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(E)-3-(4-((3R,5R,7R)-adamantan-1-yl)phenoxy)-N-(5-(piperidine-1-carbonyl)-1,4-dihydroindeno[1,2-c]pyrazol-3-yl) acrylamide
-
(NH4)2SO4
reduction of oxaloacetate to malate and oxidation of malate to oxaloacetate
1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one
-
i.e. differentiation-inducing factor DIF-1, a morphogen secreted from Dictyostelium discoideum, inhibits proliferation of several cancer cells via suppression of the Wnt/beta -catenin signaling pathway, specifically to mMDH and inhibits its activity, no binding of cytosolic MDH, overview
11-chloro-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
65.3% inhibition at 0.010 mM
2,3-dimethoxy-6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carbonitrile
-
89.2% inhibition at 0.010 mM
2,3-dimethoxy-9-(trifluoromethyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
97.7% inhibition at 0.010 mM
2,4-dichlorophenoxybutyric acid
-
-
2-Hydroxy-5-nitrobenzyl bromide
-
-
2-methoxy-1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one
-
i.e. differentiation-inducing factor 2-MIDIF-1, a morphogen secreted from Dictyostelium discoideum, inhibits proliferation of several cancer cells via suppression of the Wnt/beta -catenin signaling pathway, binds specifically to mMDH and inhibits its activity, no binding of cytosolic MDH, overview
2-Thenoyltrifluoroacetone
-
3-Aminopyridine adenine dinucleotide
-
-
3-methoxy-9-trifluormethyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
83.9% inhibition at 0.010 mM
3-methylpyridine adenine dinucleotide
-
-
3-pyridylacetonitrile adenine dinucleotide
-
-
3-pyridylcarbinol adenine dinucleotide
-
-
4-coumaric acid
-
13.4% inhibition at 0.1 mM
4-methoxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
87.6% inhibition at 0.010 mM
5-(3,4-dichlorobenzyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
5-(4-methylbenzyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
5-benzyl-9-bromo-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
8.6% inhibition at 0.010 mM
5-benzyl-9-chloro-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
5-benzyl-9-methoxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
5-benzyl-9-methyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
5-benzyl-9-tert-butyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
5-benzyl-9-trifluoromethyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carbonitrile
-
91.3% inhibition at 0.010 mM
6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylic acid
-
98.7% inhibition at 0.010 mM
7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
78.7% inhibition at 0.010 mM
8,10-dichloro-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
28.7% inhibition at 0.010 mM
9-(methylsulfinyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
96.2% inhibition at 0.010 mM
9-(methylthio)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
76.6% inhibition at 0.010 mM
9-(trifluoromethyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
88.3% inhibition at 0.010 mM
9-bromo-12-(prop-2-en-1-yl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
74.1% inhibition at 0.010 mM
9-bromo-12-methyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
98.0% inhibition at 0.010 mM
9-bromo-2,3-dimethoxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
56.3% inhibition at 0.010 mM
9-bromo-2-methoxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
58.7% inhibition at 0.010 mM
9-bromo-3-methoxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
15.0% inhibition at 0.010 mM
9-bromo-4-hydroxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
25.9% inhibition at 0.010 mM
9-bromo-4-methoxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
82.0% inhibition at 0.010 mM
9-bromo-5-(3,4-dichlorobenzyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
9-bromo-5-(4-methoxybenzyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
9-bromo-5-(4-methylbenzyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
9-bromo-5-methyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
81.9% inhibition at 0.010 mM
9-bromo-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
74.5% inhibition at 0.010 mM
9-chloro-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
73.4% inhibition at 0.010 mM
9-fluoro-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
46.2% inhibition at 0.010 mM
9-methyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
87.8% inhibition at 0.010 mM
9-nitro-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
54.2% inhibition at 0.010 mM
9-tert-butyl-5-(3,4-dichlorobenzyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
adenosine 5'-diphosphoribose
-
-
arsenate
-
uncompetitive inhibition
BaCl2
-
1 mM, 24.9% inhibition
butyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
-
CaCl2
-
1 mM, 29.1% inhibition
CoA
Coccochloris peniocystis
-
-
CoCl2
-
1 mM, 39% inhibition
CuCl2
-
1 mM, 89.8% inhibition
D-fructose 1,6-diphosphate
-
heart s-MDH, inhibits the binding of NADH
Diamide
-
isoforms cy MDH1 and cyMDH2 are reversibly inactivated by diamide treatment. Both NADH and GSH separately or together prevented inactivation of cyMDH1 and cyMDH2 by diamide
EDTA
-
1 mM, 52.2% inhibition
ethyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
-
Fe3+
complete inhibition at 5 mM
ferulic acid
-
24.5% inhibition at 0.1 mM
guanidine hydrochloride
in the presence of 4 M guanidine hydrochloride enzyme structure is unfolded with complete loss of enzyme activity
hexyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
-
HgCl2
-
1 mM, complete inhibition
hydroxylamine
-
1 mM, 57.1% inhibition
isocitrate
reduction of oxaloacetate to malate
methyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
60.9% inhibition at 0.010 mM
MgCl2
-
1 mM,34.9% inhibition
MnCl2
-
1 mM, 28.6% inhibition
NADP+
-
product inhibition; product inhibition, 26% inhibition at 10 mM
NEM
-
1 mM, complete inhibition
NiCl2
-
1 mM, 36.8% inhibition
octyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
-
oxalic acid
-
inhibits L-malate oxidation reaction
p-chloromercuribenzoate
-
-
p-chloromercuriphenylsulfonate
-
-
pentyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
-
Phenylmethanesulfonylfluoride
-
-
propyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
-
pyridine adenine dinucleotide
-
-
Semicarbazide
-
1 mM, 61.3% inhibition
sodium dodecylsulfate
0.1%, 70% loss of activity, 1%, complete loss of activity
succinate
slight inhibition of reduction of oxaloacetate
Urea
-
enzyme activity and electrophoretic pattern of MDH and lactate dehydrogenase, EC 1.1.1.27, compared in relation to heat and urea inactivation, LDH is more sensitive than MDH, overview
ZnCl2
-
1 mM, 72.6% inhibition
(S)-malate
product inhibitor
(S)-malate
substrate inhibition, 60% inhibition at 30 mM
(S)-malate
-
product inhibition, 66% inhibition at 5 mM
(S)-malate
-
24.2% substrate inhibition at 20 mM
2-oxoglutarate
reduction of oxaloacetate to malate and oxidation of malate to oxaloacetate
2-oxoglutarate
-
44% inhibition at 5 mM
acetyl-CoA
Coccochloris peniocystis
-
-
ADP
-
-
alpha-ketoglutarate
-
end-product inhibition
AMP
-
-
ATP
-
-
ATP
Coccochloris peniocystis
-
-
ATP
-
43.7% inhibition at 5 mM
Ca2+
-
-
Ca2+
-
decreases activity under normal and pathological conditions
Ca2+
-
inhibits isoform MDH1 at millimolar concentrations; inhibits isoform MDH2 at millimolar concentrations; inhibits isoform MDH3 at millimolar concentrations
citrate
Coccochloris peniocystis
-
-
citrate
reduction of oxaloacetate to malate
citrate
-
competitive with respect to oxaloacetate
Co2+
-
-
Co2+
36% inhibition at 2 mM
Cu2+
complete inhibition at 5 mM
Cu2+
-
0.01-0.4 mM, activity from ischemic tissue decreases more significantly compared to the control
Cu2+
-
in the presence of 1 mM Cu2+, the enzyme activity decreases to approximately 40% of normal activity
Cu2+
-
25% inhibition at 0.1 mM
Dicarbonate
-
-
Fe2+
-
-
Fe2+
complete inhibition at 2 mM
Hg2+
-
-
Hydroxymalonate
-
-
iodoacetate
-
1 mM, 93.6% inhibition
L-malate
-
inhibition constant: 3.65 mM
L-malate
-
MDH activity is strongly inhibited by excess of L-malate
L-malate
-
product inhibition
Mg2+
-
-
Mn2+
-
-
Mn2+
-
slight inhibition of all isoform MDH2; slight inhibition of isoform MDH1; slight inhibition of isoform MDH3
NAD+
-
-
NAD+
-
MDH activity is inhibited by 0.5 mM NADH
NAD+
-
product inhibition; product inhibition, 29% inhibition at 5 mM, 42% inhibition at 10 mM
NAD+
-
substrate inhibition
NADH
-
substrate inhibition
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
substrate inhibition
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH, over 2 mM
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH over 1 mM
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
product inhibition
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
MDH activity is inhibited by over 200 mM NADH
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
product inhibition
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
Ni2+
-
-
oxaloacetate
-
substrate inhibition
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
substrate inhibition
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH, overv 2 mM
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
substrate inhibition at above 0.3 mM, 37% inhibition at 1 mM
oxaloacetate
Coccochloris peniocystis
-
-
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH over 1 mM
oxaloacetate
above 0.025 mM
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
-
substrate inhibition
oxaloacetate
at high concentrations
oxaloacetate
substrate inhibition
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
-
substrate inhibition, pH-dependent
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
-
MDH activity is inhibited at 0.33 mM
oxaloacetate
-
substrate inhibition
oxaloacetate
substrate inhibition, 50% inhibition at 6 mM
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate
oxaloacetate
-
substrate inhibition; substrate inhibition, 29% inhibition at 5 mM
oxaloacetate
-
substrate inhibition
oxaloacetate
-
MDH activity is inhibited by over 250 mM oxaloacetate
oxaloacetate
-
27.4% substrate inhibition at 1 mM
sulfite
-
-
Zn2+
42% inhibition at 5 mM
Zn2+
-
inhibition constant 1.7 mM
Zn2+
73% inhibition at 2 mM
Zn2+
-
25% inhibition at 1 mM
additional information
-
isoform cyMDH3 maintains its low basal activity upon oxidation with 0.5 mM diamide
-
additional information
-
strong decrease in MDH activity under aerobic conditions
-
additional information
-
no effect by NaCl
-
additional information
no substrate inhibition by L-malate up to 20 mM
-
additional information
-
no substrate inhibition by L-malate up to 20 mM
-
additional information
unaffected by excess of L-malate
-
additional information
-
unaffected by excess of L-malate
-
additional information
-
differentiation-inducing factors DIF-3, i.e. 1-(3-chloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one, and 6-MIDIF-3, a 6-methoxy isomer of DIF-3, bind spefically to mMDH, but do not inhibit the enzyme activity, no binding of cytosolic MDH
-
additional information
cyMDH is sensitive to cold and salt stresses
-
additional information
-
cyMDH is sensitive to cold and salt stresses
-
additional information
-
the thermostable enzyme is not affected by metal ions (CuCl2, MgCl2, MnCl2, CoCl2, BaCl2, ZnCl2 or CaCl2 and NaCl or KCl) or various organic metabolites (pyruvate, phosphoenolpyruvate, ATP, ADP, AMP, glucose-1-phospate, fructose-1-phosphate, fructose-1,6-bisphosphate, fructose-6-phosphate, ribose-1-phosphate, ribose-5-phosphate (all 5 mM), glycerate, lactate, 2-oxoglutarate, citrate, serine, diphosphate (all 1 mM) or phosphate (10 mM))
-
additional information
the thermostable enzyme is not affected by metal ions (CuCl2, MgCl2, MnCl2, CoCl2, BaCl2, ZnCl2 or CaCl2 and NaCl or KCl) or various organic metabolites (Pyruvate, phosphoenolpyruvate, ATP, ADP, AMP, glucose-1-phospate, fructose-1-phosphate, fructose-1,6-bisphosphate, fructose-6-phosphate, ribose-1-phosphate, ribose-5-phosphate (all 5 mM), glycerate, lactate, 2-oxoglutarate, citrate, serine, pyrophosphate (all 1 mM) or ?H2PO4 (10 mM))
-
additional information
-
the thermostable enzyme is not affected by metal ions (CuCl2, MgCl2, MnCl2, CoCl2, BaCl2, ZnCl2 or CaCl2 and NaCl or KCl) or various organic metabolites (Pyruvate, phosphoenolpyruvate, ATP, ADP, AMP, glucose-1-phospate, fructose-1-phosphate, fructose-1,6-bisphosphate, fructose-6-phosphate, ribose-1-phosphate, ribose-5-phosphate (all 5 mM), glycerate, lactate, 2-oxoglutarate, citrate, serine, pyrophosphate (all 1 mM) or ?H2PO4 (10 mM))
-
additional information
MDH phosphorylation by PknD inhibits the MDH activity by 40%, phosphorylation by other kinases also inhibits the enzyme activity: 42-53% inhibition for PknF, 23-32% inhibition for PknH, and 27-38% inhibition for PknA
-
additional information
-
MDH phosphorylation by PknD inhibits the MDH activity by 40%, phosphorylation by other kinases also inhibits the enzyme activity: 42-53% inhibition for PknF, 23-32% inhibition for PknH, and 27-38% inhibition for PknA
-
additional information
urea cannot induce complete unfolding and inactivation of Pcal_1699 even at a final concentration of 8 M. Not inhibitory: EDTA Triton X-100, TWeen-20, dithiothreitol, glycerol
-
additional information
-
urea cannot induce complete unfolding and inactivation of Pcal_1699 even at a final concentration of 8 M. Not inhibitory: EDTA Triton X-100, TWeen-20, dithiothreitol, glycerol
-
additional information
-
strong decrease in MDH activity under aerobic conditions
-
additional information
MDH is not affected by DTT or EDTA
-
additional information
-
not inhibitory: AMP, ADP, ATP
-
additional information
-
development of 5-benzylpaullones and paullone-9-carboxylic acid alkyl esters as selective inhibitors of mMDH, overview
-
additional information
not inhibitory: praziquantel and albendazole
-
additional information
-
not inhibitory: praziquantel and albendazole
-