Literature summary for 3.4.21.76 extracted from

Budnjo, A.; Narawane, S.; Grauffel, C.; Schillinger, A.S.; Fossen, T.; Reuter, N.; Haug, B.E.
Reversible ketomethylene-based inhibitors of human neutrophil proteinase 3 (2014), J. Med. Chem., 57, 9396-9408.

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Inhibitors

Inhibitors	Comment	Organism	Structure
Abz-VADnV[PSI](COCH2)ADYQ-EDDnp	best inhibitor, selective for proteinase 3, displays a competitive and reversible inhibition mechanism	Homo sapiens
additional information	design of ketomethylene-based enzyme inhibitors that show low micromolar IC50 values. Molecular dynamics simulations show that the interactions between enzyme and ketomethylene-containing inhibitors are similar to those with the corresponding substrates. N- and C-terminal FRET groups are important for securing high inhibitory potency toward the enzyme	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P24158	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
neutrophil	-	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
neutrophil proteinase 3	-	Homo sapiens
PR3	-	Homo sapiens
proteinase 3	-	Homo sapiens

General Information

General Information	Comment	Organism
evolution	neutrophil serine proteases, proteinase 3 and human neutrophil elastase, share high sequence similarity, but have different substrate specificities and functions	Homo sapiens
metabolism	the enzyme is a target for chronic inflammatory diseases	Homo sapiens

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Release 2023.1 (January 2023)