNAP	-	Homo sapiens

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Release 2023.1 (January 2023)