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Literature summary for 3.4.21.B4 extracted from

  • Bovenschen, N.; Quadir, R.; van den Berg, A.L.; Brenkman, A.B.; Vandenberghe, I.; Devreese, B.; Joore, J.; Kummer, J.A.
    Granzyme K displays highly restricted substrate specificity that only partially overlaps with granzyme A (2009), J. Biol. Chem., 284, 3504-3512.
    View publication on PubMed
Search for more literature for 3.4.21.B4

Cloned(Commentary)

Cloned (Comment) Organism
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 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P49863
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
actin + H2O
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 Homo sapiens ?
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 ?
beta-tubulin + H2O cleaves beta-tubulin after Arg62 (YVPR-/-AV) and Arg282 (QQYR-/-AL) Homo sapiens ?
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 ?
endoplasmic reticulum-associated SET complex + H2O
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 Homo sapiens ?
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 ?
heterogeneous nuclear ribonucleoprotein K + H2O granzyme K and granzyme A cleave with different kinetics at distinct sites Homo sapiens ?
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 ?
additional information granzyme K prefers Arg over Lys at P1 position. Granzyme K and granzyme A display highly restricted substrate specificities that overlapp only partially. Whereas granzyme K and granzyme A cleave SET with similar efficiencies likely at the same sites, both granzymes cleave the pre-mRNA-binding protein heterogeneous ribonuclear protein K with different kinetics at distinct sites. Granzyme K is markedly more efficient in cleaving heterogeneous ribonuclear protein K than granzyme A. Granzyme K, but not granzyme A, cleaves the microtubule network protein beta-tubulin after two distinct Arg residues. Neither GrK cleavage sites in beta-tubulin nor a peptide based proteomic screen reveal a clear granzyme K consensus sequence around the P1 residue, suggesting that GrK specificity depends on electrostatic interactions between exosites of the substrate and the enzyme Homo sapiens ?
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 ?

Synonyms

Synonyms Comment Organism
GRK
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 Homo sapiens