Literature summary for 3.4.21.64 extracted from

Georgieva, D.; Rypniewski, W.; Echner, H.; Perbandt, M.; Koker, M.; Clos, J.; Redecke, L.; Bredehorst, R.; Voelter, W.; Genov, N.; Betzel, C.
Synthetic human prion protein octapeptide repeat binds to the proteinase K active site (2004), Biochem. Biophys. Res. Commun., 325, 1406-1411.

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Application

Application	Comment	Organism
medicine	segment GGG of functionally important N-terminal octapeptide region of human prion protein, involved in spongifirm encephalopathy, strongly binds as a substrate at the substrate recognition site	Parengyodontium album

Crystallization (Commentary)

Crystallization (Comment)	Organism
mercury-inhibited protein in presence of synthetic peptides GGGWGQPH and HGGGW, derived from N-terminal domain of human prion protein. Segment GGG is strongly bound as a substrate at the substrate recognition site	Parengyodontium album

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Parengyodontium album	segment GGG of human prion protein strongly binds as a substrate at the substrate recognition site	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Parengyodontium album	-	commercial preparation from Sigma-Aldrich	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	segment GGG of human prion protein strongly binds as a substrate at the substrate recognition site	Parengyodontium album	?	-	?

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Release 2023.1 (January 2023)