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
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3.4.21.61
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cholesterol
-
lipoprotein
-
cardiovascular
-
low-density
-
statin
-
hypercholesterolemia
-
coronary
-
lipid-lowering
-
atherosclerotic
-
ezetimibe
-
evolocumab
-
alirocumab
-
furin
-
artery
-
apolipoprotein
-
triglyceride
-
ldl-cholesterol
-
dyslipidemias
-
myocardial
-
placebo
-
stroke
-
high-risk
-
ascvd
-
infarction
-
atherogenic
-
hyperlipidemia
-
atorvastatin
-
cholesterol-lowering
-
intolerance
-
lipoprotein-cholesterol
-
hdl
-
cardiology
-
apheresis
-
diagnostics
-
non-high-density
-
ldl-receptors
-
angiopoietin-like
-
proinsulin
-
proopiomelanocortin
-
treatment-emergent
-
srebp-2
-
endoproteolytic
-
guideline-recommended
-
triglyceride-rich
-
drug development
-
prodomain
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endoproteases
-
degradation
-
non-hdl-c
-
fibrates
-
xanthoma
-
statin-treated
-
molecular biology
-
medicine
-
niacin
- 3.4.21.61
- cholesterol
- lipoprotein
- cardiovascular
-
low-density
- statin
- hypercholesterolemia
- coronary
-
lipid-lowering
- atherosclerotic
- ezetimibe
-
evolocumab
-
alirocumab
- furin
- artery
-
apolipoprotein
- triglyceride
-
ldl-cholesterol
- dyslipidemias
- myocardial
-
placebo
- stroke
-
high-risk
-
ascvd
- infarction
-
atherogenic
- hyperlipidemia
- atorvastatin
-
cholesterol-lowering
- intolerance
-
lipoprotein-cholesterol
- hdl
-
cardiology
-
apheresis
- diagnostics
-
non-high-density
-
ldl-receptors
-
angiopoietin-like
- proinsulin
- proopiomelanocortin
-
treatment-emergent
- srebp-2
-
endoproteolytic
-
guideline-recommended
-
triglyceride-rich
- drug development
- prodomain
- endoproteases
- degradation
-
non-hdl-c
-
fibrates
- xanthoma
-
statin-treated
- molecular biology
- medicine
- niacin
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
3.4.21.61 KexinAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.21.61 - Kexin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ac-(beta-cyclohexyl)alanineYKK 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-(beta-cyclohexyl)alanineYKK
-
-
-
?
Ac-Ala-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + ?
-
-
-
?
Ac-Ala-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + ?
-
-
-
?
Ac-alpha-aminobutyric acid-YKK 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-alpha-aminobutyric acid-YKK
-
-
-
?
Ac-Arg-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-Arg-Tyr-Lys-Lys
-
-
-
?
Ac-AYKK 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-AYKK
-
-
-
?
Ac-AYKR 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-AYKR
-
-
-
?
Ac-Cit-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-Cit-Tyr-Lys-Lys 4-methylcoumarin
-
this substrate is cleaved poorly
-
?
Ac-CYKK 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-CYKK
-
-
-
?
Ac-FYKK 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-FYKK
-
-
-
?
Ac-Nle-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-Nle-Tyr-Lys-Arg-COOH
Ac-Nle-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + ?
-
-
-
?
Ac-Nle-YKK 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-Nle-YKK
-
-
-
?
Ac-Nle-YKR 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + ?
-
-
-
?
Ac-Nle-YKR 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-Nle-YKR
-
-
-
?
Ac-norvaline-YKK 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-norvaline-YKK
-
-
-
?
Ac-Pro-Met-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + ?
-
-
-
?
Ac-Pro-Met-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-Pro-Met-Tyr-Lys-Arg
-
-
-
?
Ac-RYKK 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-RYKK
-
-
-
?
Ac-VYKK 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-VYKK
-
-
-
?
Arg-Lys(DABCYL)-Nle-Tyr-Lys-Arg-Glu-Ala-Glu-Ala-Glu(EDANS)-Arg + H2O
Arg-Lys(DABCYL)-Nle-Tyr-Lys-Arg + Glu-Ala-Glu-Ala-Glu(EDANS)-Arg
-
-
-
?
Arg-Lys(DABCYL)-Nle-Tyr-Lys-Lys-Glu-Ala-Glu-Ala-Glu(EDANS)-Arg + H2O
Arg-Lys(DABCYL)-Nle-Tyr-Lys-Lys + Glu-Ala-Glu-Ala-Glu(EDANS)-Arg
-
-
-
?
benzyloxycarbonyl-Ala-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + benzyloxycarbonyl-Ala-Tyr-Lys-Lys
-
-
-
?
benzyloxycarbonyl-Nle-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O
?
-
-
-
?
benzyloxycarbonyl-Nle-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Cbz-Nle-Tyr-Lys-Lys
-
-
-
?
benzyloxycarbonyl-Nle-YKR 4-methylcoumarin 7-amide + H2O
?
-
-
-
?
CLC chloride channel + H2O
proteolytically processed CLC chloride channel
-
cleavage in first intracellular loop at residues K136/R137
-
-
?
D-Ac-Nle-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O
?
-
-
-
?
L-pyroglutamyl-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
L-pyroglutamyl-Arg-Thr-Lys-Arg + 7-amino-4-methyl-coumarin
-
-
-
-
?
low-density lipoprotein receptor
?
PCSK9 posttranslationally promotes the degradation of the low-density lipoprotein receptor
-
-
?
N-tert-butyloxycarbonyl-Gly-Lys-Arg 4-methylcoumarin 7-amide + H2O
N-tert-butyloxycarbonyl-Gly-Lys-Arg + 7-amino-4-methylcoumarin
-
59.2% of the activity with tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
7-amino-4-methylcoumarin
-
-
-
-
?
prekallikrein
?
-
cleaved into four fragments by ASP, protein cleaved at specific sequences
-
-
?
Proinsulin + H2O
Insulin + ?
-
cleaves human proinsulin at the peptide bond between Arg32 and Glu33
-
?
proopiomelanocortin + H2O
beta-lipotropic hormone + adrenocorticotropic hormone + ?
-
-
-
-
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methyl-coumarin
-
-
-
-
?
t-butyloxycarbonyl-EKK 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + t-butyloxycarbonyl-EKK
-
-
-
?
t-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methyl-coumarin
-
best substrate
-
-
?
t-butyloxycarbonyl-Gly-Lys-Arg-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-Gly-Lys-Arg + 7-amino-4-methyl-coumarin
-
-
-
-
?
t-butyloxycarbonyl-QGR 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + t-butyloxycarbonyl-QGR
-
-
-
?
tert-Butyloxycarbonyl-Ala-Pro-Arg 4-methylcoumarin 7-amide + H2O
?
-
17% of the activity with tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide
-
-
?
tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide + H2O
tert-butyloxycarbonyl-Gln-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-Butyloxycarbonyl-Leu-Arg-Arg 4-methylcoumarin 7-amide + H2O
?
-
116% of the activity with tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide
-
-
?
tert-Butyloxycarbonyl-Leu-Lys-Arg 4-methylcoumarin 7-amide + H2O
?
-
92.8% of the activity with tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide
-
-
?
tert-Butyloxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide + H2O
?
-
38% of the activity with tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide
-
-
?
Ac-Nle-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-Nle-Tyr-Lys-Arg-COOH
-
-
-
?
Ac-Nle-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + Ac-Nle-Tyr-Lys-Arg-COOH
-
-
-
?
low density lipoprotein receptor + H2O
?
-
C-terminal domain of enzyme has a stronger affinity for substrate low density lipoprotein receptor than catalytic domain. A C-terminal deletion mutant does not mediate low density lipoprotein receptor degradation
-
-
?
low density lipoprotein receptor + H2O
?
-
PCSK9 binding to cell surface low density lipoprotein receptor cannot be described by a simple bimolecular reaction. Data suggest the presence of two populations of binding site
-
-
?
low density lipoprotein receptor + H2O
?
-
a discrete C-terminal protein fragment competes with full-length PCSK9 for binding to LDLR in vitro and attenuates PCSK9-mediated hypercholesterolemia in mice
-
-
?
low density lipoprotein receptor-related protein 1 + H2O
?
-
degradation
-
-
?
low density lipoprotein receptor-related protein 1 + H2O
?
-
the enzyme acts on the extracellular domain of the receptor molecule
-
-
?
low density lipoprotein receptor-related protein 1 + H2O
?
degradation
-
-
?
low density lipoprotein receptor-related protein 1 + H2O
?
-
the enzyme acts on the extracellular domain of the receptor molecule
-
-
?
low density lipoprotein receptor-related protein 1 + H2O
?
degradation
-
-
?
low density lipoprotein receptor-related protein 1 + H2O
?
the enzyme acts on the extracellular domain of the receptor molecule
-
-
?
Precursor protein of the mating hormone alpha-factor of Saccharomyces cerevisiae + H2O
?
-
processing
-
-
?
Precursor protein of the mating hormone alpha-factor of Saccharomyces cerevisiae + H2O
?
-
processing
-
-
?
pro-alpha-mating factor + H2O
alpha-mating factor + ?
-
-
-
?
pro-alpha-mating factor + H2O
alpha-mating factor + ?
-
-
-
?
pro-alpha-mating factor + H2O
alpha-mating factor + ?
-
mating pheromone precursor, physiological substrate
-
?
Protein + H2O
?
-
specificity: preference for Lys-Arg, while Arg-Arg, Pro-Arg, Ala-Arg, and Thr-Arg are equally rapidly cleaved but with higher Km
-
-
?
Protein + H2O
?
-
autocatalytic activation at an internal Lys108-Arg109
-
-
?
Protein + H2O
?
-
precursor protein of the mating hormone alpha-factor of Saccharomyces cerevisiae
-
-
?
Protein + H2O
?
-
specificity towards the carbonyl side of Lys-Arg, Arg-Arg and Pro-Arg sequences
-
-
?
Protein + H2O
?
-
cleaves a wide variety of precursors from higher eukaryotes including prohormones, such as proinsulin and proopiomelanocortin, as well as precursors of constitutively secreteted proteins, such as proalbumin
-
-
?
additional information
?
-
-
FRETS-25Xaa libraries as substrates. Best FRETS contains Lys at position Xaa (FRETS-25K). No cleavage of succinyl-Ala-Ala-Pro-Phe-4-methylylcoumaryl-7-amide, t-butyloxycarbonyl-Gly-Arg-Arg-4-methylylcoumaryl-7-amide, Z-His-Glu-Lys-4-methylylcoumaryl-7-amide, and t-butyloxycarbonyl-Phe-Ser-Arg-4-methylylcoumaryl-7-amide
-
-
?
additional information
?
-
both furinand hepsin-cleaved enzymes are able to degrade LDL receptor on HepG2 cells resulting in elevated serum cholesterol levels
-
-
?
additional information
?
-
the enzyme catalytic domain is capable of proteolysis in trans (i.e. as two separate polypeptides), and can perform intermolecular proteolysis
-
-
?
additional information
?
-
-
CT-peptide is not cleaved by enzymatically active PC1/3
-
-
?
additional information
?
-
-
a variety of trypsin substrates containing only one basic amino acid
-
-
?
additional information
?
-
-
cleaves peptide substrates at both Lys-Arg and Arg-Arg sites, not: benzyloxycarbonyl-Lys-Arg 4-nitroanilide, benzyloxycarbonyl-Arg-Arg 4-nitroanilide
-
-
?
additional information
?
-
-
exhibits optimal activity toward substrates with Lys or Arg at P2 and Arg at P1, also recognizes P4, with dual specificity for aliphatic and basic residues
-
?
additional information
?
-
-
generates peptide hormone by specific processing of propeptides
-
?
additional information
?
-
-
hydrolyzes peptides and proteins with basic amino acid pairs which are cleaved at the C-ends of their peptide bonds, cleaves specifically large recombinant proteins, for example a protein consisting of a gamma-interferon fragment linked to HIV1-proteinase via a Lys-Arg-containing peptide
-
?
additional information
?
-
-
carries out specific endoproteolytic cleavage of proprotein and prohormone precursors in the secretory pathway, hydrolyzes ester and amide substrates
-
?
additional information
?
-
-
transforming the precursors of biologically active agents into their functional forms, processing and conversion of prohormones
-
?
additional information
?
-
-
wild-type, preference for positively charged residues at P2 position. Mutant D176G/D210A/D211S, preference for MR- over LR- or FR-containing substrates, which cannot be cleaved by wild-type
-
-
?
additional information
?
-
-
a variety of trypsin substrates containing only one basic amino acid
-
-
?
additional information
?
-
-
cleaves peptide substrates at both Lys-Arg and Arg-Arg sites, not: benzyloxycarbonyl-Lys-Arg 4-nitroanilide, benzyloxycarbonyl-Arg-Arg 4-nitroanilide
-
-
?
