Information on EC 3.1.8.2 - diisopropyl-fluorophosphatase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.1.8.2
-
RECOMMENDED NAME
GeneOntology No.
diisopropyl-fluorophosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric triester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
diisopropyl-fluorophosphate fluorohydrolase
Acts on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including 'nerve gases'). Inhibited by chelating agents; requires divalent cations. Related to EC 3.1.8.1 aryldialkylphosphatase.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-18-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sea hare
-
-
Manually annotated by BRENDA team
gene opd
-
-
Manually annotated by BRENDA team
slime mold
-
-
Manually annotated by BRENDA team
gene opd
-
-
Manually annotated by BRENDA team
duckweed
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Lemna minor
duckweed
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Anisodoris
-
-
Manually annotated by BRENDA team
clam
-
-
Manually annotated by BRENDA team
Sepia
-
-
Manually annotated by BRENDA team
surf clam
-
-
Manually annotated by BRENDA team
squid
-
-
Manually annotated by BRENDA team
mung been
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
diisopropyl fluorophosphatase is a calcium-dependent phosphotriesterase that acts on a variety of highly toxic organophosphorus compounds, that act as inhibitors of acetylcholinesterase
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-cyclosarin + H2O
?
show the reaction diagram
-
-
-
-
?
(R)-sarin + H2O
?
show the reaction diagram
-
-
-
-
?
(S)-cyclosarin + H2O
?
show the reaction diagram
-
-
-
-
?
(S)-sarin + H2O
?
show the reaction diagram
1,2,2-trimethylpropyl methylphosphonofluoridoate + H2O
1,2,2-trimethylpropyl methylphosphonate + fluoride + H+
show the reaction diagram
-
-
-
-
?
1-methylethyl methylphosphonofluoridoate + H2O
1-methylethyl methylphosphonate + fluoride + H+
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-ethyl(phenyl)phosphinate + H2O
?
show the reaction diagram
4-nitrophenyl-methyl(phenyl)phosphinate + H2O
?
show the reaction diagram
4-nitrophenylisopropyl phenylphosphinate + H2O
?
show the reaction diagram
-
at 22% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
4-nitrophenylpropyl phenylphosphinate + H2O
?
show the reaction diagram
-
at 24% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
coumaphos + H2O
?
show the reaction diagram
-
-
-
-
?
cyclohexyl methyl fluorophosphate + H2O
cyclohexyl methyl hydrogen phosphate + fluoride
show the reaction diagram
cyclohexyl methylphosphonofluoridoate + H2O
cyclohexyl methylphosphonate + fluoride + H+
show the reaction diagram
-
-
-
-
-
cyclohexylsarin + H2O
?
show the reaction diagram
-
-
-
-
?
cyclosarin + H2O
?
show the reaction diagram
-
-
-
-
?
diazinon + H2O
?
show the reaction diagram
-
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
show the reaction diagram
diisopropyl phosphofluoridate + H2O
diisopropyl phosphate + fluoride
show the reaction diagram
diisopropyl phosphorofluoridate + H2O
diisopropyl phosphate + fluoride
show the reaction diagram
ethyl dimethylamidocyanophosphate + H2O
ethyl hydrogen dimethylphosphoramidate + HCN
show the reaction diagram
-
-
-
-
?
ethyl N,N-dimethylphosphoramidocyanidate + H2O
ethyl N,N-dimethylphosphoramide + cyanide
show the reaction diagram
-
i.e. tabun
-
-
?
fensulfothion + H2O
?
show the reaction diagram
-
-
-
-
?
methyl parathion + H2O
?
show the reaction diagram
-
-
-
-
?
mipafox + H2O
?
show the reaction diagram
-
i.e. N,N'-diisopropyl phosphorodiamidofluoridate, poor substrate
-
-
?
O-cyclohexyl methylphosphonofluoridate + H2O
O-cyclohexyl methylphosphate + fluoride
show the reaction diagram
O-cyclohexyl methylphosphonofluoridate + H2O
O-cyclohexyl methylphosphonate + fluoride
show the reaction diagram
O-cyclohexylmethylphosphonofluoridate + H2O
?
show the reaction diagram
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate + H2O
?
show the reaction diagram
-
an organophosphorous nerve agent
-
-
?
O-isopropylmethylphosphonofluoridate + H2O
O-isopropylmethylphosphate + fluoride
show the reaction diagram
O-pinacolyl methylphosphonofluoridate + H2O
O-pinacolyl methylphosphate + fluoride
show the reaction diagram
O-pinacolylmethylphosphonofluoridate + H2O
?
show the reaction diagram
-
best substrate
-
-
?
p-nitrophenyl-soman + H2O
p-nitrophenol + soman
show the reaction diagram
paraoxon + H2O
?
show the reaction diagram
parathion + H2O
?
show the reaction diagram
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
show the reaction diagram
sarin + H2O
?
show the reaction diagram
soman + H2O
?
show the reaction diagram
tabun + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
show the reaction diagram
diisopropyl phosphofluoridate + H2O
diisopropyl phosphate + fluoride
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
fully activates the hydrolysis of diisopropyl phosphofluoridate
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Acetylcholine
-
high concentration
Butyrylcholine
-
high concentration
Hg2+
-
strong
iodoacetamide
-
-
iodoacetic acid
Mipafox
N,N'-diisopropyldiamidofluorophosphate
i.e. mipafox or DDFP. the inhibitor's hydrolysis product, N,N'-diisopropyldiamidophosphate, is present in the cocrystal structure and bound by coordinating the binuclear metals and forming hydrogen bonds and nonpolar interactions with active site residues. An unusual common feature of the binding of the two ligands is the involvement of only one oxygen atom of the glycolate carboxylate and the product DDP tetrahedral phosphate in bridging the two Mn2+ ions, binding structure analysis, detailed overview
N-ethylmaleimide
O,O-dicyclopentylphosphoroamidate
-
crystallization data, phosphoryl oxygen of inhibitor is directly coordinated to the catalytic calcium ion
additional information
-
no inhibition by K+ or NH4+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dipyridyl
-
activation, synergism with Mn2+
2-mercaptoethanol
CdCl2
CoCl2
MgCl2
MnCl2
additional information
-
an approach using recombinant enzyme encapsulated within sterically stabilized liposomes to enhance diisopropyl fluorophosphates degradation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.39
Coumaphos
-
pH not specified in the publication, temperature not specified in the publication
0.45
diazinon
-
pH not specified in the publication, temperature not specified in the publication
0.048 - 65.45
diisopropyl fluorophosphate
0.46
fensulfothion
-
pH not specified in the publication, temperature not specified in the publication
0.08
methyl parathion
-
pH not specified in the publication, temperature not specified in the publication
0.68
O-cyclohexyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
0.43
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate
-
pH not specified in the publication, temperature not specified in the publication
0.7 - 1.57
O-isopropylmethylphosphonofluoridate
0.5 - 2.48
O-pinacolyl methylphosphonofluoridate
0.058 - 14.2
Paraoxon
0.24
parathion
-
pH not specified in the publication, temperature not specified in the publication
1.57
sarin
-
-
2.48 - 33
soman
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
610
Coumaphos
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
176
diazinon
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
208 - 2111
diisopropyl fluorophosphate
67
fensulfothion
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
189
methyl parathion
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
652
O-cyclohexyl methylphosphonofluoridate
Alteromonas sp.
-
pH not specified in the publication, temperature not specified in the publication
0.3
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
56 - 442
O-isopropylmethylphosphonofluoridate
5 - 151
O-pinacolyl methylphosphonofluoridate
6.11 - 3170
Paraoxon
630
parathion
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27 - 720
(R)-cyclosarin
156522
24 - 47
(R)-sarin
156520
17 - 490
(S)-cyclosarin
156523
42 - 230
(S)-sarin
156521
1600
Coumaphos
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
12481
390
diazinon
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
7454
56 - 9700
diisopropyl fluorophosphate
244
150
fensulfothion
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
14185
2400
methyl parathion
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
5347
959
O-cyclohexyl methylphosphonofluoridate
Alteromonas sp.
-
pH not specified in the publication, temperature not specified in the publication
28463
0.045
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
41630
80 - 282
O-isopropylmethylphosphonofluoridate
19510
10 - 61
O-pinacolyl methylphosphonofluoridate
9694
55000
Paraoxon
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
228
2600
parathion
Brevundimonas diminuta
-
pH not specified in the publication, temperature not specified in the publication
2864
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.125
O,O-dicyclopentylphosphoroamidate
-
wild-type, pH 7.5, 25C, in nitrogen atmosphere
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.527
purified SMP30, substrate phenyl acetate; with phenyl acetate as substrate, pH 8.0, 25C, 1 mM MgCl2
0.998
with diisopropyl phosphorofluoridate as substrate, pH 8.0, 25C, 1 mM MgCl2
1.512
purified enzyme; purified SMP30, substrate diisopropyl phosphofluoridate
2.4
-
O-cyclohexyl methylphosphonofluoridate (-)isomer as substrate, pH 7.2, 1 mM MnCl2
2.7
-
O-cyclohexyl methylphosphonofluoridate (-)isomer as substrate, pH 7.2, 1 mM MnCl2
4
-
mutant N175D
7
-
mutant N120D
19
-
mutant H287A
29.2
-
O-cyclohexyl methylphosphonofluoridate (+)isomer as substrate, pH 7.2, 1 mM MnCl2
31
-
mutant F173A
63
-
mutant F173S
65.3
-
O-cyclohexyl methylphosphonofluoridate (+)isomer as substrate, pH 7.2, 1 mM MnCl2
78
-
mutant T195A
82
-
substrate soman, pH 8.0, temperature not specified in the publication
84
-
mutant H287Y
90
-
mutant H287Q
92
-
mutant F173Y
97
-
mutant Q304F
105
-
mutant F173V
106
-
mutant R146S
110
-
substrate sarin, pH 8.0, temperature not specified in the publication
124
-
mutant H287F
129
-
mutant H287W
143
-
mutant F173L; mutant M148A
154
-
mutant H287L
158
-
mutant F173W; mutant S271A/D232S
173
-
mutant T195L
174
-
mutant Q77Y
187
-
mutant N237S
188
-
mutant Q304W; mutant T195V
193
-
mutant Q77W
194
-
wild-type
198
-
substrate cyclosarin, pH 8.0, temperature not specified in the publication
199
-
mutant F314A
200
-
mutant D232S
209
-
mutant Y144S
225
-
substrate diisopropyl fluorophosphate, pH 8.0, temperature not specified in the publication
additional information
-
pH dependence of the specific activity of the mutant H287N
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
5 mM diisopropyl fluorophosphate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
active over a range of 0-0.5 M NaCl
6 - 9
-
the effect of pH 6.0-9.0 on kinetic constants kcat and KM is studied, KM shows no perceivable dependence on pH within this pH range, kcat increases with pH to a limiting value at pH 8.0
7.6 - 9
-
about half-maximal activity at pH 7.6 and about 60% of maximal activity at pH 9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
50
-
3 mM diisopropyl fluorophosphate, pH 7.2, 1 mM MnCl2
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
3-4fold rate increase from 25C to 40C, still active at 55C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
posterior, higher activity in glands of female than male squid
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000 - 30000
-
three enzyme types of different MW: 20000-30000, 45000-50000 and 70000-100000
35220
-
calculated from amino acid frequence
42000
-
protein sequencing
45000 - 50000
-
three enzyme types of different MW: 20000-30000, 45000-50000 and 70000-100000
53000
-
1 * 53000 SDS-PAGE
58000
x * 58000, the enzyme OPAA structure is composed of two domains, a small N-terminal domain or N-domain, residue 1 to 160, and a large C-terminal domain or C-domain
58500
-
x * 58500
60000
-
1 * 60000, SDS-PAGE, under reducing and nonreducing conditions
70000 - 100000
-
three enzyme types of different MW: 20000-30000, 45000-50000 and 70000-100000
73000
-
x * 73000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 35000, OPH from displays the TIM barrel fold in the active site loaded with Zn2+, overview
monomer
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
N-glycosylation at amino acids 13 and 171
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified OPAA, in acetate buffer equilibrated in a reservoir solution containing a much greater concentration of acetate, 270 mM ammonium acetate and 60 mM sodium acetate, pH 4.6, X-ray structure determination and analysis at 2.7 A resolution for the enzyme with bound inhibitor N,N'-diisopropyldiamidophosphate, and at 2.3 A resolution for the native enzyme
at 2.2 A resolution, after exchange of available H atoms by using D2O. Collection of time-of-flight wavelength-resolved Laue images
-
by vapour diffusion using a protein solution with 2 mM protein in 10 mM Tris, pH 7.5, 2 mM CaCl2, against a precipitation solution containing 11% PEG 4000 in 0.1 M MES, pH 6.5, at room temperature, X-ray diffraction structure determination and analysis at 2.2 A resolution. Comparison with structures of enzyme mutants, overview
-
hanging drop vapour diffusion method
-
homology modeling and docking of substrates. The two identical hydrophobic isopropyl groups in diisopropyl fluorophosphate bind to two different sub-pockets in the binding-site. Sub-pocket 1 is formed by residues P36, E37, I72, A74 and M90 while sub-pocket 2 is formed by F173, N175, T195, and W244
-
hydrodynamic model calculations based on the DFPase crystal structure from the native state enzyme structure in solution by use of different scattering methods, i.e. small-angle neutron scattering, overview
-
in complex with inhibitor O,O-dicyclopentylphosphoroamidate. Phosphoryl oxygen of inhibitor is directly coordinated to the catalytic calcium ion
-
mutant enzymes are crystallized at room temperature by hanging drop vapor diffusion method, using 0.1 M Tris buffer pH 8.5, 2% tacsimate, 16% (w/v) PEG 3350 for mutant E37A/Y144A/R146A/T195M or 0.2 M KCl, 0.05 M HEPES buffer pH 7.5, 35% (w/v) pentaerythriol propoxylate for mutant E37D/Y144A/R16A/T195M
-
mutant enzymes N120D/N175D/D229N, E21QN120D/N175D/D229N, and D121E are crystallized by hanging drop vapor diffusion method, using 0.1 M MES buffer pH 6.5, 14-20% (w/v) PEG 3350
-
quantum mechanical/molecular mechanical umbrella sampling simulations. The mechanism for hydrolysis of diisopropyl fluorophosphate involves nucleophilic attack by Asp229 on phosphorus to form a pentavalent intermediate. P-F bond dissociation then yields a phosphoacyl enzyme intermediate in the rate-limiting step. A water molecule, coordinated to the catalytic Ca2+, donates a proton to Asp121 and then attacks the tetrahedral phosphoacyl intermediate to liberate the diisopropyl phosphate product. The calculated free energy barrier for hydrolysis of (S)-sarin by the same mechanism is highly unfavorable. Hydrolysis of (S)-sarin proceeds by a mechanism in which Asp229 could activate an intervening water molecule for nucleophilic attack on the substrate
-
structural characterization of a squid-type enzyme, the overall structure of this protein represents a six-fold beta propeller with two calcium ions bound in a central water-filled tunnel
-
vapor diffusion method, using 11% (w/v) PEG 6K, MES pH 6.5
-
wild-type and mutant N175D, 1.7 A resolution
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol enhances stability
-
DTT enhances stability
stable to prolonged dialysis procedures
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, in the presence of DTT, several months
-
37C, liposomes encapsulating enzyme incubated in blood, stable over 2 days
-
5C, anchored to a photoluminescent porous silicon platform, bis-trispropane buffer and glycerol (1:1), no loss of activity for at least 6 months
-
frozen, less than 35% loss of activity within 6 months with repeated freeze-thawing cycles
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; SMP30 49fold from liver by anion exchange and hydrophobic interaction chromatography, and gel filtration
Ni-NTA column chromatography and Q Sepharose column chromatography
-
Ni-NTA column chromatography and Q-Sepharose column chromatography
-
partial
partial, 3 enzymes of different MW
-
recombinant enzyme, production of large amounts
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli DH5alpha cells
-
expression in Escherichia coli
expression in Pichia pastoris
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the coexpression of recombinant human SMP30 with GroES/GroEL/Tf at 15C, combined with the addition of a membrane fluidizer, increases osmolytes, and a two-step expression results in the highest enhancement of solubility and DFPase activity
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H254R
-
the active site mutation results in increased activity with soman and VX
H275L
-
the active site mutation results in increased activity with soman and VX
H275V
-
the active site mutation results in increased activity with soman and VX
D121E
-
the mutant displays 87% activity compared to the wild type enzyme
D121F
-
no activity
D229N
-
enzymatically inactive
D229N/N120D
D229N/N175D
-
catalytically inactive, no change in the calcium coordinating environment
D232S
-
3% higher activity than the wild-type
E21Q/N120D
-
catalytically inactive
E21Q/N120D/N175D/D229N
-
the mutations lead to a loss of calcium binding and enzymatic activity
E21Q/N175D
-
catalytically inactive
E37A/Y144A/R146A/T195M
-
the mutant shows increased turnover number and kcat/Km for diisopropyl fluorophosphate compared to the wild type enzyme
E37D/Y144A/R16A/T195M
-
the mutant shows increased turnover number and kcat/Km for diisopropyl fluorophosphate compared to the wild type enzyme
F173A
-
84% lower activity than the wild-type
F173L
-
28% lower activity than the wild-type
F173S
-
68% lower activity than the wild-type
F173V
-
46% lower activity than the wild-type
F173W
-
19% lower activity than the wild-type
F173Y
-
53% lower activity than the wild-type
F314A
-
3% higher activity than the wild-type
H219N
-
no effect on catalytic activity
H224N
-
115% activity in comparison to wild-type enzyme
H248N
-
no effect on catalytic activity
H287A
-
90% lower activity than the wild-type
H287D
-
99% lower activity than the wild-type
H287F
-
36% lower activity than the wild-type
H287L
-
21% lower activity than the wild-type
H287Q
-
54% lower activity than the wild-type
H287W
-
34% lower activity than the wild-type
H287Y
-
57% lower activity than the wild-type
M148A
-
26% lower activity than the wild-type
N120D
-
96% lower activity than the wild-type
N120D/N175D/D229N
-
the mutations lead to a loss of calcium binding and enzymatic activity
N175D
-
98% lower activity than the wild-type
N237S
-
4% lower activity than the wild-type
N272F
-
no activity
Q304F
-
50% lower activity than the wild-type
Q304W
-
3% lower activity than the wild-type
Q77F
-
no activity
Q77W
-
6% higher activity than the wild-type
Q77Y
-
6% lower activity than the wild-type
R146S
-
45% lower activity than the wild-type
S271A
-
34% higher activity than the wild-type
S271A/D232S
-
19% lower activity than the wild-type
T195A
-
60% lower activity than the wild-type
T195L
-
11% lower activity than the wild-type
T195V
-
3% lower activity than the wild-type
Y144S
-
8% higher activity than the wild-type
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
degradation
environmental protection
medicine
additional information