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1 mM, 19% residual activity
1 mM, 51.9% of initial activity
32.0% inhibition at 1.0 mM
complete inhibition at 1 mM
-
1 mM: weak, 100 mM: strong
-
75.3% residual activity at 1 mM
-
81.9% residual activity at 1 mM
-
70.7% residual activity in the presence of Co2+
-
1 mM, 51.9% residual activity; 1 mM, 68.7% residual activity
-
1 mM, 68.7% of initial activity
-
0-15% inactivation at 1 mM
-
1 mM, 81.9% residual activity
-
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 64.3% residual activity at 1 mM
-
about 68.1% residual activity at 1 mM
-
5 mM, inhibition by less than 30%
-
1 mM, about 50% inhibition
-
24.7% inhibition at 1 mM
-
79.5% residual activity at 1 mM
-
about 90% activity at 0.5 mM
-
5.2% residual activity at 2 mM
-
5.96% residual activity at 2 mM
-
8.7% residual activity at 2 mM
-
46.47% relative activity at 2 mM
-
8.9% residual activity at 2 mM
-
92% inhibition in presence of 5 mM Mg2+
-
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
-
1 mM complete inhibition
-
5 mM, complete inhibition of activity
-
5 mM, complete inhibition; 5 mM, complete inhibition of activity
-
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
-
1 mM, complete inhibition
-
1.25 mM, 3% inhibition. 10 mM, 17% inhibition
-
10 mM, 99% loss of activity
-
5 mM, 67% loss of activity
-
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
-
significantly inhibition
-
inhibits the enzyme at 1-10 mM
-
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
-
66% residual activity at 5 mM
-
about 56% inhibition at 1 mM
-
1 mM, 25% residual activity
-
partial inhibition of catalase activity
-
partial inhibition at 2 mM
-
1 mM, slight inhibition
-
10 mM, 17% loss of activity, isoenzyme FP2; 10 mM, 42% loss of activity, isoenzyme FP1; 10 mM, 53% loss of activity, isoenzyme FP3
-
5 mM, 79% inhibition of cationic peroxidase GCP1. 5 mM, 20% inhibition of anionic peroxidase GCP2
-
51.9% relative activity at 10 mM
-
1.3 mM, 30 min, 24% loss of activity
-
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
-
1 mM, moderately inhibited
-
the addition of 0.005 mM Co2+ does inhibit enzyme activity to 53%
-
incubation with Fe2+ plus Co2+ in equimolar concentrations inhibits
-
47% residual activity at 2 mM
-
abolishes enzyme activity completely at 2 mM
-
2 mM abolishes enzyme activity completely
-
1 mM, 40% of initial activity
-
about 80% residual activity at 10 mM
-
0.4 mM, complete inhibition
-
IC50: 0.0019 mM, in the presence of Fe2+; IC50: 0.041 mM
-
inhibits activity by 80-95% at 0.01-0.05 mM
-
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
-
competitive versus Fe2+
-
complete inhibition competitive to Fe2+, but stabilizes the enzyme against self-inactivation in absence of proclavaminate
-
inhibition in decreasing order, Zn2+, Co2+, Ni2+
-
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
-
more than 50% decrease in activity
-
2 mM, 2% residual activity
-
2 mM, 3% residual activity
-
0.5 mM, complete inhibition
-
has an activating on multiple histone modifications at the global level. Cobalt ions significantly increase global histone H3K4me3, H3K9me2, H3K9me3, H3K27me3 and H3K36me3, as well as uH2A and uH2B and decreases acetylation at histone H4 (AcH4) in vivo. Cobalt ions increase H3K9me3 and H3K36me3 by inhibiting histone demethylation process in vivo. And cobalt ions directly inhibit demethylase activity of JMJD2A in vitro. Cobalt ions do not increase the level of uH2A in the in vitro histone ubiquitinating assay and inhibit histone-deubiquitinating enzyme activity in vitro
-
has an activating on multiple histone modifications at the global level. Cobalt ions significantly increase global histone H3K4me3, H3K9me2, H3K9me3, H3K27me3 and H3K36me3, as well as uH2A and uH2B and decreases acetylation at histone H4 (AcH4) in vivo. Cobalt ions increase H3K9me3 and H3K36me3 by inhibiting histone demethylation process in vivo. And cobalt ions directly inhibit demethylase activity of JMJD2A in vitro. Cobalt ions do not increase the level of uH2A in the in vitro histone ubiquitinating assay and inhibit histone-deubiquitinating enzyme activity in vitro
-
inhibits the enzyme activity at 0.5 mM by about 30%
-
1 mM, 80% residual activity
-
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
80% inhibition at 0.1 mM
-
competitive against Fe2+
-
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
-
about 20% residual activity at 5 mM
-
complete inhibition at 1 mM
-
1 mM, 1.5% residual activity
-
inhibition of IPNS activity
-
1 mM, 14.2% loss of 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
-
complete inhibition at 10 mM, 27% at 0.1 mM
-
34% residual activity at 0.5 mM
-
0.1 mM, 77% residual activity; 23% inhibition at 0.1 mM
-
82% activity in the presence of 1 mM Co2+
-
34% residual activity at 0.5 mM
-
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
-
2 mM, 15% loss of activity
-
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
-
53% residual activity at 2 mM
-
20 mM, 14% residual activity
-
inhibitory at 1.2 mM concentration
-
strong inhibitory effect
-
1 mM, about 10% inhibition
-
strong inhibition at 1 mM
-
1 mM, strong inhibition
-
77% residual activity at 1 mM
-
complete inhibition at 1 mM
-
GRase-1 is moderately sensitive to inhibition by Co2+
-
most powerful inhibitor, competitive inhibition
-
1 mM, 66.3% residual activity
-
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+
-
complete inhibition at 20 mM
-
about 20 % residual activity at 5 mM
-
strongly inhibits, relative activity 7% of control
-
severe inhibition at 1.5 mM
-
1 mM, 20-50% inhibition
-
complete loss of activity
-
60.03% residual activity at 1 mM
-
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
-
inhibits the free enzyme by about 70% and the immobilized enzyme by about 15% at 5 mM
-
2 mM, 50% residual activity
-
1 mM, no inhibition at 10 mM
-
complete inhibition at 1 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
-
inhibits the wild-type Chs2 and mutant Chs2DELTAN222
-
strongly inhibits chitin synthase 1
-
strongly inhibits the sterol glucosyltransferase activity, IC50 (mM): 1.3
-
42.7% residual activity at 1 mM
-
the additon of 2.5 mM of Co2+ slightly inhibits the enzyme
-
the wild type enzyme shows complete inhibition at 3 mM. The C-terminally truncated enzyme shows about 28% residual activity at 10 mM
-
1 mM, 21% of initial activity
-
87.8% residual activity at 5 mM
-
about 70% residual activity at 10 mM
-
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
-
about 68% residual activity at 5 mM
-
1 mM, stimulates activity of enzyme N, enzyme I is inhibited
-
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
-
inhibits at high concentrations, inhibits Mn2+-activated enzyme
-
less than 20% residual activity at 2 mM
-
in the presence of Mn2+
-
less than 4% activity in the presence of Co2+ions
-
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
-
strong inhibition at 5 mM
-
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
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
-
the enzyme shows clearly reduced activity (11.5%) with Co2+
-
in excess, activating below
-
at physiological pH, activating below
-
complete inhibition at 20 mM
-
complete inhibition in the forward reaction, strong inhibition in the reverse reaction
-
inhibitory at high concentration
-
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
65% residual activity in the presence of 4 mM
-
77% of the activity with Mg2+
-
CoATP2- is the true substrate
-
inhibits at high concentrations
-
complete inhibition; complete inhibition; complete inhibition
-
2 mM, 58% inhibition, even in presence of optimal Mg2+ concentrations
-
20 mM in presence of 10 mM Mg2+, more than 70% inhibition
-
inhibits when incubated in presence of Mg2+ at the same concentration
-
weak, NDP-arsenolysis or NDP/phosphate-exchange reaction
-
inhibits uridylyl removing activity
-
in excess of diphosphate-concentration, activates at lower concentrations
-
no effect on liver enzyme form I, 2fold activation of enzyme form from sublingual gland, inhibition of enzyme form from submandibular gland
-
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
-
1 mM, 5% inhibition. 10 mM, 27% inhibition
-
18% inhibition at 25 mM
-
about 42% residual activity at 5 mM Co2+ after 1 h of incubation
-
52% residual activity at 100 mM
-
56% inhibition at 0.01 mM, 24 h preincubation
-
72% residual activity at 10 mM
-
75% residual activity at 10 mM
-
78% residual activity at 10 mM
-
92.6% residual activity at 5 mM
-
25% inhibition at 10 mM
-
39.06% residual activity at 20 mM
-
87.6% residual activity at 1 mM
-
at 1 mM inhibits by 71.14%
-
complete inhibition at 1 mM
-
inhibits both isozymes TAH I and TAH II
-
47% residual activity at 1 mM
-
10.7% residual activity at 1 mM
-
36% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
-
36.2% residual activity at 1 mM
-
38.83% residual activity at 5 mM
-
46.0% residual activity at 10 mM
-
5 mM, 30 min, 70°C, pH 8.5, 65% inhibition
-
68% residual activity at 5 mM
-
74% relative activity at 5 mM
-
82.7% inhibition at 50 mM
-
88% residual activity at 2 mM
-
about 75% inhibition 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+
-
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
5 mM, less than 50% residual activity
inhibits at higher (10 mM) concentrations
1 mM inhibits 10% of the activity
-
10 mM, 74% residual activtiy
-
no activation at 1 mM, 11% at 5 mM, but 30% inhibition at 10 mM
-
significant inhibition of the intracellular enzyme, and slight inhibition of extracellular enzyme at 5 mM
-
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
50% inhibition at 0.7 mM
-
inhibits hydrolysis of inositol-1-phosphate at high concentrations
-
0.1 mM-1 mM, slight inhibition
-
1 mM, slight inhibition
-
16% inhibition at 5 mM, 49% at 10 mM
-
4.5% inhibition at 1 mM
-
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
-
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
0.1 mM activate, 4 mM inhibit, plasma membrane enzyme
inhibition of cytosolic and membrane-bound enzyme
inhibition of cytosolic and membrane-bound enzyme
strong, enzyme from glioblastoma cells
strong, enzyme from glioblastoma cells
0.1 mM-1 mM, slight inhibition
-
1 mM, 43% residual activity
-
16% inhibition at 5 mM, 49% at 10 mM
-
4.5% inhibition at 1 mM
-
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
-
about 69% inhibition at 1 mM, 83% at 5 mM
-
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
-
5 mM, complete loss of activity
5 mM, complete loss of activity
activating at 0.05 mM, higly inhibitory above 5 mM
activating at 0.05 mM, higly inhibitory above 5 mM
68.7% residual activity at 10 mM
-
1.0 mM, complete inhibition of isoenzyme PII, 21% inhibition of isoenzyme PI
-
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%
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
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
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
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 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 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
18% inhibition at 0.1 mM
-
1 mM CoCl2, 65% loss of activity
-
1 mM, 17% loss of activity
-
1 mM, 37°C, 30 min, pH 6.5, 23% relative activity
-
1 mM, pH 8.0, 24 h at 4°C, 92% and 93% residual activity for Amy I and Amy II, respectively
-
11.1% inhibition at 1 mM, 89.4% at 5 mM
-
16% residual activity at 5 mM
-
27% inhibition at 1 mM, 68% at 10 mM
-
47% inhibition of wild-type and mutant enzymes at 5 mM
-
5 mM CoCl2, 91% inhibition
-
70% residual activity at 10 mM
-
75.9% inhibition at 1 mM
-
complete inhibition at 1 mM
-
slight activation of isozyme AI-2, slight inhibition of isozymes AI-1 and AII
-
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
-
72.51% residual activity at 10 mM
-
2 mM, strong inhibition
-
10 mM, 47% loss of activity
-
53% residual activity at 10 mM
-
about 60% residual activity at 1 mM
-
0.5 mM, about 60% loss of activity
-
1 mM inhibits by 86%, with colloidal chitosan as substrate
-
38% residual activity at 10 mM
-
5 mM, 61% loss of activity
-
about 1.1% residual activity at 10 mM
-
about 13% residual activity at 5 mM
-
the enzyme is inhibited by 23% at 5 mM
-
1 mM, 22% inhibition of VpChiA, 15% inhibition of mutant enzyme VpChiAG589
1 mM, 80% of initial activity
13% inhibition at 10 mM, no effect at 5 mM
78% residual activity at 1 mM
inhibits at 13% at 0.5 mM, 14% at 2 mM
inhibits slightly at 10 mM
2 mM, 15% of initial activtiy
-
1 mM CoNO3, 66% inhibition
-
1 mM, CoCl2, 27% inhibition
-
0.31% residual activity at 2 mM
-
1mM completely inhibits
-
70.6% residual activity at 2 mM
-
98.4% residual activity at 5 mM
-
about 75% residual activity at 1 mM
-
slight inhibition at 1-5 mM
-
32% residual activity at 1 mM
-
4.8% residual activity at 10 mg/ml
-
isoforms Am0705 and Am2085 show complete inhibition at 2 mM Co2+, whereas isoforms Am0707 and Am1757 can maintain more than 60% of their enzymatic activities
-
1 mM, 37% loss of activity
-
1 mM, pH 5.0, 95°C, 24% inhibition of hydrolysis of 4-nitrophenyl alpha-D-glucopyranoside
-
10 mM, slight inhibition
-
47% residual activity at 5 mM
-
weak inhibition at 5 mM
-
50% reduction in alpha-mannosidase activity is observed after addition of 3 mM CoCl2
-
10 mM, 85% residual activity
-
2 mM, 72% residual activity
-
4% residual activity at 5 mM
-
5 mM, 58% residual activity
-
50% inhibition at 8.5 mM
-
nearly complete inhibition at 1 mM
-
notable inhibition at 10 mM
-
complete inhibition at 10 mM
-
slight 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
-
10-30% inhibition for acid alpha-mannosidase
-
51% inhibition at 10 mM
-
inhibition of alpha-mannosidases IA and IB
-
slight inhibition at 1 mM
-
slight inhibition at 10 mM
-
1 mM, 12% loss of activity
-
1.5 mM, 80% residual activity
-
2 mM, 64% residual activity
-
5 mM, 56% loss of activity
-
63.5% residual activity at 10 mM
-
5 mM, 58% loss of activity
-
complete inhibition at 1-5 mM
-
1 mM, activation to 102% of control. 10 mM, 71% loss of activity
-
10 mM, 32% loss of activity
-
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
-
1 mM, 40-50% inhibition
-
80.8% residual activity at 1 mM
-
94% residual activity at 10 mM
-
slight inhibition at 1 mM
-
1 mM CoCl2, 44% inhibition
1 mM, 62% residual activity
1 mM, represses the enzyme activity up to 37%
10 mM, almost 30% loss of activity
10.1% inhibition at 10 mM
2 mM, less than 50% of initial activity
5 mM, 2% loss of activity, substrate: xylan
5 mM, 37% residual activity
5 mM, 43% of initial activity
5 mM, 76% residual activity
5 mM, 90% of initial activity
activates 38% at 2 mM, inhibits 20% at 10 mM
10 mM, 17% loss of activity
-
2 mM, 36% loss of activity
-
1 mM, 18% residual activity
-
2 mM, 15% of initial activtiy
-
5 mM, at least 60% inhibition
-
complete inhibition at 5 mM
-
1 mM, 61% loss of activity
-
10 mM cause 37% inhibition
-
about 90% residual activity at 1 mM
-
10 mM, 16.9% residual activity
-
39% residual activity at 5 mM
-
5 mM, 25.4% residual activity
-
54.4% residual activity at 1 mM
-
75% inhibition at 20 mM
-
90% residual activity at 1 mM
-
almost complete inhibition at 1 mM
-
5 mM, 70% residual activity
-
76.5% inhibition at 5 mM
-
F1 and F2 form 47% inhibition
-
about 18% residual activity at 1 mM
-
0.8fold decrease of activity at 10 mM
-
36% residual activity at 4 mM
-
7% inhibition at 10 mM, 7% activation at 2 mM
-
80% residual activity at 1 mM
-
87.23% residual activity at 10 mM
-
at 1 mM 19% inhibition, at 5 mM 45% inhibition
-
1 mM, strong inhibition
-
43% inhibition at 10 mM
-
5 mM, 50% residual activity
-
6% inhibition at 10 mM, 16% at 1 mM
-
82.19% residual activity at 1 mM
-
inhibits isozyme EG1 by 35%, and isozyme EG2 also slightly, at 2.5 mM
-
90% residual activity at 5 mM
-
70.9% residual activity at 1 mM
-
1 mM, 50% loss of activity
-
2.5 mM, 42% residual activity
-
32% residual activity at 1 mM
-
about 90% residual activity at 1 mM
-
1 mM, 64% residual activity
10 mM partially inhibits the activity of XynAS27
10 mM reduces the enzyme activity by 26.1%
10 mM, activity decreased to 60%
10 mM, more than 80% inhibition
5 mM, 2% loss of activity, substrate: xylan
63% residual activity at 5 mM
complete inhibition of xylanase II at 10 mM, 50% at 2 mM, no inhibition of xylanase I
in the presence of 10 mM, the relative xylanase activity decreases by 5%
inhibits hydrolysis activity
strong inhibition of XYN10G at 1 mM
30 min at 30ºC, 10 mM, 70% inhibition; 30 min at 30ºC, 1 mM, 17% inhibition; 30 min at 30ºC, 5 mM, 39% inhibition
-
27.39% residual activity at 10 mM
-
complete inhibition at 1 mM
-
13.2% residual activity at 10 mM
-
almost complete inhibition at 1 mM
-
moderate inhibition at 1 mM
-
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
75.74% residual activity at 5 mM
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
about 40% residual activity at 5 mM; the addition of 5 mM CoCl2 inhibits enzyme activity by 59%
1 mM, 68.3% loss of activity
-
very slight inactivation
-
82% residual activity at 1 mM
-
about 70% residual activity at 5 mM
-
87.1% residual activity at 10 mM
-
about 30% residual activity at 1 mM
-
about 30% residual activity at 10 mM
-
at 1 mM, isoforms agarase-a and agarase-b show 81.31% and 91.81% residual activity, respectively
-
complete inhibition at 1 mM
-
complete inhibition at 2mM
-
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
-
about 10% residual activity at 5 mM
-
complete inhibition at 5 mM
-
inhibition of Mg2+-dependent acrtivity
-
reversible by addition of EDTA
-
0.1 mM, 86% loss of activity
-
17% inhibition at 1 mM, 63% at 10 mM
-
39% activation at 2 mM, 40% inhibition at 10 mM
-
activates at 0.1-1.0 mM, inhibitory at 1.0-10 mM
-
activates at 2 mM, inhibits at 10 mM and above
-
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
1.0 mM CoCl2, 58% inhibition
1.0 mM CoCl2, 58% 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
Show all BRENDA pathways known for Co2+
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