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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

Engineering

Engineering on EC 3.4.21.61 - Kexin

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A433T
is associated with a plasma PCSK9 concentration of 222 ng/ml
A443T
-
is expressed, processed, and secreted normally, and reduces cellular LDL uptake in a concentration-dependent like the wild-type
C678X
a loss-of-function mutation that abolishes the release of the enzyme from the endoplasmic reticulum
D374Y
DeltaN218
-
in COS-1 cells only apparent upon co-expression of PC5A. Untreated Y1 cells secrete PCSK9-DeltaN218, stimulation with 8-Br-cAMP increases the level and especially that of the 34-kDa PCSK9 product
E569K
site-directed mutagenesis, the mutant shows slightly decreased ability to block LDL uptake into HepG2 cells compared to the wild-type enzyme
E607A/K609A/E612N
mutation does not affect the overall integrity of the PCSK9 protein, shows similar cellular uptake potencies as the wild-type, impairs 1G08-PCSK9 binding
F216L
G365R
is associated with a plasma PCSK9 concentration of 205 ng/ml
G517R
site-directed mutagenesis, the mutant shows highly decreased ability to block LDL uptake into HepG2 cells compared to the wild-type enzyme
N425S
-
is expressed, processed, and secreted normally, and reduces cellular LDL uptake in a concentration-dependent like the wild-type
Q152H
a dominant negative mutation that restricts enzyme proteolysis and secretion independently
Q152I
te mutation completely abrogates proteolysis in both intra- and intermolecular systems but has only a limited impact on secretion
Q152R
the mutation completely abolished both proteolysis and secretion
Q152X
four phenotypes of Q152X mutants, overview
Q190R
is associated with a plasma PCSK9 concentration of 55 ng/ml
R215H
a naturally occurring gain-of-function mutation associated with hypercholesterolemia, the mutation impairs furin-mediated enzyme cleavage
R218S
R434W
is associated with a plasma PCSK9 concentration of 51 ng/ml
R469W
-
natural mutation, cannot modify the ability of PC5A to produce the 34-kDa PCSK9 product in HEK293 cells
R46L
is associated with a plasma PCSK9 concentration of 51-59 ng/ml
R496W
-
natural mutation, cannot modify the ability of PC5A to produce the 34-kDa PCSK9 product in HEK293 cells
R53V
is associated with a plasma PCSK9 concentration of 39 ng/ml
R549A
mutation does not affect the overall integrity of the PCSK9 protein, shows similar cellular uptake potencies as the wild-type, impairs 1G08-PCSK9 binding
R580A/R582A
mutation does not affect the overall integrity of the PCSK9 protein, shows similar cellular uptake potencies as the wild-type, impairs 1G08-PCSK9 binding
R659A
site-directed mutagenesis, the mutant shows slightly decreased ability to block LDL uptake into HepG2 cells compared to the wild-type enzyme
R659E
site-directed mutagenesis, the mutant shows slightly decreased ability to block LDL uptake into HepG2 cells compared to the wild-type enzyme
S127R
S386A
S462P
a loss-of-function mutation that abolishes the release of the enzyme from the endoplasmic reticulum
S636R
site-directed mutagenesis, the mutant shows slightly decreased ability to block LDL uptake into HepG2 cells compared to the wild-type enzyme
V149A
the mutant shows intolerance for intermolecular cleavage of the enzyme, residue Val149 is critical for secretion
V610R
site-directed mutagenesis, the mutant shows highly decreased ability to block LDL uptake into HepG2 cells compared to the wild-type enzyme
V644R
site-directed mutagenesis, the mutant shows highly decreased ability to block LDL uptake into HepG2 cells compared to the wild-type enzyme
C678X
a loss-of-function mutation that abolishes the release of the enzyme from the endoplasmic reticulum
N146A
-
mutation results in the decreased zymogen activation of proPC1/3 and virtually inhibits its secretion
N374A
-
mutant is processed and secreted at nearly the same rate and with the same apparent molecular mass as wild-type. Residue N374 does not appear to bear an N-glycan
N618A
-
mutation does not significantly affect zymogen activation
S462P
a loss-of-function mutation that abolishes the release of the enzyme from the endoplasmic reticulum
D176G/D210A/D211S
-
no preference for positively charged residues at P2 position, and S2 pocket is more solvent accessible, leading to preference for MR- over LR- or FR-containing substrates
E255I
-
significantly decreased recognition of P4Arg residue in a tetrapeptide substrate
T252D
-
increased recognition of Arg in P4 position, 14fold higher kcat/KM ratio for Arg than for Ala at position P6
T252D/Q283E
-
increased recognition of Arg in P4 position, 15fold higher kcat/KM ratio for Arg than for Ala at position P6
additional information