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1 mM, 51.9% residual activity; 1 mM, 68.7% residual activity
-
1 mM, 19% residual activity
-
complete inhibition at 1 mM
-
1 mM: weak, 100 mM: strong
-
1 mM, 51.9% residual activity; 1 mM, 68.7% residual activity
-
0-15% inactivation at 1 mM
-
inhibition of activity at 10 mM
-
slight inhibition at 1 mM
-
0.1 mM and 1.0 mM, weak inhibition
-
activates enzyme MGR I, slightly inhibits enzyme MGR II
-
about 68.1% residual activity at 1 mM
-
about 64.3% residual activity at 1 mM
-
5 mM, inhibition by less than 30%
-
1 mM, about 50% inhibition
-
79.5% residual activity at 1 mM
-
about 90% activity at 0.5 mM
-
92% inhibition in presence of 5 mM Mg2+
-
46.47% relative activity at 2 mM
-
more than 50% inhibition at 20 mM
-
competitive, 60% inhibition at 0.01 mM
-
6.8% residual activity at 1 mM
-
80.5% inhibition at 1 mM
-
0.02 mM, 75% inhibition
-
88% residual activity at 1 mM
-
91% residual activity at 100 mM
-
35% residual activity at 10 mM
-
1 mM, 51% of inhibition
-
61.9% residual activity at 20 mM
-
75.3% residual activity at 01 mM
-
inhibits the enzyme activity at 100 mM but increases it at 12.5-50 mM
-
1 mM, complete inhibition
-
1.25 mM, 3% inhibition. 10 mM, 17% inhibition
-
5 mM, 67% loss of activity
-
significantly inhibition
-
at concentrations below 4 mM in presence of H2O2 competitive inhibitor to Mn2+, slightly stimulates NaN3 or alkylhydrazine inactivation
-
competitive inhibitor to Mn2+
-
5 mM, 80% of initial activity
-
about 56% inhibition at 1 mM
-
partial inhibition of catalase activity
-
1 mM, 25% residual activity
-
partial inhibition at 2 mM
-
51.9% relative activity at 10 mM
-
complete inhibition at 1 mM
-
65% inhibition at 0.1 mM
-
85% inhibition at 0.1 mM
-
1 mM, 89% inhibition; complete inhibition by 0.1 mM and 1 mM
-
1 mM, complete inhibition
-
the addition of 0.005 mM Co2+ does inhibit enzyme activity to 53%
-
incubation with Fe2+ plus Co2+ in equimolar concentrations inhibits
-
abolishes enzyme activity completely at 2 mM
-
47% residual activity at 2 mM
-
2 mM abolishes enzyme activity completely
-
0.4 mM, complete inhibition
-
inhibits activity by 80-95% at 0.01-0.05 mM
-
IC50: 0.0019 mM, in the presence of Fe2+; IC50: 0.041 mM
-
competitive versus Fe2+
-
active site binding structure analysis, in both Co(II)-bound structures, in addition to the catalytic triad residues and 2-oxoglutarate or, malonate that coordinate cobalt, the remaining coordinate sites are occupied by water molecules thus forming a six-coordinate cobalt complex
-
complete inhibition competitive to Fe2+, but stabilizes the enzyme against self-inactivation in absence of proclavaminate
-
inhibition in decreasing order, Zn2+, Co2+, Ni2+
-
cobalt ions increase H3K9me3 and H3K36me3 by inhibiting histone demethylation process. Cobalt ions do not affect JMJD2A protein level but directly inhibit its demethylase activity. Exposure of both lung carcinoma A-549 cells and bronchial epithelial Beas-2B cells, to CoCl2 at 0.2 mM for 24 h increases methylation of histone H3 lysine residues 4, 9, 27 and 36, i.e. H3K4me3, H3K9me2, H3K9me3, H3K27me3, H3K36me3, as well as ubiquitination of histone H2A and H2B, while it decreases acetylation at histone H4, overview
-
more than 50% inhibition at 1 mM
-
more than 90% inhibition at 1 mM
-
95% inhibition at 0.25 mM
-
0.04 mM, about 65% inhibition
-
less than 15% activity at 1 mM
-
2 mM, 3% residual activity
2 mM, 3% residual activity
2 mM, 2% residual activity
2 mM, 2% residual activity
0.5 mM, complete inhibition
-
cobalt ions increase H3K9me3 and H3K36me3 by inhibiting histone demethylation process. cobalt ions do not affect JMJD2A protein level but directly inhibit its demethylase activity. Exposure of both lung carcinoma A549 cells and bronchial epithelial Beas-2B cells, to CoCl2 at 0.2 mM for 24 h increases methylation of histone H3 lysine residues 4, 9, 27 and 36, i.e. H3K4me3, H3K9me2, H3K9me3, H3K27me3, H3K36me3, as well as ubiquitination of histone H2A and H2B, while it decreases acetylation at histone H4, overview
-
slight effect, crude enzyme extract
-
63% residual activity at 1 mM
-
0.4 mM, significant inhibition
-
1 mM inhibits by 20%; 20% inhibition at 1 mM
-
replaced Fe2+ at the active site
replaced Fe2+ at the active site
replaced Fe2+ at the active site
replaced Fe2+ at the active site
replaced Fe2+ at the active site
replaced Fe2+ at the active site
replaced Fe2+ at the active site
replaced Fe2+ at the active site
replaced Fe2+ at the active site
replaced Fe2+ at the active site
competitive against Fe2+
-
80% inhibition at 0.1 mM
-
62.4% inhibition at 0.5 mM
-
80% inhibition at 0.1 mM
-
75% residual activity at 10 mM
-
82.73% inhhibition at 20 mM
-
inhibition in decreasing order, Zn2+, Co2+, Ni2+
-
0.4 mM, 100% inhibition
-
completely abolishes activity of WelO5 toward 12-epi-fischerindole U
-
40% inhibition at 0.1 mM
-
RNR activity chelates with copper leading to inactivation
RNR activity chelates with copper leading to inactivation
RNR activity chelates with copper leading to inactivation
RNR activity chelates with copper leading to inactivation
-
weak inhibition of the enzyme, when FAD is used as reducing cofactor
-
1 mM, isozyme A, 71% inhibition, isozyme B, 51% inhibition, complete inhibition of isozyme A from pyridoxine auxotroph mutant strain WG3
-
30-40% inhibition at 1.0 mM
-
50.3% residual activity at 1 mM
-
89.01% residual activity at 1 mM
-
complete inhibition at 1 mM
-
0.2 mM, almost complete inhibition
-
50% inhibition at 2.5 mM
-
42% residual activity at 2 mM
-
1 mM causes 18% inhibition at 30°C
-
89% residual activity at 1 mM
-
10 mM CoCl2, 78% inhibition
-
both isoforms, concentration above 3 mM
-
1 mM, 1.5% residual activity
-
inhibition of IPNS activity
-
only after preincubation with cation
-
complete inhibition at 1 mM
-
10 mM, 60% inhibition of reductive amination
-
17% inhibition at 10 mM, 23.75% at 20 mM
-
34% residual activity at 0.5 mM
-
82% activity in the presence of 1 mM Co2+
-
0.5 mM, 71% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
-
15% residual activity at 1 mM
-
there is a sharp decrease in activity when 1 mM Co2+ is added to the reaction assay
-
67% residual activity at 1 mM (pH 5.5)
-
88% residual activity at 1 mM
-
strong inhibition of both isoforms at 10 mM
-
inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
-
almost total inhibition at 0.1 mM
-
strong inhibitory effect
-
inhibitory at 1.2 mM concentration
-
1 mM, about 10% inhibition
-
strong inhibition at 1 mM
-
1 mM, strong inhibition
-
complete inhibition at 1 mM
-
GRase-1 is moderately sensitive to inhibition by Co2+
-
most powerful inhibitor, competitive inhibition
-
in sodium phosphate buffer and in Hepes buffer
-
inhibits activity by 71%, inhibition prevented by inclusion of 10 mM EDTA; inhibits TNMT activity by 71%, can be prevented by the inclusion of EDTA
-
5 mM, severe inhibition
-
5 mM, 75% inhibition; 75% inhibition at 5 mM Co2+
-
strongly inhibits, relative activity 7% of control
-
severe inhibition at 1.5 mM
-
1 mM, 20-50% inhibition
-
slight inhibition; strong inhibition
-
strong inhibition at 1 mM
-
inhibits AP3 production at 0.5-2 mM
inhibits AP3 production at 0.5-2 mM
inhibits AP3 production at 0.5-2 mM
inhibits AP3 production at 0.5-2 mM
inhibits AP3 production at 0.5-2 mM
inhibits AP3 production at 0.5-2 mM
0.1 mM, 44% residual activity
divalent cations at concentrations of more than 5 mM are inhibitory, 10 mM, total inhibition
-
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
5 mM, strong inhibition
-
5 mM, strong inhibition
-
accumulation of Co2+-protoporphyrin containing products of hemolysis
-
; 39% remaining activity isoenzyme NAT-a
-
1 mM, no inhibition at 10 mM
-
0.05 mM, 20% loss of activity
-
strong, 1 mM, even in the presence of Mn2+, wild-type
-
in the presence of Mn2+
-
10 mM CoCl2, 20% inhibition
-
strongly inhibits chitin synthase 1
-
inhibits the wild-type Chs2 and mutant Chs2DELTAN222
-
strongly inhibits the sterol glucosyltransferase activity, IC50 (mM): 1.3
-
the additon of 2.5 mM of Co2+ slightly inhibits the enzyme
-
1 mM, 21% of initial activity
-
strong inhibition at 1 mM and 10 mM
-
about 30% residual activity at 10 mM; about 35% residual activity at 10 mM
-
10 mM, 54.2% inhibition
-
1 mM, 98% inhibition with quercetin as substrate, 85% inhibition with gossypetin as substrate
-
complete inhibition near 0.04 mM, UGT71F1; complete inhibition near 0.04 mM, UGT73A4
-
divalent cation inhibit in decreasing order: Sr2+, Ni2, Co2+, Ca2+, Mn2+, Zn2+
about 90% residual activity in the presence of 2 mM
-
1 mM, 31% residual activity
-
the addition of 5 mM Co2+ reduces the activation by 5 mM MnCl2 of the enzyme by 45%; the addition of 5 mM Co2+ reduces the activation by 5 mM MnCl2 of the enzyme by 76%
-
8.2% residual activity at 5 mM
-
25 mM, 1% residual activity
-
complete inhibition at 5 mM
-
inhibition by binding to 2 types of metal ion sites, one type consists of a single site and has a low apparent affinity to Ca2+, at the remaining site(s), Ca2+ has a much higher apparent affinity than Zn2+, Ni2+ or Co2+ and prevents inhibition by these metal ions
-
1 mM, stimulates activity of enzyme N, enzyme I is inhibited
-
inhibits at high concentrations, inhibits Mn2+-activated enzyme
-
less than 20% residual activity at 2 mM
-
in the presence of Mn2+
-
0.25 mM CoCl2, 12.7% inhibition
-
inhibits Mg2+-activation
-
Co2+ reduces activity by more than 60% at 5 mM
-
59% inhibition at 10 mM
-
20 mM, 85% loss of activity
-
10 mM CoCl2, 44% inhibition
-
0.1-1 mM, complete inhibition
-
5 mM, 50-80% inhibition
-
28% inhibition at 0.1 mM
-
38.7% of activity remaining at 10 mM
-
complete inhibition at 1 mM
-
concentrations above 0.1 mM
concentrations above 0.1 mM
concentrations above 0.1 mM
concentrations above 0.1 mM
concentrations above 0.1 mM
concentrations above 0.1 mM
stabilizes at low and inhibits at higher concentrations
-
1 mM, 15% decrease of activity
-
about 45% residual activity at 10 mM
0.1 mM CoCl2, 95% inhibition
-
strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
-
20% conversion in presence of Co2+
-
3.9% conversion in presence of Co2+
-
1 mM, 49% residual activity
-
0.004 M, 80% inhibition
-
1.6 mM, 40% inhibition; 1.6 mM, 61% inhibition
-
in excess, activating below
-
at physiological pH, activating below
-
complete inhibition at 20 mM
-
inhibitory at high concentration
-
complete inhibition in the forward reaction, strong inhibition in the reverse reaction
-
above 30 mM, activating below 20 mM
above 30 mM, activating below 20 mM
above 30 mM, activating below 20 mM
above 30 mM, activating below 20 mM
above 30 mM, activating below 20 mM
above 30 mM, activating below 20 mM
above 30 mM, activating below 20 mM
above 30 mM, activating below 20 mM
CoATP2- is the true substrate
-
77% of the activity with Mg2+
-
inhibits at high concentrations
-
complete inhibition; complete inhibition; complete inhibition
-
2 mM, 58% inhibition, even in presence of optimal Mg2+ concentrations
-
inhibits when incubated in presence of Mg2+ at the same concentration
-
20 mM in presence of 10 mM Mg2+, more than 70% inhibition
-
weak, NDP-arsenolysis or NDP/phosphate-exchange reaction
-
inhibits uridylyl removing activity
-
no effect on liver enzyme form I, 2fold activation of enzyme form from sublingual gland, inhibition of enzyme form from submandibular gland
-
in excess of diphosphate-concentration, activates at lower concentrations
-
Mn2+ or Co2+ stimulates at lower concentration, inhibition at higher concentration
-
at high concentration inhibits the phosphoenolpyruvate, pyruvate exchange reaction
-
inhibits the synthesis of s4U
-
slight inhibition at 1 mM
-
1 mM, almost complete inhibition
-
P-PST, not M-PST; P-PST, slightly inhibiting with minoxidil as substrate
-
recombinant enzyme form SULT1 ST5
-
slight inhibition at 2 mM
-
sensitive to metal ions, almost complete inhibition at 6.0 mM
-
18% inhibition at 25 mM
-
about 42% residual activity at 5 mM Co2+ after 1 h of incubation
-
1 mM, 5% inhibition. 10 mM, 27% inhibition
-
52% residual activity at 100 mM
-
56% inhibition at 0.01 mM, 24 h preincubation
-
75% residual activity at 10 mM
-
78% residual activity at 10 mM
-
72% residual activity at 10 mM
-
92.6% residual activity at 5 mM
-
complete inhibition at 1 mM
-
inhibits both isozymes TAH I and TAH II
-
at 1 mM inhibits by 71.14%
-
87.6% residual activity at 1 mM
-
39.06% residual activity at 20 mM
-
47% residual activity at 1 mM
-
10.7% residual activity at 1 mM
-
5 mM, 30 min, 70°C, pH 8.5, 65% inhibition
-
38.83% residual activity at 5 mM
-
68% residual activity at 5 mM
-
36.2% residual activity at 1 mM
-
74% relative activity at 5 mM
-
isoyzme SCO1725 shows 93% residual activity in the presence of 10 mM Co2+; isozyme SCO7513 shows 72% residual activity in the presence of 10 mM Co2+
-
36% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
-
82.7% inhibition at 50 mM
-
46.0% residual activity at 10 mM
-
about 75% inhibition at 5 mM
-
88% residual activity at 2 mM
-
can replace Ca2+, decreased activity
can replace Ca2+, decreased activity
pH 5.3: stimulates, optimal concentration: 80 mM, pH 9.3: inhibition
-
10 mM, 56% residual activity, EST1, p-nitrophenyl acetate as substrate
-
complete inhibition at 2 mM
-
1.0 mM, 68% relative residual activity
-
10 mM, acetylxylan esterase Axe6B
-
inhibits at higher (10 mM) concentrations
-
5 mM, less than 50% residual activity
-
1 mM inhibits 10% of the activity
-
no activation at 1 mM, 11% at 5 mM, but 30% inhibition at 10 mM
-
10 mM, 74% residual activtiy
-
3 mM gradually decreases activity about 78fold
-
100% inhibition by 0.01 M CoCl2
-
82% of maximal activity at 1 mM CoCl2
-
slightly inhibits the mitochondrial enzyme
-
slightly inhibits the mitochondrial enzyme
-
complete inhibition at 1 mM
-
in presence of Mg2+, inhibition
-
over 95% inhibition at 5 mM and below
-
5 mM, 20% residual activity
5 mM, 20% residual activity
1 mM: 8% of enzyme activity
-
5 mM, SAP2, 95% inhibition
5 mM, SAP2, 95% inhibition
inhibition of leaf and root nodule isozymes
inhibition of leaf and root nodule isozymes
inhibits hydrolysis of inositol-1-phosphate at high concentrations
-
50% inhibition at 0.7 mM
-
0.1 mM-1 mM, slight inhibition
-
60% inhibition at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
slight inhibitory effect
-
1 mM, slight inhibition
-
IC50: 0.029 mM, reaction with phosphatidic acid. IC50: 1.1 mM, reaction with diacylglycerol diphosphate. IC50: 1.2 mM, reaction with lysophosphatidic acid
-
0.1 mM activate, 4 mM inhibit, plasma membrane enzyme
-
strong, enzyme from glioblastoma cells
-
inhibition of cytosolic and membrane-bound enzyme
-
0.1 mM-1 mM, slight inhibition
-
60% inhibition at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
76.08% residual activity at 5 mM
-
1 mM, 43% residual activity
-
almost complete inhibition of 3'-AMP hydrolysis by 1 mM CoCl2
-
isozyme Nuc1 shows 79% activity at 5 mM concentration
isozyme Nuc1 shows 79% activity at 5 mM concentration
FS-44: 5'-PDase activity of bifunctional enzyme: cyclic-ribonucleotide phosphomutase-5'-phosphodiesterase
-
inhibits at concentrations higher than optimal
-
inhibits at higher concentrations
-
PdeA and PdeB are inhibited (20-30%) at 0.25 mM Co2+
-
80.6% inhibition at 2 mM
-
1 mM, 50-60% inhibition
-
2.5 mM, complete loss of both hydrolytic activity and transphosphatidylation
-
1.0 mM, complete inhibition of isoenzyme PII, 21% inhibition of isoenzyme PI
-
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
; plasma enzyme more sensitive than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
plasma enzyme more resistant than liver enzyme
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
at 37°C, 1 mM reduces activity by 30%
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
competitive inhibition of isoenzyme Q192 and R192
18% inhibition at 0.1 mM
-
5 mM CoCl2, 91% inhibition
-
1 mM, 17% loss of activity
-
1 mM CoCl2, 65% loss of activity
-
slight activation of isozyme AI-2, slight inhibition of isozymes AI-1 and AII
-
1 mM, pH 8.0, 24 h at 4°C, 92% and 93% residual activity for Amy I and Amy II, respectively
-
1 mM, 37°C, 30 min, pH 6.5, 23% relative activity
-
; 16% residual activity at 5 mM
-
complete inhibition at 1 mM
-
70% residual activity at 10 mM
-
96% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
-
potent inhibitor, inhibition reversed by adding an excess of dithiothreitol
-
1 mM, 61% residual activity
-
50% reduction in alpha-mannosidase activity is observed after addition of 3 mM CoCl2
-
53% residual activity at 10 mM
-
about 60% residual activity at 1 mM
about 60% residual activity at 1 mM
about 60% residual activity at 1 mM
about 60% residual activity at 1 mM
about 60% residual activity at 1 mM
1 mM inhibits by 86%, with colloidal chitosan as substrate
-
38% residual activity at 10 mM
-
the enzyme is inhibited by 23% at 5 mM
-
about 1.1% residual activity at 10 mM
-
about 13% residual activity at 5 mM
-
1 mM, 22% inhibition of VpChiA, 15% inhibition of mutant enzyme VpChiAG589
inhibits slightly at 10 mM
inhibits at 13% at 0.5 mM, 14% at 2 mM
13% inhibition at 10 mM, no effect at 5 mM
1 mM, 80% of initial activity
2 mM, 15% of initial activtiy
-
1 mM, CoCl2, 27% inhibition
-
1 mM CoNO3, 66% inhibition
-
1mM completely inhibits
-
1 mM, 37% loss of activity
-
10 mM, slight inhibition
-
1 mM, pH 5.0, 95°C, 24% inhibition of hydrolysis of 4-nitrophenyl alpha-D-glucopyranoside
-
50% inhibition at 8.5 mM
-
notable inhibition at 10 mM
-
nearly complete inhibition at 1 mM
-
2 mM, 72% residual activity
-
10 mM, 85% residual activity
-
5 mM, 58% residual activity
-
slight inhibition at 10 mM
-
complete inhibition at 10 mM
-
1.5 mM, complete inhibition
-
10 mM CoCl2, 5% inhibition
-
2.5 mM CoCl2, inhibits hydrolysis of lactose and transferase activity
-
slight inhibition at 1 mM
-
slight inhibition at 10 mM
-
inhibition of alpha-mannosidases IA and IB
-
51% inhibition at 10 mM
-
10-30% inhibition for acid alpha-mannosidase
-
1.5 mM, 80% residual activity
-
1 mM, 12% loss of activity
-
2 mM, 64% residual activity
-
63.5% residual activity at 10 mM
-
1 mM, 15% of initial activity
-
10 mM, 20.4% residual activity
-
74.96% residual activity at 10 mM
-
50% inhibition at 50 mM for beta-D-fucosidase I, 22% inhibition for beta-D-fucosidase II
-
slight inhibition at 1 mM
-
1 mM, 40-50% inhibition
-
94% residual activity at 10 mM
-
80.8% residual activity at 1 mM
-
1 mM CoCl2, 44% inhibition
5 mM, 37% residual activity
5 mM, 90% of initial activity
5 mM, 76% residual activity
10 mM, almost 30% loss of activity
1 mM, 62% residual activity
5 mM, 43% of initial activity
2 mM, less than 50% of initial activity
1 mM, represses the enzyme activity up to 37%
5 mM, at least 60% inhibition
-
1 mM, 18% residual activity
-
2 mM, 15% of initial activtiy
-
complete inhibition at 5 mM
-
10 mM cause 37% inhibition
-
90% residual activity at 1 mM
-
54.4% residual activity at 1 mM
-
almost complete inhibition at 1 mM
-
75% inhibition at 20 mM
-
5 mM, 25.4% residual activity
-
10 mM, 16.9% residual activity
-
39% residual activity at 5 mM
-
76.5% inhibition at 5 mM
-
5 mM, 70% residual actvity
-
5 mM, 70% residual activity
-
F1 and F2 form 47% inhibition
-
about 18% residual activity at 1 mM
-
at 1 mM 19% inhibition, at 5 mM 45% inhibition
-
7% inhibition at 10 mM, 7% activation at 2 mM
-
1 mM, strong inhibition
-
82.19% residual activity at 1 mM
-
6% inhibition at 10 mM, 16% at 1 mM
-
inhibits isozyme EG1 by 35%, and isozyme EG2 also slightly, at 2.5 mM
-
5 mM, 50% residual activity
-
1 mM, 50% loss of activity
-
2.5 mM, 42% residual activity
-
63% residual activity at 5 mM
10 mM reduces the enzyme activity by 26.1%
10 mM partially inhibits the activity of XynAS27
inhibits hydrolysis activity
in the presence of 10 mM, the relative xylanase activity decreases by 5%
complete inhibition of xylanase II at 10 mM, 50% at 2 mM, no inhibition of xylanase I
strong inhibition of XYN10G at 1 mM
10 mM, activity decreased to 60%
1 mM, 64% residual activity
10 mM, more than 80% inhibition
30 min at 30ºC, 10 mM, 70% inhibition; 30 min at 30ºC, 1 mM, 17% inhibition; 30 min at 30ºC, 5 mM, 39% inhibition
-
complete inhibition at 1 mM
-
almost complete inhibition at 1 mM
-
13.2% residual activity at 10 mM
-
moderate inhibition at 1 mM
-
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
very slight inactivation
-
about 70% residual activity at 5 mM
-
82% residual activity at 1 mM
-
complete inhibition at 1 mM
-
about 30% residual activity at 1 mM
-
complete inhibition at 2mM
-
at 1 mM, isoforms agarase-a and agarase-b show 81.31% and 91.81% residual activity, respectively
-
24.2% residual activity at 0.1 M using inosine as substrate, 25.8% residual activity at 0.1 M using guanosine as substrate, 33.3% residual activity at 0.1 M using adenosine as substrate
-
complete inhibition at 5 mM
-
inhibition of Mg2+-dependent acrtivity
-
reversible by addition of EDTA
-
39% activation at 2 mM, 40% inhibition at 10 mM
-
activates at 2 mM, inhibits at 10 mM and above
-
0.1 mM, 86% loss of activity
-
1 mM, complete inhibition
-
25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited, IC50: 0.1 mM
65-90% inhibition at 1 mM
-
7-DMATS, FgaPT1, and CdpNPT show 10.2%, 32.3%, and 46.9% relative activity at 5 mM Co2+, respectively
-
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% inhibition
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
inhibitory above 0.0625 mM, activating below
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
1 mM, 50% residual activity
-
68% inhibition at 0.2 mM
-
50-60% inhibition at 1 mM
-
2% residual activity in the presence of 1 mM; 98% inhibition at 1 mM
-
66% inhibition at 0.03 mM
-
reverses EDTA inhibition
-
at high concentration inhibition
-
0.1 mM CoCl2, 23% inhibition
-
inhibits Cd2+-saturated enzyme, inhibits the Ni2+-saturated enzyme
-
strong inhibition at 1 mM
-
1.5 mM CoCl2, complete inhibition
-
1 mM CoCl2, 90% inhibition
-
only inhibits Mn2+-activated enzyme
-
stimulatory at 0.01 mM, inhibitory above 0.1 mM
-
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
-
stimulation of enzyme activity at 0.4 mM, inhibition at 4 mM
-
when substrates are cleaved rapidly by dipeptidase, addition of Co2+ inhibits the reaction. The more slowly a substrate is hydrolyzed in the absence of metals, the greater the activating effect
-
hydrolysis of the relative poor substrates, Pro-Gly and Gly-Gly is activated, whereas that of Ala-Gly is inhibited
-
activation up to 50% at 0.001-0.0001 mM, inbhibitory above 0.002 mM
-
testicular enzyme is inhibited, lung enzyme not
-
at 0.01 mM 59.7% activity relative to control
-
hydrolysis of hippuryl-L-Arg
-
48% residual activity at 0.2 mM
-
at 37°C and pH of 7.5, 1 mM reduces prosubtilisin JB1 relative activity to 14% and 5 mM reduces prosubtilisin JB1 relative activity to 24%
-
some inhibition at 1 mM
-
about 10% inhibition at 5 mM
-
inhibition of amidolytic activity
-
competitive to other metal ions
-
order of decreasing inhibitory effect: Cu2+, Hg2+, Zn2+, Ni2+, Co2+, 50% inhibition at 0.25 mM
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
-
complete inhibition at 1 mM
-
8.01% residual activity at 5 mM
-
58.88% residual activity at 5 mM
-
5.09% residual activity at 5 mM
-
6.85% residual activity at 5 mM
-
5 mM, inhibits in presence of 5 mM Ca2+
-
5 mM, completely blocks activation of the enzyme by Ca2+
-
0.01 mM, 50% inhibition
-
inhibits 74% at 0.2 mM and precipitates the enzyme at 1 mM
-
20% inhibition at 0.01 mM
-
10 mM, complete inhibition
-
0.1 mM, caseinolytic activity
-
50% inhibition at 0.625 mM
-
increases the activity 3-4fold at up to 2 mM, but inhibits at 2-18 mM, activation-and-inhibition dual effects of Co2+ ion are analysed kinetically
competitive, 72% inhibition at 18 mM, partial protection or reverse effect by Ca2+ at 0.5 mM, Co2+ show partly Ca2+-sensitive and partly Ca2+-insensitive inhibition, molecular mechanism, Co21 accelerates the autolysis, overview
30% activation at 8 mM, 40% inhibition at 10 mM
-
protease II inactive in presence of, protease I slightly stimulated
-
above 1-2 mM, native or apoenzyme
-
1 mM, complete inhibition
-
specific strong inhibition
-
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