Literature summary for 3.1.3.2 extracted from

Strater, N.; Jasper, B.; Scholte, M.; Krebs, B.; Duff, A.P.; Langley, D.B.; Han, R.; Averill, B.A.; Freeman, H.C.; Guss, J.M.
Crystal structures of recombinant human purple acid phosphatase with and without an inhibitory conformation of the repression loop (2005), J. Mol. Biol., 351, 233-246.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli and Pichia pastoris	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
recombinant enzyme expressed in Escherichia coli and Pichia pastoris, the enzyme is in its oxidized, inactive state with both iron ions at the active site are Fe3+, X-ray diffraction structure determination and analysis at 2.2 A resolution	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	the repression loop involved in iron binding has an inhibitory function	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	the 22 iron ions bound at the active site are Fe2+ in the active enzyme state, and Fe3+ in the inactive state influencing the conformation of the repression loop, binding and structure overview	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P13686	-	-

Synonyms

Synonyms	Comment	Organism
PAP	-	Homo sapiens
purple acid phosphatase	-	Homo sapiens

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Release 2023.1 (January 2023)