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Literature summary for 3.4.21.61 extracted from

  • Wheatley, J.L.; Holyoak, T.
    Differential P1 arginine and lysine recognition in the prototypical proprotein convertase Kex2 (2007), Proc. Natl. Acad. Sci. USA, 104, 6626-6631.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
Kex2 in complex with the Ac-R-E-R-K-chloromethylketone, containing a noncognate lysine at the P1 position. Secondary subsite in the S1 pocket is present, which recognizes and binds the P1 lysine in a more shallow fashion than arginine. Kex2 contains well defined subsites that have optimally arranged electrostatic charge that positions correct substrates for hydrolysis. Chemical nature of the peptidyl inhibitor has little effect on ligand positioning at the active site in the alkylated enzyme forms Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
Ac-R-E-R-K-chloromethylketone alternate binding site and resultant displacement of the scissile bond in the active site results in a decrease in the acylation rate Saccharomyces cerevisiae
decanoyl-R-V-K-R-chloromethylketone
-
 Saccharomyces cerevisiae
decanoyl-R-V-R-K-chloromethylketone
-
 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Kex2
-
 Saccharomyces cerevisiae
kexin
-
 Saccharomyces cerevisiae
proprotein convertase Kex2
-
 Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00019
-
 decanoyl-R-V-K-R-chloromethylketone
-
 Saccharomyces cerevisiae
0.00845
-
 decanoyl-R-V-R-K-chloromethylketone
-
 Saccharomyces cerevisiae