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Information on EC 3.4.21.61 - Kexin and Organism(s) Saccharomyces cerevisiae and UniProt Accession P13134
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- 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
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pcsk9, proprotein convertase subtilisin/kexin type 9, proprotein convertase, pc1/3, kexin, kex2p, pcsk6, prohormone convertase 1, proprotein convertase subtilisin kexin type 9, prohormone convertase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adrenorphin-Gly-generating enzyme
-
-
-
-
endoproteinase Kex2p
-
-
-
-
Gene KEX2 dibasic proteinase
-
-
-
-
Kex 2p proteinase
-
-
-
-
Kex2 endopeptidase
-
-
-
-
Kex2 endoprotease
-
-
-
-
Kex2 endoproteinase
-
-
-
-
Kex2 protease
-
-
-
-
Kex2 proteinase
-
-
-
-
Kex2-like endoproteinase
-
-
-
-
Kex2-like precursor protein processing endoprotease
-
-
-
-
Paired-basic endopeptidase
-
-
-
-
Prohormone-processing endoprotease
-
-
-
-
Prohormone-processing KEX2 proteinase
-
-
-
-
Prohormone-processing proteinase
-
-
-
-
Proprotein convertase
-
-
-
-
Protease KEX2
-
-
-
-
Proteinase Kex2p
-
-
-
-
Proteinase yscF
-
-
-
-
Proteinase, prohormone-processing
-
-
-
-
Yeast KEX2 protease
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage of -Lys-Arg-/- and -Arg-Arg-/- bonds to process yeast alpha-factor pheromone and killer toxin precursors
catalytic residues are D175, H213, S385
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
99676-46-7
-
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
?
-
-
-
?
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
-
-
?
Precursor protein of the mating hormone alpha-factor of Saccharomyces cerevisiae + H2O
?
-
processing
-
-
?
Proinsulin + H2O
Insulin + ?
-
cleaves human proinsulin at the peptide bond between Arg32 and Glu33
-
?
t-butyloxycarbonyl-EKK 4-methylcoumarin 7-amide + H2O
7-amino-4-methylcoumarin + t-butyloxycarbonyl-EKK
-
-
-
?
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
-
-
-
?
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
CLC chloride channel + H2O
proteolytically processed CLC chloride channel
-
cleavage in first intracellular loop at residues K136/R137
-
-
?
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 + ?
-
mating pheromone precursor, physiological substrate
-
?
additional information
?
-
-
generates peptide hormone by specific processing of propeptides
-
?
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
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
no effect with Mg2+, Mn2+, Co3+, and Fe3+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
-
Nalpha-(p-tosyl)lysine chloromethyl ketone
-
additional information
-
L-1-tosylamido-2-phenylethyl chloromethyl ketone
-
additional information
-
no inhibition with eglin c mutant Arg replaced with Asp at P3
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
Ac-Nle-Tyr-Lys-Arg 4-methylcoumarin 7-amide
-
pH 7.0, 37°C, in natural abundance H2O
0.023
benzyloxycarbonyl-Ala-Tyr-Lys-Lys 4-methylcoumarin 7-amide
-
pH 7.0, 21°C
0.001
D-Ac-Nle-Tyr-Lys-Arg 4-methylcoumarin 7-amide
-
pH 7.0, 37°C, in natural abundance H2O
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2640
benzyloxycarbonyl-Ala-Tyr-Lys-Lys 4-methylcoumarin 7-amide
-
pH 7.0, 21°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000003
eglin c mutant Tyr replaced with Glu at P4
-
pH 7.5, 37°C
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
deficiency of Kex2p endopeptidase completely removes K2 killing ability. Deficiency in Kex2p protease compromises the protein-dependent immunity function, and Deltakex2 transformants fail to display full resistance. They are sensitive to K2 toxins produced by wild-type K2 killer strains and only resistant to their own toxin
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
37°C, t1/2: 250 min in Bis-Tris-HCl buffer, 6 min in Na-HEPES buffer
29424
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned KEX2 gene introduced into the kex2 mutant cells and the KEX2 gene product expressed in these cells
-
transformation of the single-gene deletion strain Deltakex2 with pYEX12 plasmid
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
requirement of both Kex1p and Kex2p peptidases for functional K2 toxin production
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Steiner, D.F.; Smeekens, S.P.; Ohagi, S.; Chan, S.J.
The new enzymology of precursor processing endoproteases
J. Biol. Chem.
267
23435-23438
1992
Saccharomyces cerevisiae
Fuller, R.S.; Brake, A.; Thorner, J.
Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease
Proc. Natl. Acad. Sci. USA
86
1434-1438
1989
Saccharomyces cerevisiae, Saccharomyces cerevisiae overproducing
Achstetter, T.; Wolf, D.H.
Hormone processing and membrane-bound proteinases in yeast
EMBO J.
4
173-177
1985
Saccharomyces cerevisiae
Julius, D.; Brake, A.; Blair, L.; Kunisawa, R.; Thorner, J.
Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor
Cell
37
1075-1089
1984
Saccharomyces cerevisiae
Mizuno, K.; Nakamura, T.; Oshima, T.; Tanaka, S.; Matsuo, H.
Characterization of KEX2-encoded endopeptidase from yeast Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
159
305-311
1989
Saccharomyces cerevisiae
Mizuno, K.; Nakamura, T.; Ohshima, T.; Tanaka, S.; Matsuo, H.
Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases
Biochem. Biophys. Res. Commun.
156
246-254
1988
Saccharomyces cerevisiae
Angliker, H.; Wikstrom, P.; Shaw, E.; Brenner, C.; Fuller, R.S.
The synthesis of inhibitors for processing proteinases and their action on the Kex2 proteinase of yeast
Biochem. J.
293
75-81
1993
Saccharomyces cerevisiae
Brenner, C.; Bevan, A.; Fuller, R.S.
Biochemical and genetic methods for analyzing specificity and activity of a precursor-processing enzyme: yeast Kex2 protease, kexin
Methods Enzymol.
244
152-167
1994
Saccharomyces cerevisiae
Rockwell, N.C.; Krysan, D.J.; Fuller, R.S.
Synthesis of Peptidyl Methylcoumarin Esters as Substrates and Active-Site Titrants for the Prohormone Processing Proteases Kex2 and PC2
Anal. Biochem.
280
201-208
2000
Saccharomyces cerevisiae
Rockwell, N.C.; Fuller, R.S.
Interplay between S1 and S4 subsites in Kex2 protease: Kex2 exhibits dual specificity for the P4 side chain
Biochemistry
37
3386-3391
1998
Saccharomyces cerevisiae
Rockwell, N.C.; Fuller, R.S.
Direct measurement of acylenzyme hydrolysis demonstrates rate-limiting deacylation in cleavage of physiological sequences by the processing protease Kex2
Biochemistry
40
3657-3665
2001
Saccharomyces cerevisiae
Holyoak, T.; Wilson, M.A.; Fenn, T.D.; Kettner, C.A.; Petsko, G.A.; Fuller, R.S.; Ringe, D.
2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor
Biochemistry
42
6709-6718
2003
Saccharomyces cerevisiae (P13134)
Bessmertnaya, L.; Loiko, II; Goncharova, T.I.; Ivanov, N.V.; Rumsh, L.D.; Antonov, V.K.
Specific cleavage of hybrid proteins by proteinase encoded by the KEX2 gene
Biochemistry
62
850-857
1997
Saccharomyces cerevisiae
Suzuki, Y.; Ikeda, N.; Kataoka, E.; Ohsuye, K.
Effect of amino acid substitution at the P3 and P4 subsites of fusion proteins on Kex2 protease activity
Biotechnol. Appl. Biochem.
32
53-60
2000
Saccharomyces cerevisiae
-
Liu, Z.X.; Fei, H.; Chi, C.W.
Two engineered eglin c mutants potently and selectively inhibiting kexin or furin
FEBS Lett.
556
116-120
2004
Saccharomyces cerevisiae
Rockwell, N.C.; Fuller, R.S.
Differential utilization of enzyme-substrate interactions for acylation but not deacylation during the catalytic cycle of Kex2 protease
J. Biol. Chem.
276
38394-38399
2001
Saccharomyces cerevisiae
Han, H.E.; Rho, S.H.; Lee, Y.J.; Park, W.J.
Engineering of Kex2 variants exhibiting altered substrate specificity
Biochem. Biophys. Res. Commun.
337
1102-1106
2005
Saccharomyces cerevisiae
Holyoak, T.; Kettner, C.A.; Petsko, G.A.; Fuller, R.S.; Ringe, D.
Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases
Biochemistry
43
2412-2421
2004
Saccharomyces cerevisiae
Waechter, A.; Schwappach, B.
The yeast CLC chloride channel is proteolytically processed by the furin-like protease Kex2p in the first extracellular loop
FEBS Lett.
579
1149-1153
2005
Saccharomyces cerevisiae
Rozan, L.; Krysan, D.J.; Rockwell, N.C.; Fuller, R.S.
Plasticity of extended subsites facilitates divergent substrate recognition by Kex2 and furin
J. Biol. Chem.
279
35656-35663
2004
Saccharomyces cerevisiae
Serviene, E.; Cepononyte, S.; Lebionka, A.; Melvydas, V.
Influence of Kex1p and Kex2p proteases on the function of Saccharomyces cerevisiae K2 preprotoxin
Biologija (Vilnius)
53
35-38
2007
Saccharomyces cerevisiae
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EXTERNAL LINKS (specific for EC-Number 3.4.21.61)
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Release 2023.1 (January 2023)
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