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3.4.24.69: bontoxilysin

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

Word Map on EC 3.4.24.69

Reaction

Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or syntaxin. No detected action on small molecule substrates =

Synonyms

abobotulinumtoxinA, antigen E, Balc424, BoNT, BoNT A, BoNT B, BoNT E, BoNT F, BoNT F/A, BoNT LC, BoNT LC/A, BoNT serotype A, BoNT serotype E, BoNT serotype F, BoNT-A, BoNT-C, BoNT-D, BoNT-E, BoNT-F, BoNT/A, BoNT/A LC, BoNT/A Lc endopeptidase, BoNT/A-LC, BoNT/A1, BoNT/A2, BoNT/A3, BoNT/A4, BoNT/A5, BoNT/A6, BoNT/A8, BoNT/B, BoNT/B light chain protease, BoNT/B-LC, BoNT/B1, BoNT/B6, BoNT/C, BoNT/C1, BoNT/C1-LC, BoNT/C3, BoNT/CD, BoNT/D, BoNT/E, BoNT/F, BoNT/F proteolytic F toxin, BoNT/F-LC, BoNT/F1, BoNT/F5, BoNT/F6, BoNT/F7, BoNT/F9, BoNT/FA, BoNT/G, BoNT/HA, BoNT/T, BoNT/X, BoNTA, BoNTA endopeptidase, BoNTB, BoNTC, BoNTE, BoNTF, Bontoxilysin C1, botox A, botulinum A neurotoxin light chain, Botulinum neurotoxin, botulinum neurotoxin a, botulinum neurotoxin A light chain, botulinum neurotoxin A protease, botulinum neurotoxin A subtype 1, botulinum neurotoxin A subtype 2, botulinum neurotoxin A subtype 6, botulinum neurotoxin A3, botulinum neurotoxin A4, botulinum neurotoxin A8 subtype, botulinum neurotoxin B, botulinum neurotoxin B protease, botulinum neurotoxin C, botulinum neurotoxin D light chain, botulinum neurotoxin E, botulinum neurotoxin endopeptidase, botulinum neurotoxin F, botulinum neurotoxin serotype A, botulinum neurotoxin serotype A endopeptidase, botulinum neurotoxin serotype A light chain, botulinum neurotoxin serotype A protease, botulinum neurotoxin serotype B, botulinum neurotoxin serotype BA, botulinum neurotoxin serotype C1, botulinum neurotoxin serotype C1 light chain protease, botulinum neurotoxin serotype D, botulinum neurotoxin serotype E, botulinum neurotoxin serotype F, botulinum neurotoxin serotype FA, botulinum neurotoxin serotype G, botulinum neurotoxin serotype H, botulinum neurotoxin subtype A, botulinum neurotoxin subtype A3, botulinum neurotoxin subtype A4, botulinum neurotoxin subtype B6, botulinum neurotoxin subtype F5, botulinum neurotoxin type A, botulinum neurotoxin type A light chain, botulinum neurotoxin type B, botulinum neurotoxin type C, botulinum neurotoxin type D, botulinum neurotoxin type E, botulinum neurotoxin type F, botulinum neurotoxin type F light chain, botulinum neurotoxin type G, botulinum neurotoxin type HA, botulinum neurotoxin X, Botulinum neurotoxin-A, botulinum toxin, botulinum toxin C3, botulinum toxin serotype E, botulinum toxin serotype F, botulinum toxin type A, botulinum toxin type B, botulinum toxin type F, Botulinumtoxin A, BoTxA, C2 toxin, CDC69016, Clostridium botulinum A2 neurotoxin, Clostridium botulinum C2 toxin, Clostridium botulinum neurotoxin, Clostridium botulinum neurotoxin A1, Clostridium botulinum neurotoxin F, Clostridium botulinum neurotoxin serotype A, Clostridium botulinum neurotoxin serotype A light chain, Clostridium botulinum neurotoxin type E, Clostridium botulinum serotype D neurotoxin, CNT endopeptidase, D-4947 L-TC, daxibotulinumtoxinA, HCB, HCE, incobotulinumtoxinA, LC/A, LC/D, LC/F5, LC/HA, LC/X, LCA, LcB, lcc1, LCD, LCE, LCF, LHn/D, More, mosaic toxin, neurotoxin A, NT, onabotulinumtoxinA, serotype D botulinum neurotoxin, subtype A4 neurotoxin, TeNT, Tetanus neurotoxin, type A BoNT, type A botulinum neurotoxin, type A botulinum neurotoxin light chain, type A botulinum neurotoxin protease, type F toxin

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.69 bontoxilysin

Engineering

Engineering on EC 3.4.24.69 - bontoxilysin

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A308L
-
the mutant shows 8.7% of wild type SNAP-25 cleavage activity
A308V
-
the mutant shows 86.4% of wild type SNAP-25 cleavage activity
C134A
-
site-directed mutagenesis, mutation of a binding site residue, the mutant shows reduced activity compared to the wild-type enzyme
C461S
the mutant shows similar levels of activity as the wild type enzyme
C467S
the mutant shows similar levels of activity as the wild type enzyme
D130A
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
D161A
-
the mutant exhibits a 1000fold reduction of wild type activity
D341A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
D342C
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
D369N
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
D370A
-
site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
D370R
-
site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
D426A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
D70A
-
the mutant exhibits a 10fold reduction of wild type activity
D70A/D161A
-
inactive
D877N
the mutant shows 20% reduced neurotoxicity compared to the wild type
E110A
the mutant shows similar activity to wild-type BoNT/F
E1172A
-
the binding of radioactively-labeled, in vitro translated HCE E1172A to rat brain synaptosomes is highly decreased to 8.5% of wild-type levels, as well as the binding of Escherichia coli derived HCE mutants to isolated GT1b
E1191C/S1199W
-
the mutations enhance enzyme binding to human synaptotagmin II and human synaptotagmin I
E1191M/S1199Y
E1191Q/S1199W
-
the mutation enhances binding to the human receptor synaptotagmin 2
E1191V/S1199W
-
the mutations enhance enzyme binding to human synaptotagmin II and human synaptotagmin I
E1195A
-
the HCF mutant E1195A displays a diminished affinity of 31.6% to synaptosomes as well as a reduction of about 85% in binding to isolated GT1b compared to HCF wild-type
E147A/E308A
-
the mutant exhibits a 5fold reduction of wild type activity
E147R
-
the mutant exhibits a 80fold reduction of wild type activity
E148A
-
the mutant shows 8.2% of wild type SNAP-25 cleavage activity
E148K
-
the mutant shows 1.7% of wild type SNAP-25 cleavage activity
E148R
-
the mutant shows 4.0% of wild type SNAP-25 cleavage activity
E158A/T159A/N160A
-
kcat/KM for synaptosome-associated protein SNAP-25 is 7.4fold lower than the wild-type value
E163L
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
E163Q
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
E170A
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
E200A
-
Km (VAMP-2) similar to wild-type, kcat strongly decreased compared to wild-type
E212A/E335Q
-
no detectable activity with synaptosome-associated protein SNAP-25
E224A
-
the mutation abrogates the catalytic activity of the endopeptidase of BoNT/A
E224A/E262A
-
the recombinant full length botulinum type A with mutation in its two active site residues is a detoxified BoNT/A mutant since it lacks its endopeptidase activity
E224D
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E224Q/H227Y
P10844, P10845
the mutation removes the endopeptidase activity of BoNT/A LH fragment
E224Q/R363A/Y366F
P10845
enzymatically inactive
E231Q/H234Y
P10844, P10845
the mutation removes the endopeptidase activity of BoNT/B LH fragment
E249A
-
kcat/KM for synaptosome-associated protein SNAP-25 is 20fold lower than the wild-type value
E256A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme in addition of ZnCl2 but not in absence of it, the ratio of activity in absence or presence of exogenous ZnCl2 is altered compared to the wild-type enzyme
E257A
-
site-directed mutagenesis, mutation of an S4' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
E257K
-
site-directed mutagenesis, mutation of an S4' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
E262D
-
site-directed mutagenesis, the mutant shows a three-fold reduced activity compared to the wild-type enzyme
E262Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E272A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
E280C
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
E308R
-
the mutant exhibits a 0.8fold reduction of wild type activity
E315A
-
Km (VAMP-2) increased compared to wild-type, kcat similar to wild-type
E335A
-
kcat/KM for synaptosome-associated protein SNAP-25 is 37fold lower than the wild-type value
E335Q
-
kcat/KM for synaptosome-associated protein SNAP-25 is 7300fold lower than the wild-type value. Mutation causes the toxin to transform into a persistent apoenzyme decoid of zinc
E346A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
E399/D426A/F428A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows almost no channel forming activity
E399A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
E399A/D425A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows almost no channel forming activity
E48Q
the mutant shows 64% reduced neurotoxicity compared to the wild type
E48Q/D877N
the mutant shows 8% increased neurotoxicity due to faster cytosolic delivery of the enzymatic domain
E48Q/E653K
the mutant shows 9% reduced neurotoxicity compared to the wild type
E48Q/E653Q
the mutant shows 38% reduced neurotoxicity compared to the wild type
E48Q/E653Q/D877N
the mutant shows 54% increased neurotoxicity due to faster cytosolic delivery of the enzymatic domain
E54A
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
E63A
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
E653 K/D877N
the mutant shows 28% increased neurotoxicity due to faster cytosolic delivery of the enzymatic domain
E653K
the mutant shows 15% reduced neurotoxicity compared to the wild type
E653Q
the mutant shows 31% reduced neurotoxicity compared to the wild type
E653Q/D877N
the mutant shows 32% increased neurotoxicity due to faster cytosolic delivery of the enzymatic domain
F163A
-
site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
F194A
-
site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
F194A/T220A
-
site-directed mutagenesis, mutation of S1' pocket residues, the mutant shows reduced activity compared to the wild-type enzyme
F428A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows altered chloroquine binding and almost no channel formation activity compared to the wild-type enzyme
F428D
-
site-directed mutagenesis, a C2II component mutant, the mutant shows altered chloroquine binding and almost no channel formation activity compared to the wild-type enzyme
F428W
-
site-directed mutagenesis, a C2II component mutant, the mutant shows altered chloroquine binding and almost no channel formation activity compared to the wild-type enzyme
F428Y
-
site-directed mutagenesis, a C2II component mutant, the mutant shows altered chloroquine binding and almost no channel formation activity compared to the wild-type enzyme
F50A
the mutant shows wild type activity
F50A/I191A
the mutant shows 60fold activity reduction compared to the wild type enzyme
F50D
the mutant shows 4fold activity reduction compared to the wild type enzyme
F50D/I191D
the mutant shows 400fold activity reduction compared to the wild type enzyme
H1241K
mutant shows an increased affinity for GD1a and confers the ability to bind ganglioside GM1a
H132A
the mutant shows wild type activity
H132Q
the mutant shows 100fold activity reduction compared to the wild type enzyme
H223A
-
the mutation abrogates the catalytic activity of the endopeptidase of BoNT/A
H223A/E224A/H227A
-
site-directed mutagenesis of active site residues, catalytically inactive BoNT/A1 mutant
H227A
-
the mutation abrogates the catalytic activity of the endopeptidase of BoNT/A
H233Y/E230Q
inactive
H269A
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
I115A
-
site-directed mutagenesis, mutation of a binding site residue, the mutant shows reduced activity compared to the wild-type enzyme
I151A
the mutant shows 2fold activity reduction compared to the wild type enzyme
I151D
the mutant shows 1000fold activity reduction compared to the wild type enzyme
I152D
the mutant shows 2fold activity reduction compared to the wild type enzyme
I191A
the mutant shows wild type activity
I191D
the mutant shows 4fold activity reduction compared to the wild type enzyme
I52A
-
Km (VAMP-2) increased compared to wild-type, kcat decreased compared to wild-type
K165L
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
K172A
-
Km (VAMP-2) increased compared to wild-type, kcat moderately decreased compared to wild-type
K218A
-
inactive
K218D
-
inactive
K218R
-
the mutant exhibits an 8fold reduction of wild type activity
K224D
-
mutation of BoNT/E light chain. The mutant shows extended substrate specificity to cleave SNAP-23, and the natural substrate, SNAP-25, but not SNAP-29 or SNAP-47, introduction into HeLa cells
K23A
-
the mutant shows 111% of wild type SNAP-25 cleavage activity
K23D
-
the mutant shows 72% of wild type SNAP-25 cleavage activity
K29A
the BoNT F K29A mutation does not abrogate VAMP cleavability
K337A
-
the mutant shows 55% of wild type SNAP-25 cleavage activity
K337E
-
the mutant shows 28.5% of wild type SNAP-25 cleavage activity
K340A
-
the mutant shows 99.5% of wild type SNAP-25 cleavage activity
K340D
-
the mutant shows 71.5% of wild type SNAP-25 cleavage activity
K340H
-
the mutant shows 64.1% of wild type SNAP-25 cleavage activity
K340R
-
the mutant shows 147.5% of wild type SNAP-25 cleavage activity
K41A
-
site-directed mutagenesis, mutation of a binding site residue, the mutant shows reduced activity compared to the wild-type enzyme
K58A
-
the mutant exhibits a 250fold reduction of wild type activity
L173A
-
Km (VAMP-2) increased compared to wild-type, kcat moderately decreased compared to wild-type
L175A
-
site-directed mutagenesis, mutation of an S5 pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
L175A/R177A
-
site-directed mutagenesis, mutation of S5 pocket residues, the mutant shows reduced activity compared to the wild-type enzyme
L200A
the mutant shows 2fold activity reduction compared to the wild type enzyme
L200D
the mutant shows 8fold activity reduction compared to the wild type enzyme
L256E
-
the mutant shows 13.9% of wild type SNAP-25 cleavage activity
L256E/V258P
-
the mutant shows 49.3% of wild type SNAP-25 cleavage activity
L260F/I264R
-
these mutations do not alter the activity of the enzyme
M106A
-
the mutant shows 73% of wild type SNAP-25 cleavage activity
M344A
-
the mutant shows 73% of wild type SNAP-25 cleavage activity
N26D
-
the mutant shows 90.8% of wild type SNAP-25 cleavage activity
N26K
-
the mutant shows 82.8% of wild type SNAP-25 cleavage activity
P154D
the mutant shows 4fold activity reduction compared to the wild type enzyme
P25A
-
Km (VAMP-2) increased compared to wild-type, kcat decreased compared to wild-type
Q138G/P139G/D140G
-
site-directed mutagenesis, the mutant is no longer recognized by antibody F1-40
Q161A
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
Q162A
Q34A
-
the mutation reduces the VAMP-2 cleavability by about 3fold compared to the wild type enzyme
Q66A
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
R1111A/H1241K/R1256A
triple mutant binds GD1a 17fold greater than the double-mutant
R1111A/R1256A
triple mutant binds GD1a 17fold greater than the double-mutant
R133A
R133K
the BoNT/F mutant shows over 95% reduced activity with VAMP substrate compared to the wild-type enzyme
R171A
-
Km (VAMP-2) increased compared to wild-type, kcat decreased compared to wild-type
R171K
the exosite 1 variant BoNT F shows about 98% reduction in activity with VAMP compared to the wild-type enzyme
R177A
R177D
-
the mutant shows 77% of wild type SNAP-25 cleavage activity
R230K
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
R230L
R23A
the mutant shows wild type activity
R23D/H132A
the mutant shows 25fold activity reduction compared to the wild type enzyme
R240A
-
Km (VAMP-2) similar to wild-type, kcat decreased compared to wild-type
R263A
-
Km (VAMP-2) similar to wild-type, kcat decreased compared to wild-type
R347A
-
kcat/KM for synaptosome-associated protein SNAP-25 is 1060fold lower than the wild-type value
R362L
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
R370A/373F
-
inactive
R372A
the mutant shows 40fold activity reduction compared to the wild type enzyme
R63A
the mutant shows 10fold activity reduction compared to the wild type enzyme
R63E
the mutant shows 50fold activity reduction compared to the wild type enzyme
S147A
-
Km (VAMP-2) increased compared to wild-type, kcat similar to wild-type
S224A
-
Km (VAMP-2) similar to wild-type, kcat decreased compared to wild-type
S28E
-
the mutation reduces the VAMP-2 cleavability by about 2fold compared to the wild type enzyme
T132D
-
the mutant shows 42.5% of wild type SNAP-25 cleavage activity
T176A
-
site-directed mutagenesis, mutation of an S5 pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
T192A
-
the mutant exhibits a 3fold reduction of wild type activity
T220A
-
site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
V129A
-
site-directed mutagenesis, mutation of a binding site residue, the mutant shows reduced activity compared to the wild-type enzyme
V137A
-
Km (VAMP-2) increased compared to wild-type, kcat decreased compared to wild-type
V148/I151A
the mutant shows 15fold activity reduction compared to the wild type enzyme
V148A
the mutant shows wild type activity
V148D
the mutant shows wild type activity
V258A
-
the mutant shows 33.1% of wild type SNAP-25 cleavage activity
W1224L
-
the binding of radioactively-labeled, in vitro translated HCE W1224L to rat brain synaptosomes is highly decreased to 3.7% of wild-type levels, as well as the binding of Escherichia coli derived HCE mutants to isolated GT1b
W1250L
-
the HCF mutant W1250L displays a diminished affinity of 20.5% to synaptosomes as well as a reduction of about 85% in binding to isolated GT1b compared to HCF wild-type
W1266L
-
the mutant HCA W1266L that lacks ganglioside binding, does not interfere with BoNT/A neurotoxicity
W315A
the mutant shows 20fold activity reduction compared to the wild type enzyme
W315D
the mutant shows 40fold activity reduction compared to the wild type enzyme
W319A
-
Km (VAMP-2) increased compared to wild-type, kcat similar to wild-type
W44A
-
Km (VAMP-2) increased compared to wild-type, kcat similar to wild-type
W44A/I152A/P154A
the mutant shows 20fold activity reduction compared to the wild type enzyme
W44D
the mutant shows 2fold activity reduction compared to the wild type enzyme
Y113A
-
Km (VAMP-2) increased compared to wild-type, kcat similar to wild-type
Y133A
-
Km (VAMP-2) increased compared to wild-type, kcat decreased compared to wild-type
Y168A
Y168A/L200A
the mutant shows 2fold activity reduction compared to the wild type enzyme
Y168D
the mutant shows 2fold activity reduction compared to the wild type enzyme
Y168D/L200D
the mutant shows 60fold activity reduction compared to the wild type enzyme
Y183A
-
the mutant exhibits a 3.2fold reduction of wild type activity
Y183A/Y239A
-
the mutant exhibits a 1000fold reduction of wild type activity
Y239A
-
the mutant exhibits an 8fold reduction of wild type activity
Y26A/Y50A/T192A
-
the mutant exhibits a 600fold reduction of wild type activity
Y322A
-
Km (VAMP-2) increased compared to wild-type, kcat similar to wild-type
Y350A
-
no detectable activity with synaptosome-associated protein SNAP-25
Y361A
the BoNT/F mutant shows about 18% reduction in activity with VAMP compared to the wild-type enzyme
Y365F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y365N
Y368A
-
Km (VAMP-2) similar to wild-type, kcat strongly decreased compared to wild-type
Y50A
-
the mutant exhibits a 10fold reduction of wild type activity
L260F/I264R
-
these mutations do not alter the activity of the enzyme
-
E224A/E262A
-
the recombinant full length botulinum type A with mutation in its two active site residues is a detoxified BoNT/A mutant since it lacks its endopeptidase activity
-
Q34A
-
the mutation reduces the VAMP-2 cleavability by about 3fold compared to the wild type enzyme
-
S28E
-
the mutation reduces the VAMP-2 cleavability by about 2fold compared to the wild type enzyme
-
E48Q
-
the mutant shows 64% reduced neurotoxicity compared to the wild type
-
E48Q/E653Q/D877N
-
the mutant shows 54% increased neurotoxicity due to faster cytosolic delivery of the enzymatic domain
-
E653 K/D877N
-
the mutant shows 28% increased neurotoxicity due to faster cytosolic delivery of the enzymatic domain
-
E653Q
-
the mutant shows 31% reduced neurotoxicity compared to the wild type
-
E653Q/D877N
-
the mutant shows 32% increased neurotoxicity due to faster cytosolic delivery of the enzymatic domain
-
additional information