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(4E)-6-oxodec-4-enedioic acid
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1,1',1''-[(3-ethoxyprop-1-ene-1,1,2-triyl)triselanyl]tribenzene ethyl 2,3,3-tris(phenylselanyl)prop-2-en-1-yl ether
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0.6 mM, 65% inhibition
1,1',1''-[(3-ethoxyprop-1-ene-1,1,2-triyl)triselanyl]tris(2,4,6-trimethylbenzene) ethyl 2,3,3-tris[(2,4,6-trimethylphenyl)selanyl]prop-2-en-1-yl ether
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0.6 mM, 44% inhibition
1,1',1''-[(3-ethoxyprop-1-ene-1,1,2-triyl)triselanyl]tris(4-chlorobenzene) ethyl 2,3,3-tris[(4-chlorophenyl)selanyl]prop-2-en-1-yl ether
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modest inhibition
1-amino-4-hydroxy-2-butanone
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1-amino-4-methoxy-2-butanone
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1-amino-5-hydroxy-2-pentanone
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-
2,2-difluorosuccinic acid
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competitive
2,3-dimercaptopropane-1-sulfonic acid
2,3-Dimercaptopropanol
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cysteine and ZnCl2 protects. Dithiothreitol protects inhibition by 1 mM 2,3-dimercaptopropanol in a concentration dependent manner
2-bromo-3-(imidazol-5-yl)propionic acid
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3-acetyl-4-oxoheptane-1,7-dioic acid
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formation of a Schiff base complex between the inhibitors and the active site Lys
4,7-dioxosebacic acid
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hanging-drop method, irreversible inhibitor binds by forming Schiff-base linkages with lysines 200 and 253 at the active site. 4,7-dioxosebacic acid is a better inhibitor of the zinc-dependent 5-aminolaevulinic acid dehydratases than of the zinc-independent 5-aminolaevulinic acid dehydratases
4-amino-3-oxobutanoate
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4-oxosebaic acid
active site-directed irreversible inhibitor, less potent than 4,7-dioxosebaic acid
5,5'-dithio(bis-2-nitrobenzoic acid)
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5,5'-dithiobis(2-nitrobenzoic acid)
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5,5'-iminobis(4-oxopentanoic acid)
5,5'-oxybis(4-oxopentanoic acid)
5,5'-sulfinylbis(4-oxopentanoic acid)
5,5'-sulfonylbis(4-oxopentanoic acid)
5,5'-thiobis(4-oxopentanoic acid)
5-amino-4-oxopentanenitrile
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5-bromo-levulinic acid
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5-bromolevulinic acid
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5-fluorolevulinic acid
both inhibitor molecules are covalently bound to two conserved, active-site lysine residues, Lys205 and lys260, through Schiff bases
5-hydroxy-4-oxo-L-norvaline
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competitive
5-hydroxy-4-oxopentanoic acid
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-
5-hydroxylaevulinic acid
the competitive inhibitor is bound by a Schiff-base link to one of the invariant active-site lysine residues (Lys263). The inhibitor appears to bind in two well defined conformations
5-hydroxylevulinate
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competitive
5-hydroxylevulinic acid
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5-nitrilo-4-oxopentanoic acid
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6-amino-5-oxohexanoic acid
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7-(3-aminopentan-3-yl)-5-chloroquinolin-8-ol
using in silico screening two hexamer-stabilizing inhibitors of PBGS are identified: N-(3-methoxyphenyl)-1-methyl-6-oxo-2-[(pyridin-2-ylmethyl)sulfanyl]-1,6-dihydropyrimidine-5-carboxamide and 7-(3-aminopentan-3-yl)-5-chloroquinolin-8-ol
8-Hydroxyquinoline-5-sulfonic acid
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Al2(SO4)3
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ALA-D inhibition may be due to the fact that aluminum present in the growth medium can compete with Mg2+ or reduce the expression of ALA-D
Al3+
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IC50: 0.319 mM, GSH has no protective effect
alaremycin
porphobilinogen synthase is cocrystallized with the alaremycin. At 1.75 A resolution, the crystal structure reveals that the antibiotic efficiently blocks the active site of porphobilinogen synthase. The antibiotic binds as a reduced derivative of 5-acetamido-4-oxo-5-hexenoic acid. The corresponding methyl group is not coordinated by any amino acid residues of the active site, excluding its functional relevance for alaremycin inhibition. Alaremycin is covalently bound by the catalytically important active-site lysine residue 260 and is tightly coordinated by several active-site amino acids
AlCl3
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0.001-0.01 mM AlCl3
alloxan
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i.e. 2,4,5,6-tetraoxypyrimidine 5,6-dioxyuracil , 0.00125-0.02 mM alloxan causes a concentration-dependent uncompetitive inhibition. Dithiothreitol (0.7and 1 mM) completely prevents the inhibition induced by 0.01 and 0.02 mM alloxan. Similar protection is obtained in the presence of 2 mMglutathione
alpha-lipoic acid
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significant inhibition
arsenic acid
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inhibition of 5-aminolevulinic acid dehydratase activity by arsenic in excised etiolated maize leaf segments during greening. KNO3, chloramphenical, cycloheximide, DTNB and levulinic aciddecrease inhibition. GSH increase inhibition
ascorbic acid
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0.4 mM, 23% inhibition
bathocuproine disulfonic acid
bis(4-chlorophenyl)diselenide
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bis(4-methoxyphenyl)diselenide
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bis[3-(trifluoromethyl)phenyl]diselenide
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Butanedione
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protection by 5-aminolevulinate
Carbonate
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using a carbonate buffer rather than phosphate causes nearly a 90% drop in activity in the developed assay method
Coproporphyrinogen III
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Cuprizone
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bis-cyclohexanoneoxaldihydrazone
D-fructose
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formation of a Schiff base with the critical lysine residue of the enzyme is involved in inhibition of the enzyme by hexoses and pentoses
D-ribose
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formation of a Schiff base with the critical lysine residue of the enzyme is involved in inhibition of the enzyme by hexoses and pentoses
diammine(dichloro)platinum
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mechanism of inhibition is a direct interaction of the inhibitor with sulfhydryl groups, whereas zinc site appears to be involved with the higher doses only
dicholesteroyl diselenide
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significant at 0.1 mM
diethyldithiocarbamate
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diphenyl ditelluride
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dithiothreitol protects
DTNB
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reversible loss of activity
ebselen
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dithiothreitol protects
Ga3+
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inhibits by competing with Zn2+, IC50: 0.442 mM, GSH has no protective effect, Zn2+ completely recovers inhibition
HgCl2
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pretreatment with a nontoxic dose of Na2SeO3 partially or totally prevents in vivo mercury effects in kidney, including prevention of inhibition of delta-aminolevulinate dehydratase
In3+
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inhibits by competing with Zn2+, IC50: 0.298 mM, GSH reduces inhibition, DL-dithiothreitol has modest effect on inhibition, Zn2+ completely recovers inhibition
meso-2,3-dimercaptosuccinic acid
methyl methanethiosulfonate
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N-(3-methoxyphenyl)-1-methyl-6-oxo-2-[(pyridin-2-ylmethyl)sulfanyl]-1,6-dihydropyrimidine-5-carboxamide
using in silico screening two hexamer-stabilizing inhibitors of PBGS are identified: N-(3-methoxyphenyl)-1-methyl-6-oxo-2-[(pyridin-2-ylmethyl)sulfanyl]-1,6-dihydropyrimidine-5-carboxamide and 7-(3-aminopentan-3-yl)-5-chloroquinolin-8-ol
Na2SeO3
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inhibits renal and hepatic enzyme
Neocuproine
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2,9-dimethyl-1,10-phenanthroline
Ni2+
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0.5 mM, 8% inhibition
p-hydroxymercuribenzoate
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phenyl selenoxideacetylene
phosphate
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competitive against Mg2+
protoporphyrinogen IX
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feedback inhibition by downstream intermediate
pyridoxamine phosphate
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-
rac-2-hydroxy-4-oxopentanoic acid
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rac-3-hydroxy-4-oxopentanoic acid
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succinic acid
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noncompetitive
succinic acid monomethyl ester
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competitive
Tl3+
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inhibits by direct oxidation of essential sulfhydryl groups, IC50: 0.0085 mM, DL-dithiothreitol restores completely enzyme activity inhibited by Tl3+, Zn2+ is unable to change inhibition
1,10-phenanthroline
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2,3-dimercaptopropane-1-sulfonic acid
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1 mM, 0.5 mM ZnCl2 protects but does not reverse inhibition. Dithiothreitol protects inhibition by 1 mM 2,3-dimercaptopropane-1-sulfonic acid in a concentration dependent manner
2,3-dimercaptopropane-1-sulfonic acid
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in presence of Hg2+ or Cd2+ the inhibitory potency increases, no change in inhibitory potency by inclusion of Pb2+, Zn2+ does not modify the inhibitory effect
2,3-dimercaptopropane-1-sulfonic acid
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0.1 mM, 20% inhibition, more pronounced inhibition in combination with Cd2+
5,5'-iminobis(4-oxopentanoic acid)
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5,5'-iminobis(4-oxopentanoic acid)
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5,5'-oxybis(4-oxopentanoic acid)
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5,5'-oxybis(4-oxopentanoic acid)
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5,5'-sulfinylbis(4-oxopentanoic acid)
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5,5'-sulfinylbis(4-oxopentanoic acid)
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5,5'-sulfonylbis(4-oxopentanoic acid)
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5,5'-sulfonylbis(4-oxopentanoic acid)
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5,5'-thiobis(4-oxopentanoic acid)
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5,5'-thiobis(4-oxopentanoic acid)
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5-chlorolevulinic acid
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5-chlorolevulinic acid
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inactivation results fromthe initial formation of a Schiff base with lysine-247, followed by alkylation of lysine-195 by the resulting reactive chloroimide
bathocuproine disulfonic acid
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bathocuproine disulfonic acid
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i.e. 2,9-dimethyl-4,7-diphenyl-1,10-phenanthrolinedisulfonate
Cd2+
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inhibition at low concentration of substrate and stimulation at high levels of substrate
Cd2+
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0.5 mM, 9% inhibition
Cd2+
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0.1 mM Cd2+ totally inhibits enzyme activity. Dithiothreitol (0.003 mM) is able to restore the inhibition of enzyme activity caused by Cd2+ (0.02 mM)
Cd2+
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inhibits delta-ALA-D activity. Chelating and antioxidant agents potentiated the inhibition
Cd2+
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enzyme inhibition in excised etiolated leaf segments during greening. Cd2+ inhibits ALAD activity by affecting the ALA binding to the enzyme and/or disrupting thiol interaction. Inhibition of ALAD activity by Cd2+ is decreased in the presence of nitrogenous compounds, glutamine and NH4NO3, overview. Supply of some essential metal ions, such as Mg2+, Zn2+, and Mn2+, also reduces the inhibition of enzyme activity by Cd2+
Co2+
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0.5 mM, 15% inhibition
Cu2+
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D-glucose
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competitive inhibitor for ALA dehydratase
D-glucose
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formation of a Schiff base with the critical lysine residue of the enzyme is involved in inhibition of the enzyme by hexoses and pentoses
D-glucose
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incubations of erythrocytes for 24 h with glucose results in an increase of delta-ALA-D activity. Incubations of erythrocytes with 100 to 200 mM glucose for 48 h inhibit delta-ALA-D activity
dibutyl diselenide
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IC50: 0.01 mM
dibutyl diselenide
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IC50: 0.693 mM, enzyme from liver; IC50: 0.985 mM, enzyme from gill
diphenyl diselenide
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dithiothreitol protects
diphenyl diselenide
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IC50: 0.007 mM
diphenyl diselenide
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0.0005 mM, 17% inhibition
diphenyl diselenide
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significantl inhibition
diphenyl diselenide
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significant at 0.001 mM
diphenyl diselenide
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IC50: 0.076 mM, enzyme from liver; IC50: 0.274 mM, enzyme from gill
EDTA
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EDTA
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0.3 mM, 51% inhibition
EDTA
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5 mM, 90% inhibition
EDTA
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activity can be completely restored by addition of Mg2+ or Mn2+. Co2+, Zn2+, and Ni2+ partially restore EDTA-inhibited activity
Hg2+
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inhibitory effect is increased by meso-2,3-dimercaptosuccinic acid, inhibition is prevented by dithiothreitol
Hg2+
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inhibits enzyme in vivo at 6 h and 12 h after treatment. Se4+ abolishes the inhibitory effect of Hg2+
Hg2+
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the inhibition caused by 0.37 mM Hg2+ is alleviated by addition of 10 mM KNO3. 10 mM NH4Cl and 5 mM sucrose increase the inhibitory effect of Hg2+ on enzyme activity, while 10 mM levulinic acid and 0.0001 mM 5,5'-dithio(bis-2-nitrobenzoic acid) glutamine and glutathione decrease it
iodoacetamide
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irreversible
iodoacetamide
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1 mM, 97% inhibition
iodoacetamide
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insensitive
iodoacetate
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irreversible
levulinic acid
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levulinic acid
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competitive
levulinic acid
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a weak competitive inhibitor
levulinic acid
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competitive inhibitor, 8% residual activity at 20 mM
meso-2,3-dimercaptosuccinic acid
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4 mM, 1 mM ZnCl2 protects but does not reverse inhibition. Dithiothreitol protects inhibition by 1 mM meso-2,3-dimercaptosuccinic acid in a concentration dependent manner
meso-2,3-dimercaptosuccinic acid
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in presence of Hg2+ or Cd2+ the inhibitory potency increases, Zn2+ does not modify the inhibitory effect
meso-2,3-dimercaptosuccinic acid
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0.1 mM, 18% inhibition
Mg2+
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0.5 mM, 7% inhibition
Mn2+
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0.5 mM, 21% inhibition
NaCN
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competitive
NaCN
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in presence of the substrate
NEM
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1 mM, 85% inhibition
Pb2+
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does not produce a change in the quarternary structure detectable by small angle X-ray scattering
Pb2+
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0.5 mM, 44% inhibition
Pb2+
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5-aminolevulinate protects
PCMB
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1 mM, 97% inhibition
phenyl selenoacetylene
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IC50: above 0.4 mM
phenyl selenoacetylene
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IC50: 0.25 mM
phenyl selenoacetylene
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inhibition involves conversion of phenyl selenoacetylene to diphenyl diselenide, that induces oxidation of essential -SH groups of the enzyme. Inhibition is partially prevented by incubation under argon atmosphere and is completely prevented by dithiothreitol
phenyl selenoxideacetylene
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IC50: 0.1 mM, inhibition is antagonized by dithiothreitol
phenyl selenoxideacetylene
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IC50: 0.045 mM, inhibition is antagonized by dithiothreitol
pyridoxal 5'-phosphate
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30% inhibition at 1 mM, negligible inhibition at 0.05 mM
pyridoxal 5'-phosphate
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competitive
sodium selenide
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IC50: 0.005 mM
sodium selenide
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IC50: 0.386 mM, enzyme from gill; IC50: 0.902 mM, enzyme from liver
succinylacetone
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50% inhibition by 125 nM
succinylacetone
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50% inhibition by 250 nM
Zn2+
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-
Zn2+
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the inhibitory zinc is located at a subunit interface using Cys219 and His10 as ligands
Zn2+
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activates at 0.1-0.02 mM, inhibits at 1.0 mM
Zn2+
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exocenous addition of zinc results in a decrease by up to 35% in enzyme activity
Zn2+
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pH 7.5, 50% inhibition at 0.12 mM
Zn2+
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at pH 8.5, 50% inhibition by 0.075 mM. At pH 7.5, 50% inhibition by less than 0.02 mM
Zn2+
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activity is progressively increased with increasing Zn2+ concentrations up to 0.1 mM, inhibition at high concentrations
additional information
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the enzyme from human erythrocytes is a potential target for organochalcogens
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additional information
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not inhibited by Seleno-furanoside
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additional information
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no inhibition by EDTA even at 25 mM
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additional information
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no inhibition by dicholesteroyl diselenide
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additional information
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in vivo iron reduction in rat blood has a negative correlation with the activity of delta-ALA-D, overview
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additional information
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insensitive to inhibition by hemin and protoporphyrin
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additional information
no inhibition by 10 mM EDTA or 1,20-phenanthroline
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additional information
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no inhibition by 10 mM EDTA or 1,20-phenanthroline
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