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inhibition of isoenzyme A2 and C2, no inhibition of isoenzyme B2
0.2 mM, strong inhibition
1 mM, complete inhibition
loses 30% of its activity immediately on addition of o-phenanthroline
1.26 mM, 41% inhibition after 1 h, 82% inhibition after 2 h, no change in remaining activity after removal of 1,10-phenanthroline
-
competitive inhibition vs. indanol
-
uncompetitive inhibition with respect to NAD+ and competitive inhibition with respect to D-galactose
-
inhibits 96% at 4 mM, reduction reaction
-
at concentrations higher than 3 mM and low concentration of NAD+, about 50% inhibition
-
complete inhibition at 0.1 mM
-
50% inhibition at 0.065 mM
-
70% remaining acitvity at concentration 1 mM
-
50% inhibition at 16.7 mM
-
about 11% inhibition at 1 mM
-
slight inhibition at 1 mM
-
in 250 mM glycine-NaOH buffer (pH 9.0), purified water and 20 mM heptanal, at 5 mM inhibits by 16% and at 10 mM inhibits by 68% in the presence of 10 mM NADH, at 5 mM inhibits by 25% and at 10 mM inhibits by 63% in the presence of 10 mM NADPH
-
wild-type, W86Y and W227Y
-
weak irreversible inhibitor
-
complete inhibition at 1 mM
-
30% of activity at 10 mM
-
54% inhibition at 1 mM, 96% at 5 mM
-
slight inhibition at 1 mM, 50-70% inhibition at 5 mM
-
dose dependent decrease in enzyme activity
-
inhibition, (R)-2,3-butanediol dehydrogenase activity
-
79% inhibition at 1.0 mM, 87% at 10 mM
-
10 mM, decrease of 13% in the enzymatic activity
-
0.025 mM, 70% activity lost after 5 min
-
50% inhibition at a concentration of 50 mM
-
1 mM, 100% inhibition with NAD+ as cofactor, 40% with NADP+ as cofactor
-
1 mM, 30% inhibition after 3 h incubation
-
2 mM, 0.4% residual activity
-
2 mM, 9% residual activity
-
1 mM, 43% residual activity
-
very strong, reactivation with Zn2+ and Co2+
-
1 mM, 56% loss of activity
-
93% residual activity at 1 mM
-
strong inhibition between 0.1-1.0 mM
-
5-23% inhibition at 1 mM
-
5-14% inhibition at 1 mM
-
1 mM, 30 min at 4°C, 30% inhibition
-
1 mM, 30 min at 4°C, 26% inhibition
-
18.6% inhibition at 1 mM
-
88% residual activity at 1 mM
-
inhibition potentiated by KCN
-
inactivation during preincubation at 0°C; progressive inactivation, substrate decreases rate of inactivation
-
10 mM, complete loss of activity
-
1 mM, 14.7% loss of activity. 10 mM, 89.1% loss of activity
-
inhibits competitive Mn(III)-malonate formation
-
progressive inactivation, loss of all activation after 90 min, reactivation with Fe3+
-
CD I and CD II respectively
-
0.05 mM, 10 min, 3% inhibition
-
45-55% inhibition at 10 mM
-
totally inhibits at very low concentrations
-
13% inhibition at 0.01 mM, 88% inhibition at 0.1 mM
-
non-preincubated protein-B: 91% inhibition at 1 mM, with cysteine preincubated protein-B: 67% inhibition at 1 mM
-
without protein-A: 96% inhibition at 0.1 mM, with protein A: 100% inhibition at 0.1 mM
-
0.21 mM, 46% residual activity
-
1 mM, 68% inhibition after 10 min, noncompetitive inhibition
-
0.01 mM, 50% inhibition
-
85% inhibition at 0.1 mM
-
0.005 mM, approx. 50% inhibition after 30 min, complete inhibition after 60 min, complete restoration of inactivated enzyme by addition of excess ferric EDTA complex
-
90% inhibition at 0.1 mM
-
0.01 mM, 34% inhibition
-
0.1 mM, reactivation by incubating with FeSO4 and ascorbic acid
-
inhibits at 0.01 mM, addition of 0.1 mM FeSO4 restores the enzyme activity; inhibits at 0.01 mM, addition of 0.1 mM FeSO4 restores the enzyme activity
-
0.05 mM, over 90% inhibition
-
inactivation in the absence of O2 due to formation of a white precipitate corresponding to apoprotein
-
largely irreversible losses
-
Fe2+ chelator, 1 mM, complete inhibition
-
1 mM, complete loss of activity
-
complete inhibition at 1 mM
-
1% residual activity at 2 mM
-
26% residual activity at 0.5 mM
-
0.01 mM, 89% inhibition
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
-
91% inhibition at 0.02 mM
-
0.6 mM, 100% inhibition of hydroxylation reaction, EC 1.14.11.26
-
0.5 mM, no residual activity
-
at 0.02 mM complete inhibition
-
2 mM, no residual activity
-
10 mM, 63% inhibition of ferredoxinNAP reductase
-
100% inhibition at 0.5 mM
-
0.5 mM, 82% loss of activity
-
0.1 mM, 100% inhibition
-
50% inhibition at 0.25 mM, 80% inhibition at 0.5 mM and 95% inhibition at 1 mM
-
46% inhibition at 0.5 mM , 60% inhibition at 1 mM, 80% inhibition at 3 mM, anthranilic acid protects the enzyme from inhibition
-
46% inhibition at 0.5 mM, 60% inhibition at 1 mM
-
2 mM, 40% inhibition. Activity is completely restored by 2 mM Fe2+
-
slight inhibition at 0.0005 to 0.001 mM
-
complete inhibition at 1 mM
-
complete inhibition at 1 mM
-
0.05 mM, 70% inhibition
-
10% residual activity at 1 mM
-
1 mM, removes Fe2+ from the reduced enzyme
-
74.2% inhibition at 0.5 mM
-
0.0024 mM, 50% inhibition, competitive vs. tryptophan
-
1.0 mM, 68% inhibition, reaction with RS-batyl alcohol and 6-methyl-5,6,7,8-tetrahydropterin
-
1 mM, inactivation, half-life: 30 min
-
44% residual activity at 1 mM
-
47% residual activity at 1 mM
-
5 mM, complete inhibition
-
83% residual activity at 1 mM
-
0.02 mM, 37% inhibition
-
0.6 mM, 100% inhibition of expandase reaction, EC 1.14.20.1
-
complete inhibition at 0.01 mM
-
depending on assay method; Fe-SOD
-
2.71% residual activity at 0.1 mM
-
12% inhibition of xanthine-NAD+-activity at 7.5 mM
-
50% inhibition at 5-15 mM
-
19.5% inhibition of hypoxanthine oxidation at 10 mM
-
1 mM, 30-50% inhibition
-
63% inhibition at 10 mM
-
; inhibits BZDH by 60%, probably by chelation of tightly bound Mg2+ ions
-
enzyme a, b, c, d and e
-
1 mM causes 5% inhibition at 30°C
-
0.1 mM, 15% residual activity
-
0.1 mM concentration 26% inhibition
-
1 mM, inactivates CO/acetyl-CoA exchange activity completely but has no effect on CO oxidation
-
50% inhibition at 0.006 mM
-
0.025 mM, 50% inhibition. The rate of conversion of violaxanthin to antheraxanthin is relatively unchanged whereas the conversion of antheraxanthin to zeaxanthin is 50-80% inhibited
-
5 mM, 58% residual activity
-
DD1, recombinant DD1, but DD2 less sensitive
-
recombinant: DD1, DD4, CDD1-4, CDD4-1
-
enzyme preincubated with the inhibitor, 0.00166 mM, for 60 min at room temperature before the addition of the substrate, 71% inhibition
-
in absence of substrate
-
25% inhibition of aerobic, 53% inhibition of anaerobic enzyme at 10 mM
-
90% inhibition of anaerobic reaction at 0.17 mM
-
in presence of glutathione
-
37% inhibition at 10 mM
-
complete inhibition at 10 mM
-
5 mM, strong inhibition of isozymes 1-3
-
0.05 mM, 50% inhibition
-
complete inhibition of isoform LAAOII and about 30% inhibition of isoform LAAOI at 5 mM
-
15% residual activity at 1 mM (pH 5.5)
-
84% residual activity at 1 mM
-
0.005 M, 14% inhibition
-
0.005 M, 52% inhibition
-
1 mM, slight inhibition
-
1 mM, complete inhibition
-
1 mM, complete inhibition
-
50% inhibition at 0.12 mM
-
2 mM, 4% residual activity
-
5 mM, complete inhibition
-
1 mM, 12% residual activity
-
1 mM, complete inhibition. 1,10-Phenanthroline additionally has inhibitory effects on growth of Peptoclostridium difficile
-
2 mM, 82% inhibition, 1 mM, 73% inhibition
-
93.1% residual activity after 1 h at 1 mM
-
20% residual activity at 20 mM
-
2 mM, complete inhibition
-
inactivated enzyme can be fully restored by addition of Zn2+ in the presence of equimolar concentrations of EDTA, little reactivation by Co2+ and Mn2+
-
time-dependent inactivation
-
0.01 mM, 91% inhibition
-
strong inhibition at 5 mM
-
1 mM, 84% residual activity
-
0.1 mM, 55% inhibition, 1,2-dioleoylglycerol protects and activates enzyme
-
activity is restored by Fe2+ or Zn2+
-
inhibits wild-type enzyme, no inhibition of mutant enzyme C11N
-
inhibits reactivation of O2-inactivated enzyme
-
inactivation of the enzyme by chelation of Zn2+ and Fe2+ ions, UDP-glucose protects, but alpha-D-glucose 1-phosphate does not
-
1 mM, 28% inhibition, major poly(A) polymerase, 50% inhibition, minor poly(A) polymerase
-
inhibition of AMP incorporating activity only, the CMP incorporating activity is much less sensitive
-
34% inhibition at 10 mM
-
slight inhibition, 1 mM, 88% remaining activity
-
40% residual activity at 1 mM
-
55% remaining activity after 5 min, 18% remaining activity after 60 min, 1 mM
-
dose-dependent inhibition
-
80% relative residual activity
-
19% inhibition by 1 mM, 27% inhibition by 2 mM
-
20 mM, strong inhibition
-
inhibition of Mn2+-dependent enzyme, no inhibition of the Mg2+-dependent enzyme
-
1 mM, irreversibly inactivates the enzyme
-
inhibition of cytosolic and membrane-bound enzyme
-
0.24 mM, complete inhibition of plasmid nicking activity
-
inhibits the phospholipase C hydrolytic activity of the enzyme, but not its membrane fusion activity
-
inhibitory effects of 1,10-phenanthroline at different concentrations on lysoPLD activity against palmitoyl-lysophosphatidylcholine
-
50% inhibition at 2.5 mM, 70% inhibition
-
more effective than EGTA
-
Zn2+ and to a lesser extent Co2+ protect
-
almost total inhibition
-
0.3 mM, more than 95% inhibition
-
1 mM, complete inhibition
-
34% inhibition at 1 mM, 76% inhibition at 10 mM
-
complete inhibition at 1 mM
-
1 mM, 39% loss of activity of the membrane-bound enzyme
-
10.7% inhibition at 10 mM
-
22% inhibition at 10 mM
-
slight inhibition at 10 mM
-
no inhibition of isozyme MG4, 22.5 inhibition of isozyme MG6
-
inhibits the neutral trehalase in presence of 5 mM trehalose
-
inhibits the acid trehalase, inhibits the neutral trehalase in presence of 5 mM trehalose
-
less effective inhibitor, when the 1,10-phenanthroline concentration is raised to 10 mM, the activity of isoform RhaB1 decreases by 50%; less effective inhibitor, when the 1,10-phenanthroline concentration is raised to 10 mM, the activity of isoform RhaB2 decreases by 50%
-
concentration of 1 mM causes 25% inhibition
-
40.5% inhibition at 5 mM
-
strong inhibitor, after preincubation of the purified enzyme for 1 h at 0°C
-
63.3% residual activity at 5 mM
-
IFO 3134, slight inhibition
-
5 mM, no inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 5% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
-
61.5% inhibition at 5 mM
-
0.5 mM, completely inhibited
-
86.3% inhibition at 5 mM
-
87.8% inhibition at 5 mM
-
31.1% residual activity at 0.2 mM
-
30.4% residual activity at 1 mM
-
16% inhibition at 1 mM, 77% at 10 mM
-
0.25 mM: 17% activity, restored by Mn2+ and Ca2+
-
7.2% residual activity at 1 mM
-
3.3% activity at 0.2 mM
-
-
650891, 665011, 731553, 81176, 95176, 95178, 95181, 95182, 95195, 95196, 95198, 95218, 95222, 95224, 95225, 95226
-
10 mM, abolishes enzyme activity in presence or absence of Co2+
-
complete inhibition, reversible by Zn2+
-
complete inhibition at 0.25 mM, reversible by Zn2+, not by other divalent cations, overview
-
the recombinant enzyme shows 18.8% relative activity in the presence of 1 mM 1,10-phenanthroline on hydrolysis of L-Leu-7-amido-4-methylcoumarin
-
1 mM, complete inhibition
-
99% inhibition at 0.5 mM; Ki 0.028 mM
-
19.4% residual activity at 0.2 mM
-
22% inhibition at 0.1 mM
-
100% inhibition at 1 mM
-
99% inhibition at 0.4 mM, Ki: 0.067 mM
-
97% inhibition after 10 min at 10 mM
-
80% inhibition at 0.01 mM
-
the inhibition is completely reversible by Zn2+, but not by other metal ions such as Mg2+ or Ca2+, partially by Co2+ or Mn2+
-
92.5% inhibition at 1 mM
-
0.005 mM, 5% residual activity
-
0.01 mM, complete inhibition
-
-
35863, 35867, 35870, 35894, 652119, 665114, 666144, 666997, 683496, 707405, 710669
-
complete inhibition at 2 mM
-
treatment with 1,10-ortho-phenanthroline in order to deplete metal ions, results in a residual activity of about 8% compared to the initial activity. Activity is partially restored by the addition of divalent metal cations with Zn2+ being the most potent
-
after preincubation total loss of activity
-
; 33.5% inhibition at 5 mM
-
43% residual activity at 5 mM; 43% residual activity at 5 mM
-
activity is reduced to 8.3% after incubating with 20 mM o-phenanthroline
-
half-maximal inhibition at 1.8 mM, competitive and reversible inhibition is reversed by ZnCl2, increases 20fold the inhibition by EDTA
-
86.3% inhibition at 5 mM
-
87.8% inhibition at 5 mM
-
3% residual activity at 10 mM
-
50% inhibition at pI 4.9
-
1 mM, complete inhibition
-
0.1 mM, 83% inhibition. 0.01 mM, 10% inhibition
-
competition between 1,10-phenanthroline and the substrate only in presence of EDTA. Inhibitory effect of EDTA plus 1,10-phenanthroline can be completely reversed by Zn2+. Ca2+ and Mg2+ increase the potency of Zn2+ for this process
-
IC50: 0.2 mM. Inhibitory effect is substantially potentiated by both EDTA and EGTA. A combined and complete inhibition of the enzyme activity by 0.1 mM EDTA and 0.1 mM 1,10-phenanthroline can be prevented in the presence of 0.04-0.1 mM ZnCl2
-
1 mM, complete inhibition
-
strongly inhibitory at 1 mM
-
activity restored by Co2+
-
complete inhibition at 1 mM
-
complete inhibition, reversible by Zn2+
-
68.5% inhibition at 5 mM
-
34% residual activity at 1 mM
-
the native enzyme is inhibited by 76% at 0.5 mM, the recombinant enzyme is inhibited by 80% at 0.5 mM
-
reactivation by Co2+ or Zn2+
-
0% residual activity at a concentration of 1 mM
-
activity is reduced to 8.3% after incubating with 20 mM o-phenanthroline
-
complete inhibition at 0.1 mM
-
50% inhibition at 0.036 mM
-
50% inhibition at 0.01 mM
-
-
36042, 36044, 36047, 36054, 36055, 36057, 36059, 36061, 36062, 651109, 731113, 731729
-
1,7-phenanthroline has no effect
-
ZnSO4 restores activity
-
5 mM, 67% residual activity
-
50% inhibition at 0.1 mM
-
1.0 mM inhibitor, 46% inhibition, 2.5 mM inhibitor, 85% inhibition, 5.0 mM inhibitor, 96% inhibition
-
1.0 mM, 14 mM 40°C, partial
-
5.0 mM, complete inhibition
-
complete inhibition at 10 mM
-
80% inhibition at 0.1 mM
-
complete inhibition at 1 mM
-
-
36317, 36321, 36323, 36324, 36325, 36330, 36334, 36335, 36338, 668942, 679958, 706874
-
1 mM, complete inhibition
-
0.1 mM and 1 mM, 95.6% and 74.7% compared to a control without additives
-
Ki: 0.035 mM, reversible by addtion of bivalent metal ions like Zn2+, Co2+, Cd2+ and Mn2+
-
100% inhibition at 1 mM
-
0.1 mM, proPoCtX: 51.3% inhibition, native PoCtX: 56.6% inhibition
-
reactivation by zinc, cobalt and manganese ions
-
inhibits at a molar ratio of inhibitor to enzyme of 50:1
-
partial inhibition at very high concentrations
-
complete inactivation at 5 mM
-
79% residual activity at 0.2 mM
-
20% inhibition at 0.01 mM, 55% inhibition at 0.1 mM, 64% inhibition at 0.5 mM
-
at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 40%
-
substrates Nalpha-benzoyl-DL-Arg-4-nitroanilide, acetyl-Leu-Leu-Arg-4-nitroanilide, anticompetitive
-
zinc-selective chelator, inhibits NS2/3 auto-cleavage and NS3 protease activity
-
inhibits NS2/3 auto-cleavage and NS3 protease activity
-
0.26 mM, 50% inhibition
-
66% remaining activity at 1 mM, 68% remaining activity at 2 mM
-
77.3% residual activity at 1 mM
-
36.6% inhibition at 0.1 mM
-
inhibits processing of proenzyme to active form
-
in trans cleavage activity
-
27.5% inhibition at 5 mM
-
concentration of 1 mM, 10 min before addition of substrate, 40% inhibition; concentration of 1mM, 10 min before addition of substrate, 40% inhibition observed
-
15.28% inhibition at 0.1 mM
-
Ca2+ enhances inhibitory effect
-
45% inhibition at 0.1 mM
-
100% inhibition at 1 mM
-
complete inhibition at 4 mM
-
complete inhibition at 4 mM
-
at neutral and alkaline pH-values, reversible by dialysis
-
strong, caseinolytic activity
-
1 mM, isoform LAST, 10% residual activity, isoform LAST_MAM, 12% residual activity
-
r; reactivation of apoenzyme by Zn2+ (100%), Cu2+ (70%) or Co2+ (50%); strong, kinetics
-
a non-specific inhibitor of metalloproteinases
-
1 mM, 73% loss of activity
-
complete inhibition at 1 mM
-
5 mM, 0% residual activity
-
1 mM, 16% residual activity
-
5 mM, complete inhibition
-
85% inhibition at 1 mM, 93% at 5 mM
-
94.2% inhibition at 0.5 mM, 100% at 5 mM
-
activity restored by Co2+, Mn2+, Ca2+, Cu2+, Ni2+ and Zn2+
-
The half maximal inhibitory concentrations of the catalytic domains for 1,10-phenanthroline are significantly decreased in the presence of the N-terminal His6-tag
-
The half maximal inhibitory concentrations of the catalytic domains for 1,10-phenanthroline are significantly decreased for both isoforms ColG and ColH in the presence of the N-terminal His6-tag
-
Zn2+ does not restore after prolonged incubation
-
cannot be reactivated by Zn2+
-
totally inhibited by 10 mM 1,10-phenanthroline
-
strong inhibition at 1 mM
-
inactivation by dialysis against 1,10-phenanthroline, reactivation of apoenzyme by Zn2+, partially by Cu2+, Co2+, Cd2+ or Ni2+, not by Hg2+, Ca2+, Fe2+, Pb2+, Ba2+, Sn2+, Mg2+, Mn2+, Fe3+ or Ag+; strong, 1 mM, Zn2+ reverses, bovine serum albumin as substrate
-
complete inhibition at 0.1 mM
-
reversible by dialysis, Mg2+ or Co2+ partially restores; strong
-
neither Ca2+, Zn2+ nor Fe2+ restores
-
Serratia marcescens enzyme
-
30 min, room temperature, pH 7.5, complete and irreversible inhibition in a concentration range below 1 mM
-
pH 7.8, 37°C, 1 mM 66% inhibition, 3mM 90% inhibition
-
10 mM, strong inhibition at pH 5.5 and pH 8.0 with and without addition of 1 mM Co2+
-
activity can be restored with the addition of Mn2+, Cu2+ and Co2+ up to 90-200% of its original value, while Zn2+ is inefficient
-
2 mM, no residual activity
-
0.5 mM, 10% residual activity
-
inhibits proteolytic and hemorrhagic activities
-
inhibits proteolytic and hemorrhagic activity of atrolysin C
-
inhibits proteolytic and hemorrhagic activities
-
inhibits proteolytic activity
-
+ 4 mM Ca2+: 85% inhibition
-
totally inhibits at 0.1 mM
-
inhibits the hemorrhagic and proteolytic activity of HR1A
-
inhibits lethal and hemorrhagic activities
-
Co2+, and to a lesser extent but at lower metal ion concentration Zn2+ restores activity
-
Zn2+, Co2+, Mn2+ and to a smaller extent Cd2+ and Fe2+ are capable of preventing the inhibition
-
0.1 mM, wild-type, 73% residual activity, mutants H112D, H112Q, less than 2.5% residual activity
-
total inhibition at 10 mM
-
5 mM inhibits in the presence of 10 mM Ca2+
-
metalloendopeptidase character
-
0.01 or 0.05 mM Zn2+, Ca2+ or Mn2+ fully restores; metalloendopeptidase character
-
dynorphin A or [Ala17,Tyr20]-somatostatin-28-(10-20)-NH2 as substrate
-
chelator function, hNRDc1 is Zn2+ dependant
-
excess Zn2+ or Co2+ partially restores; soluble matrix enzyme
-
excess Zn2+ or Co2+ partially restores
-
excess Zn2+ or Co2+ partially restores; in vitro and in vivo
-
not Zn2+, Ca2+, Mg2+, Cu2+, Ni2+, Fe2+
-
excess Mn2+ (bovine, rat) restores
-
excess Co2+ (rat) restores; excess Mn2+ (bovine, rat) restores
-
enzyme inhibition leads to degradation of the unprocessed preproteins in the mitochondrial matrix space
-
chelates the required Zn2+
-
totally inhibits at 4 mM
-
1 mM, inhibition of ECE-1 activity
-
complete and rapid inhibition
-
rapid and complete inhibition
-
1 mM, complete inhibition
-
10 mM, complete inhibition
-
inhibits shedding of Eph-A5
-
inhibit activity 0.1 mM
-
1 mM, complete inhibition of aggrecanase 1 and 2
-
inhibition of recombinant Ste24 CAAX proteolytic activity
-
1,10-phenanthroline specifically inhibits substrate cleavage in a concentration-dependent manner
-
activity can be restored by Ca2+
-
total inhibition when incubated with gelatin at 37 °C for either 2 or 18 h
-
inhibition of the soluble isozyme SEP
-
complete inhibition at 1 mM
-
inhibition of the staphylolytic activity
-
chelator for divalent metal ions
-
strongly inhibits at 10 mM
-
4 mM, complete inhibition
-
hemorrhagic as well as the proteinase activity is inhibited
-
91% inhibition at 0.1 mM
-
0.1 mM, 8.3% inhibition
-
0.1 mM, 82% inhibition of the enzyme isolated on the Ni-affinity column. 0.1mM 1,10-phenanthroline produces no signifiant inhibition of the enzyme isolated on the Zn-affinity column and 10% activity remains after treatment with 1 mM 1,10-phenanthroline. MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity, but Ca2+ and Mg2+ produce no restoration of activity; inhibition of the Zn enzyme by 1,10-phenanthroline is slower or less complete than inhibition of the Ni enzyme. MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity. Ca2+ and Mg2+ produce no restoration of activity
-
the enzyme is completely inhibited by low levels of 1,10-phenanthroline
-
0.19% residual activity at 1 mM 1,10-phenanthroline
-
; 20-30% inhibition at 1 mM
-
10% residual activity at 1 mM; 90% inhibition at 1 mM
-
0.005 mM, complete inhibition after 30 min, activity can be restored by 0.1 mM ZnSO4
-
strong, 5 mM, 94% inhibition
-
inactivation through depletion of zinc ions
-
2 mM, 90-100% inhibition
-
99% inhibition at 0.5 mM
-
complete inhibition at 1 mM
-
20-30% inhibition at 1 mM
-
84% inhibition at 50 mM
-
1 mM, 96% inhibition, activity can be partially restored by Zn2+
-
o-phenanthroline, 10 mM: 97% inhibition, partially reversed by CuCl2, CoCl2 and to a lesser extent by ZnCl2 and MnCl2, 1 mM: 29% inhibition, 0.1 mM: no inhibition. 2.5 mM: 73% inhibition, totally reversed by 0.66 mM ZnCl2, CuCl2 or CoCl2 and to a lesser extent also by nickel and manganous ions
-
10 mM, 18% loss of activity
-
rapid inactivation even at an alkaline pH, 9.3
-
similar inhibition of Fe2+- and Co2+-bound enzyme
-
complete inhibition at 5 mM
-
competitive with respect to N-formyl-Met-Val; time-dependent inhibition of cobalt-substituted enzyme with loss of the active site metal
-
competitive with respect to N-formyl-Met-Val
-
25% inhibition at 0.1 mM
-
at 1 mM 47% and at 2 mM 46% residual enzyme acitvity
-
inactivation due to removal of bound Zn2+, reversible by Zn2+ and Co2+, and partially by Mn2+
-
inactivation due to removal of bound Zn2+, reversible by Zn2+ and Co2+, and partially by Mn2+
-
removes Fe2+ from the Fe2+CDase to give the apoenzyme, cause of loss in activity, reversible by Fe2+ addition, poor effect on Zn2+CDase
-
66% residual activity at 1 mM
-
1 mM, 45% loss of activity. 1 mM, 91% loss of activity
-
5 mM abolishes activity up to 70%
-
5 mM, 30% residual activity, Mn2+, Co2+ or Ni2+ restores
-
72% inhibition, not due to metal removal
-
complete inhibition at 5 mM
-
weak, 2-mercaptoethanol partially protects
-
5 mM causes near full inactivation in 1.5 h
-
complete inactivation at 2 mM, no reversal by addition of metal ions, m-phenanthroline no effect
-
complete inactivation at 2 mM, partial reactivation by divalent cations
-
60-90% inhibition at 0.1 mM, reversal by FeSO4
-
complete inhibition, recovered by the subsequent supplementation with Zn2+
-
complete inhibition, reversible by addition of Fe2+, Mn2+, or Co2+
-
partial reactivation by Zn2+
-
10 mM, 4.5% residual activity
-
competitive with L-rhamnulose 1-phosphate or glycerone phosphate; noncompetitive with L-lactaldehyde
-
competitive with L-rhamnulose 1-phosphate or glycerone phosphate
-
the enzyme is completely inhibited by the presence of 2 mM o-phenanthroline
-
40% residual activity at 0.1 mM
-
43% activity after 4 h at 4 mM
-
not m-Phenanthroline, probably acts as metal chelator
-
1 mM, complete inhibition, CuCl2 restores, CoCl2 and ZnCl2 partially restore activity; strong
-
16% inhibition at 0.1 mM
-
loss of activity within 5 min in the presence of 40 mM pseudouridine synthetase Pus1
-
39% reduced activity at 1 mM
-
5 mM, 75% residual activity
-
weak, 20% inhibition at 10 mM
-
24% loss of activity in the deamination reaction of L-threo-3-methylaspartate
-
20 mM, complete inactivation
-
10 mM, almost complete inhibition
-
reactivation by Mg2+, Mn2+ or Ca2+
-
2 mM, approx. 50% inactivation after 10 min, almost complete inhibition after 180 min
-
decreases GloA3 activity
-
inhibition after enzyme dialysis against 0.001 M o-phenanthroline
-
reversible, noncompetitive
-
10% residual activity at 3 mM
-
little or no inhibition by 1,7-phenanthroline and 4,7-phenanthroline
-
complete inhibition of the cytoplasmic isozyme at 1 mM
-
ATP protects the enzyme against zinc removal
-
inactivation follows pseudo-first-order kinetics, the rate of inactivation is greater at low enzyme concentrations
-
complete inhibition of Na+ transport at 0.5 mM
-
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Isolation and characterization of a novel enzyme, Nalpha-benzylxycarbonyl amino acid urethane hydrolase, from Streptococcus faecalis R ATCC 8043.
1985
Murao, S.; Matsumura, E.; Kawano, T.
Agric. Biol. Chem.
49
967-972
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Characteristics and specificity of purified N-feruloylglycine amidohydrolase from isolated barley embryos
1988
Martens, M.; Cottenie-Ruysschaert, M.; Hanselaer, R.; De Cooman, L.; Vande Casteele, K.; Van Sumere, C.F.
Phytochemistry
27
2465-2475
Purification and characterization of iron-containing urethanase from Bacillus licheniformis
1994
Zhao, C.J.; Kobashi, K.
Biol. Pharm. Bull.
17
773-778
Bovine liver dihydropyrimidine amidohydrolase: pH dependencies of inactivation by chelators and steady-state kinetic properties
1986
Lee, M.H.; Cowling, R.A.; Sander, E.G.; Pettigrew, D.W.
Arch. Biochem. Biophys.
248
368-378
Bovine liver dihydropyrimidine amidohydrolase: Purification, properties, and characterization as a zinc metalloenzyme
1983
Brooks, K.P.; Jones, E.A.; Kim, B.D.; Sander, E.G.
Arch. Biochem. Biophys.
226
469-483
-
Microbial synthesis of D-amino acids from DL-5-substituted hydantoins
1983
Takahashi, S.
Hakko Kogaku Kaishi
61
139-151
-
Purification, crystallization and properties of hydantoinase from Pseudomonas striata
1978
Takahashi, S.; Kii, Y.; Kumagai, H.; Yamada, H.
J. Ferment. Technol.
56
492-498
A thermostable hydantoinase of Bacillus stearothermophilus NS1122A: Cloning, sequencing, and high expression of the enzyme gene, and some properties of the expressed enzyme
1994
Mukohara, Y.; Ishikawa, T.; Watabe, K.; Nakamura, H.
Biosci. Biotechnol. Biochem.
58
1621-1626
beta-Lactamase (Bacillus cereus)
1975
Thatcher, D.R.
Methods Enzymol.
43
640-652
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Characterisation and sequence of the Chryseobacterium (flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile
1998
Rossolini, G.M.; Franceschini, N.; Riccio, M.L.; Mercuri, P.S.; Perilli, M.; Galleni, M.; Frere, J.M.; Amicosante,G.
Biochem. J.
332
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Purification, characterization, and kinetic studies of a soluble Bacteroides fragilis metallo-beta-lactamase that provides multiple antibiotic resistance
1998
Wang, Z.; Benkovic, S.
J. Biol. Chem.
273
22402-22408
Biochemical characterization of the carbapenem-hydrolyzing beta-lactamse AsbM1 from Aeromonas sobria AER 14M; a member of a novel subgroup of metallo-beta-lactamases
1996
Yang, A.; Bush, K.
FEMS Microbiol. Lett.
137
193-200
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Guanidinoacetate amidinohydrolase from a Flavobacterium. Purification, crystallization and properties
1979
Yorifuji, T.; Komaki, N.; Oketani, K.; Entani, E.
Agric. Biol. Chem.
43
55-62
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Purification and some properties of guanidinoacetate amidinohydrolase produced by Corynebacterium sp.
1986
Shirokane, Y.; Nakayima, M.
J. Ferment. Technol.
64
29-36
Guanidinobutyrase for L-arginine degradation in Brevibacterium helvolum
1992
Yorifuji, T.; Shimizu, E.; Hirata, H.; Imada, K.; Katsumi, T.; Sawamura, S.
Biosci. Biotechnol. Biochem.
56
773-777
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Purification and properties of cytosine deaminase from Aspergillus fumigatus
1991
Yu, T.S.; Kim, J.K.; Kasuragi, T.; Sakai, T.; Tonomura, K.
J. Ferment. Bioeng.
72
266-269
Cytosine deaminase the roles of divalent metal ions in catalysis
1993
Porter, D.J.T.; Austin, E.A.
J. Biol. Chem.
268
24005-24011
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Chemical modification of cytosine deaminase from Aspergillus fumigatus
1998
Yu, T.S.; Kim, J.; Kim, H.S.
J. Microbiol.
36
39-42
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Chemical modification of extracellular cytosine deaminase from Chromobacterium violaceum YK 391
1998
Kim, T.H.; Yu, T.S.
J. Microbiol. Biotechnol.
8
581-587
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Purification and characterization of extracellular adenosine deaminase from a Streptomyces sp.
1991
Jun, H.K.; Kim, T.S.; Sakai, T.
J. Ferment. Bioeng.
71
6-11
Purification and charaterization of an extracellular adenosine deaminase from Nocardioides sp. J-326TK
1994
Jun, H.K.; Yeeh, Y.
Biotechnol. Appl. Biochem.
20
265-277
Human placenta cytidine deaminase: A zinc metalloprotein
1997
Vincenzetti, S.; Cambi, A.; Balducci, E.; Natalini, P.; Volpini, R.; Vita, A.
Biochemistry
42
469-476
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Asymmetric hydrolysis of alpha-aminonitriles to optically active amino acids by a nitrilase of Rhodococcus rhodochrous PA-34
1992
Bhalla, T.C.; Miura, A.; Wakamoto, A.; Ohba, Y.; Furuhashi, K.
Appl. Microbiol. Biotechnol.
37
184-190
-
Studies on nucleotidases in plants: Part II - Isolation and properties of an enzyme hydrolyzing FAD at alkaline pH from mung bean seedlings (Phaseolus radiatus)
1968
Ravindranath, S.D.; Rao, N.A.
Indian J. Biochem.
5
137-142
Purification and characterization of flavine-adenine dinucleotide phosphohydrolase from rat liver lysosomal membranes
1993
Kim, J.K.; Ezaki, J.; Himeno, M.; Kato, K.
J. Biochem.
114
126-131
Flavin adenine dinucleotide and flavin mononucleotide metabolism in rat liver: The occurrence of FAD pyrophosphatase and FMN phosphohydrolase in isolated mitochondria
1997
Barile, M.; Brizio, C.; de Virgilio, C.; Delfine, S.; Quagliariello, E.; Passarella, S.
Eur. J. Biochem.
249
777-785
Deoxyuridine triphosphatase: a potential site of interaction with pyrimidine nucleotide analogues
1982
Ingraham, H.A.; Goulian, M.
Biochem. Biophys. Res. Commun.
109
746-752
Drosophila deoxyuridine triphosphatase. Purification and characterization
1987
Giroir, L.E.; Deutsch, W.A.
J. Biol. Chem.
262
130-134
Purification and characterization of the vaccinia virus deoxyuridine triphosphatase expressed in Escherichia coli
1996
Roseman, N.A.; Evans, R.K.; Mayer, E.L.; Rossi, M.A.; Slabaugh, M.B.
J. Biol. Chem.
271
23506-23511
Purification and characterization of nucleoside diphosphatase from rat-liver microsomes. Evidence for metalloenzyme and glycoprotein
1980
Ohkubo, I.; Ishibashi, T.; Taniguchi, N.; Makita, A.
Eur. J. Biochem.
112
111-118
Mechanism of porphobilinogen synthase. Requirement of Zn2+ for enzyme activity
1980
Bevan, D.R.; Bodlaender, P.; Shemin, D.
J. Biol. Chem.
255
2030-2035
The metalloprotein nature of Ustilago delta-aminolevulinate dehydratase
1969
Komai, H.; Neilands, J.B.
Biochim. Biophys. Acta
171
311-320
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