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3.4.21.61: Kexin

This is an abbreviated version!
For detailed information about Kexin, go to the full flat file.

Word Map on EC 3.4.21.61

Reaction

Cleavage of -Lys-Arg-/- and -Arg-Arg-/- bonds to process yeast alpha-factor pheromone and killer toxin precursors =

Synonyms

adrenorphin-Gly-generating enzyme, ASP, BLI-4, corin activating enzyme, EC 3.4.22.23, endoproteinase Kex2p, Gene KEX2 dibasic proteinase, HuPCSK6, Kex 2p proteinase, Kex2, Kex2 endopeptidase, Kex2 endoprotease, Kex2 endoproteinase, Kex2 protease, Kex2 proteinase, Kex2-660, Kex2-like endoproteinase, Kex2-like precursor protein processing endoprotease, Kex2p, kexin, More, NARC-1, Paired-basic endopeptidase, PC 1/3, PC1, PC1/3, PC2, PCSK type 9, PCSK6, PCSK9, plasma proprotein convertase subtilisin-kexin type 9, pro-protein convertase subtilisin/kexin type 9, prohormone convertase 1, prohormone convertase 1/3, prohormone convertase 2, prohormone processing protease, Prohormone-processing endoprotease, Prohormone-processing KEX2 proteinase, Prohormone-processing proteinase, Proprotein convertase, proprotein convertase 1/3, proprotein convertase Kex2, proprotein convertase subtilisin kexin type 9, proprotein convertase subtilisin kexin-9, proprotein convertase subtilisin-like/kexin type 9, proprotein convertase subtilisin/kexin 6, proprotein convertase subtilisin/kexin type 6, proprotein convertase subtilisin/kexin type 9, proprotein convertase subtilisin/kexin type 9 (PCSK9)Proprotein convertase subtilisin/kexin type 9, proprotein processing protease, Protease KEX2, Proteinase Kex2p, Proteinase yscF, Proteinase, prohormone-processing, Yeast KEX2 protease

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.61 Kexin

Crystallization

Crystallization on EC 3.4.21.61 - Kexin

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized by hanging drop method, in complex with an Ala-Lys-Arg boronic acid inhibitor, space group P6(5)22, a = b = 113.8 A, c = 370.2 A
in complex with Ac-Arg-Glu-Lys-Arg-peptidyl boronic acid inhibitor
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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
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