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Literature summary for 3.4.21.79 extracted from

  • Giesuebel, U.; Daelken, B.; Mahmud, H.; Wels, W.S.
    Cell binding, internalization and cytotoxic activity of human granzyme B expressed in the yeast Pichia pastoris (2006), Biochem. J., 394, 563-573.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
S183A no catalytic activity Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.16
-
acetyl-IETD-p-nitroanilide recombinant enzyme, pH 7.4, 37°C Homo sapiens
7.38
-
acetyl-IETD-p-nitroanilide native enzyme, pH 7.4, 37°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm rapid uptake of external enzyme by HeLa cells and accumulation in cytoplasm in inactive form, uptake does not depend on enzyme activity or on mannose 6-phosphate receptor Homo sapiens 5737
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens after prolonged incubation, enzyme causes pronounced morphological changes in human tumor cells, leading to partial loss of contact to the culture support ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
expression in Pichia pastoris
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-IETD-p-nitroanilide + H2O
-
Homo sapiens ?
-
?
additional information after prolonged incubation, enzyme causes pronounced morphological changes in human tumor cells, leading to partial loss of contact to the culture support Homo sapiens ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.34
-
acetyl-IETD-p-nitroanilide native enzyme, pH 7.4, 37°C Homo sapiens
5.23
-
acetyl-IETD-p-nitroanilide recombinant enzyme, pH 7.4, 37°C Homo sapiens