Literature summary for 3.1.3.8 extracted from

Dionisio, G.; Brinch-Pedersen, H.; Welinder, K.G.; Jorgensen, M.
Different site-specific N-glycan types in wheat (Triticum aestivum L.) PAP phytase (2011), Phytochemistry, 72, 1173-1179.

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Organism

Organism	UniProt	Comment	Textmining
Triticum aestivum	C4PKK7	isozyme a1	-
Triticum aestivum	C4PKK8	isozyme a2	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	seven N-linked glycosylation sites, three of these sites are dominated by variant forms of the XylMan3FucGlcNAc2, i.e. the HRP-type of glycan. Complex-type glycans with one or two additional GlcNAc occur, but in trace amounts only. At four sites, the glycan consisted of a single GlcNAc residue, mass spectrometric isozyme glycan analysis, overview	Triticum aestivum
glycoprotein	seven N-linked glycosylation sites, three of these sites are dominated by variant forms of the XylMan3FucGlcNAc2, i.e. the HRP-type of glycan. Complex-type glycans with one or two additional GlcNAc occur, but in trace amounts only. At four sites, the glycan consists of a single GlcNAc residue, mass spectrometric isozyme glycan analysis, overview	Triticum aestivum

Synonyms

Synonyms	Comment	Organism
PAPhy	-	Triticum aestivum
purple acid phosphatase	-	Triticum aestivum

General Information

General Information	Comment	Organism
physiological function	phytase activity in grain is essential to make phosphate available to cell metabolism, and in food and feed	Triticum aestivum

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Release 2023.1 (January 2023)