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Literature summary for 3.4.21.75 extracted from

  • Gawlik, K.; Shiryaev, S.A.; Zhu, W.; Motamedchaboki, K.; Desjardins, R.; Day, R.; Remacle, A.G.; Stec, B.; Strongin, A.Y.
    Autocatalytic activation of the furin zymogen requires removal of the emerging enzymes N-terminus from the active site (2009), PLoS ONE, 4, e5031.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.75

Cloned(Commentary)

Cloned (Comment) Organism
mutants expressed in Sf9 cells. Mutant constructs transiently transfected in LoVo cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
D153N is catalytically inert, is efficiently synthesized but inefficiently processed and secreted and therefore is difficult to be purified. Is incapable of self-activation, is less active than the wild-type Homo sapiens
D4K is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type Homo sapiens
G is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type Homo sapiens
G5 is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type Homo sapiens
G6 is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type Homo sapiens
H6 is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type Homo sapiens
K117P mutation does not affect the efficiency of autocatalytic processing and the resulting secretory mutants are capable of prodomain processing at the primary cleavage site Arg-Thr-Lys-Arg107-Asp108. Is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type Homo sapiens
K74G/R75G secondary cleavage sites are inactivated, is incapable of self-activation Homo sapiens
K74G/R75G/R107G is incapable of self-activation Homo sapiens
K74G/R75G/R89G is incapable of self-activation Homo sapiens
K74G/R75G/R89G/R107G is incapable of self-activation Homo sapiens
R107G primary cleavage sites are inactivated, is incapable of self-activation Homo sapiens
R89G efficiency of self-activation of the mutant in which the tertiary cleavage site (Arg-Leu-Gln-Arg89Q-Glu90) is inactivated, is significantly reduced compared to that of wild-type furin Homo sapiens
R89G/R107G is incapable of self-activation Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
decanoyl-Arg-Val-Lys-Arg-chloromethylketone fully blocks the substrate cleavage by the wild-type enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by metal-chelating chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Abz-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH + H2O
-
 Homo sapiens ?
-
 ?
anthrax protective antigen-83 + H2O
-
 Homo sapiens anthrax protective antigen-63 + ?
-
 ?
additional information a three-step autocatalytic processing including the cleavage of the prodomain at the Arg-Leu-Gln-Arg89Q-Glu90 site, is required for the efficient activation of furin Homo sapiens ?
-
 ?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
-
 Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
Proprotein convertase
-
 Homo sapiens