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(NH4)2SO4
-
mutant enzyme is less sensitive to inhibition than wild-type enzyme
3-dimethylsulfoniopropionaldehyde
-
at high concentrations
5,5'-dithiobis[2-nitrobenzoic acid]
-
the effect of the thiol reagent DTNB on the native enzyme structure of the wild type enzyme and the mutants is examined
Acetylcholine
-
10 mM, 18% inhibition
AgNO3
-
3 mM, 90-100% inhibition
benzaldehyde
-
1 mM, 51% inhibition
benzyltrimethylamine iodide
-
10 mM, 45% inhibition
bis[diethylthiocarbamyl]disulfide
-
the effect of the thiol reagent disulfiram on the native enzyme structure of the wild type enzyme and the mutants is examined
Butyrylcholine
-
100 mM, 73% inhibition
cyclophosphamide
CTX, an antineoplastic and immuno-suppressant pre-drug, the enzyme loses 43% and 69% of its activity at 0.2 mM and 2.0 mM CTX, respectively, after 120 min. Docking of CTX to pkBADH and molecular modeling. The pseudofirst-order rate constant of inactivation (kobs) is dependent on CTX concentration only at low concentrations (0.2 and 0.6 mM CTX), and then the kobs between 1.0 and 2.0 mM show similar values. CTX can have access more easily to the catalytic cysteine when NAD+ opens the active site for substrate betaine aldehyde binding according to the kinetic mechanism, kinetics of inactivation of pkBADH by CTX in the presence of NADH, overview. Reversibility of inactivation, pkBADH inactivated with 2 mM CTX and incubated with DTT recovers 96% of its activity, and 93% with 2-mercaptoethanol, but in the presence of glutathione (GSH), the enzyme is not reactivated
ethanolamine
-
100 mM, 35% inhibition
Glutaraldehyde
-
10 mM, 83% inhibition
glyceraldehyde
-
100 mM, 83% inhibition
H2O2
-
more than 50% inhibition at 0.1 mM H2O2, noncompetitive inhibition with respect to NAD+ or to betaine aldehyde at saturating concentrations of the other substrate at pH 7.0 or 8.0
Isobutanal
-
10 mM, 93% inhibition
isopentanal
-
1 mM, 84% inhibition
Isovaleraldehyde
-
wild-type enzyme shows stronger inhibition than the mutant enzyme
methyl methanethiosulfonate
methyl methanethiosulphonate
-
pH-dependence of the second-order rate constant of inactivation suggests that at low pH values the essential Cys exists as thiolate by the formation of an ion pair with a positively charged residue
methyl(bis-beta-chloroethyl)amine
-
-
Mg2+
-
0.4 M, complete inhibition
N,N-dimethylethanolamine
-
100 mM, 57% inhibition
N,N-dimethylglycine
-
1 mM, 24% inhibition
n-butylaldehyde
-
10 mM, 96% inhibition
N-Methylethanolamine
-
100 mM, 50% inhibition
N-methylglycine
-
1 mM, 24% inhibition
NAD(P)H
reversible inactivation
NADP+
-
substrate inhibition above 10 mM
NADPH
-
product inhibition
phenylacetaldehyde
-
1 mM, 54% inhibition
S-methyl-N,N-diethyldithiocarbamoyl sulfone
most potent irreversible inhibition in vitro at 0.05 mM, but no inhibition in situ
S-methyl-N,N-diethyldithiocarbamoyl sulfoxide
irreversible inhibition
S-methyl-N,N-diethylthiocarbamoyl sulfone
irreversible inhibition
S-methyl-N,N-diethylthiocarbamoyl sulfoxide
-
S-methylmethanesulfonate
-
the effect of the thiol reagent MMTS on the native enzyme structure of the wild type enzyme and the mutants is examined
sodium meta-arsenite plus 2,3-dimercaptopropanol
-
arsenite-BAL
tetraethylamine iodide
-
10 mM, 19% inhibition
tetramethylamine iodide
-
10 mM, 19% inhibition
tetramethylammonium hydroxide
-
100 mM, 57% inhibition
tetrapropylamine iodide
-
10 mM, 43% inhibition
trimethylacetaldehyde
-
100 mM, 89% inhibition
1,10-phenanthroline
-
-
1,10-phenanthroline
-
no inhibition at 1 mM
2,2'-dipyridyl
-
-
2,2'-dipyridyl
-
no inhibition at 3 mM
acetaldehyde
-
100 mM, 83% inhibition
acetaldehyde
-
10 mM, 69% inhibition
AMP
-
competitive with respect to NAD+ and mixed with betaine aldehyde and uncompetitive with respect to NAD+
AMP
-
competitive with respect to NAD+ and mixed with betaine aldehyde
betaine
-
10 mM, 14% inhibition
betaine
-
product inhibition
Betaine aldehyde
-
0.5 mM, non-competitive inhibitor against NAD+
Betaine aldehyde
-
above 0.5 mM
Betaine aldehyde
-
the enzyme is reversibly and partially inactivated by betaine aldehyde in the absence of NAD+ in a time- and concentration-dependent mode
Betaine aldehyde
strongly inhibited by betaine aldehyde at concentrations of more than 0.15 mM
Betaine aldehyde
-
substrate inhibition at concentrations of betaine aldehyde as low as 0.15 mM
Betaine aldehyde
-
substrate inhibition
Ca2+
-
500 mM CaCl2, about 50% loss of activity
Ca2+
-
500 mM CaCl2, about 50% loss of activity
Ca2+
-
10 mM CaCl2, 90% inhibition
Ca2+
-
500 mM CaCl2, about 50% loss of activity
choline
-
-
choline
-
100 mM, 78% inhibition
choline
-
10 mM, 23% inhibition
choline
-
mutant enzyme shows stronger inhibition compared to wild-type enzyme
choline
-
competitive against betaine aldehyde and uncompetitive with respect to NAD+
cimetidine
-
-
Disulfiram
-
inactivates in a time- and dose-dependent manner, inactivation kinetics is biphasic with second-order inactivation rate constants at pH 7.5 of 6.8 per M per sec and 0.33 per M per sec, inactivation is faster in presence of NAD(P)+ than in absence, inactivation is increased by NAD(P)H and betaine aldehyde, reactivation by dithiothreitol, inactivation is reversible by glutathione
Disulfiram
-
inactivates in a time- and dose-dependent manner, inactivation kinetics is monophasic with a second-order inactivation rate constant at pH 6.0 of 4.9 per M per sec and at pH 8.8 of 1000 per M per sec, inactivation is faster in presence of NAD(P)+ than in absence, inactivation is protected by NAD(P)H and betaine aldehyde, reactivation by dithiothreitol, inactivation is reversible by glutathione
Disulfiram
-
CAS 97-77-8, reaction of disulfiram with protein thiol groups by formation of a mixed disulfide or formation of an intra-molecular disulfide resulting in conformational changes. Inactivation under pseudo-first order conditions occurs in a time- and dose-dependent manner. In the absence of disulfiram, but in the presence of 2% methanol as DSF vehicle, no changes in enzymatic activities are observed. Using a DSF concentration range 10-30 microM, inactivation kinetics were biphasic with rate constants differing in one order of magnitude, and inactivation partial. The residual activity at infinite time, decreases as the disulfiram concentrations increases, reaching a value near zero at 30 microM disulfiram, whereas the amplitude of the two inactivation phases increases, each one reaching about 50% of initial activity at 30 microM disulfiram.
glycine betaine
-
no inhibition up to 10 mM
glycine betaine
Amaranthus sp.
-
product inhibition
Hg2+
-
-
Hg2+
-
0.0001-0.0005 mM HgCl2
Hg2+
-
3 mM HgCl2, 90-100% inhibition
iodoacetamide
-
1 mM
iodoacetate
-
-
K+
-
1.0 mM, 35% inhibition
K+
-
thermal stability of the pkBADH-NAD+ complex in the presence of K+ shows a complete loss of the ellipticity signal and highly cooperative thermal transitions in each thermogram in the presence of each K+ concentration tested. In all tested conditions, the thermal denaturation is irreversible
methyl methanethiosulfonate
-
in absence of ligands, the kinetics of inactivation is biphasic, suggesting the existence of two enzyme conformers differing in the reactivity of their catalytic thiolate. Preincubation with NADH or betaine aldehyde prior to the chemical modification brings about active site rearrangements that result in an import decrease in the inactivation rate. Binding of NAD+ increases the rate of inactivation after prolonged preincubation
methyl methanethiosulfonate
-
in absence of ligands, the kinetics of inactivation is biphasic, suggesting the existence of two enzyme conformers differing in the reactivity of their catalytic thiolate. Preincubation with coenzyme or the aldehyde prior to the chemical modification brings about active site rearrangements that result in an import decrease in the inactivation rate
NaCl
In response to high salt stress conditions numerous truncated transcripts of two BADH homologs resulting from an unusual posttranscriptional processing are detected in barley. The observed events take place at the 5' exonic region, and lead to the insertion of exogenous gene sequences and a variety of deletions that result in the removal of translation initiation codon, loss of functional domain, and frameshifts with premature termination by introducing stop codon.; In response to high salt stress conditions numerous truncated transcripts of two BADH homologs resulting from an unusual posttranscriptional processing are detected in barley. The observed events take place at the 5' exonic region, and lead to the insertion of exogenous gene sequences and a variety of deletions that results in the removal of translation initiation codon, loss of functional domain, and frameshifts with premature termination by introducing stop codon.
NaCl
-
the activity of isoform BADH2 decreases at NaCl concentrations greater than 300 mM
NaCl
0.5 M, expression of OsBADH2 is increased under salt stress conditions, but at high concentrations, expression is inhibited.; 0.5 M, firstly, expression of OsBADH1 is increased under salt stress conditions, but at high concentrations, expression has been inhibited.
NaCl
-
inhibitory effect increases with concentrations from 50 mM to 250 mM
NaCl
-
0.5 M, 50% inhibition
NaCl
-
mutant enzyme is slightly more sensitive to inhibition than wild-type enzyme
NaCl
Yeast strains containing the BADH gene from Suaeda salsa were streaked on YPD medium supplemented with 0.5% methanol and different NaCl concentrations (0-1.5 mol/l). Salt tolerance is examined after incubation at 30°C for 3 days. Growth of yeast strains A764, A765, A767 and YPIC3 is severely suppressed containing 0.8 mol/l NaCl and completely inhibited on 1.0 mol/l NaCl without methanol induction. However, induced with 0.5% of methanol, A764, A765 and A767 grow well but YPIC3 is suppressed greatly on YPD medium containing 1.0 mol/l NaCl. A764, A765, and A767 can resist 1.2 mol/l NaCl and can grow a little on 1.5 mol/l NaCl with 0.5% of methanol induction.
NaCl
-
40% inhibition above 0.3 M
NaCl
at a concentration of 0.5 M, expression of BADH2 is inhibited
NaCl
Q53CF4
at a concentration of 0.5 M, expression of BADH1 is inhibited; at a concentration of 0.5 M, expression of BADH2 is inhibited
NaCl
100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity
NAD+
Amaranthus sp.
-
glycerol favours substrate inhibition
NAD+
substrate inhibition by high concentrations of NAD+
NADH
-
mixed inhibitor against NAD+ and betaine aldehyde
NADH
-
product inhibition
NADH
-
mixed inhibited against NAD+ and betaine aldehyde
NADH
-
a mixed-type inhibitor of the enzyme. After NADH release, the enzyme cannot start a new catalytic cycle, possibly because of the catalytic residue protonation state
NH4+
-
-
NH4+
-
above 0.4 M, more than 60% inhibition
PCMB
-
-
ZnCl2
-
0.0001-0.0005 mM
ZnCl2
-
3 mM, 90-100% inhibition
additional information
Amaranthus sp.
-
no product inhibition
-
additional information
-
no substrate inhibition with NAD+
-
additional information
diethyldithiocarbamic acid does not inactivate the enzyme in vitro and in situ
-
additional information
-
diethyldithiocarbamic acid does not inactivate the enzyme in vitro and in situ
-