Ligand malonyl-CoA

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Basic Ligand Information

Molecular Structure
Picture of malonyl-CoA (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C24H38N7O19P3S
malonyl-CoA
LTYOQGRJFJAKNA-DVVLENMVSA-N
Synonyms:
(2) malonyl-CoA, 2-carboxyacetyl-CoA, an omega-carboxyacyl-CoA, malonyl CoA
Pathway Source
Pathways
MetaCyc
(1'S,5'S)-averufin biosynthesis, (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoate biosynthesis II (4-desaturase), (4Z,7Z,10Z,13Z,16Z)-docosapentaenoate biosynthesis (6-desaturase), (5R)-carbapenem carboxylate biosynthesis, (9Z)-tricosene biosynthesis more


Show all pahtways known for Show all BRENDA pathways known for malonyl-CoA

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (56 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
malonyl-CoA + NADPH = malonate-semialdehyde + CoA + NADP+
-
show the reaction diagram
S-adenosyl-L-methionine + malonyl-CoA = S-adenosyl-L-homocysteine + malonyl-CoA methyl ester
-
show the reaction diagram
malonyl-CoA + dephospho-CoA = CoA + malonyl-dephospho-CoA
-
show the reaction diagram
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA = [biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
-
show the reaction diagram
malonyl-CoA + D-tryptophan = CoA + N2-malonyl-D-tryptophan
-
show the reaction diagram
malonyl-CoA + 3,4-dichloroaniline = CoA + N-(3,4-dichlorophenyl)-malonamate
-
show the reaction diagram
apigenin 7-O-apiosylglucoside + malonyl-CoA = apigenin 7-O-apiosylglucoside -6''-O-malonylester + CoA
-
show the reaction diagram
malonyl-CoA + kaempferol 3-O-glucoside = CoA + kaempferol 3-O-glucoside malonylester
-
show the reaction diagram
cinnamoyl-CoA + malonyl-CoA = 3,5-dihydroxystilbene + CoA + CO2
-
show the reaction diagram
Malonyl-CoA + 3-hydroxybenzoyl-CoA = ?
-
show the reaction diagram
isovaleryl-CoA + malonyl-CoA = phloroisovalerophenone + CO2 + CoA
-
show the reaction diagram
malonyl-CoA + N-methylanthraniloyl-CoA = CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
show the reaction diagram
malonyl-CoA + 4-coumaroyl-CoA + NADPH + H+ = CoA + isoliquiritigenin + CO2 + NADP+ + H2O
-
show the reaction diagram
malonyl-CoA + delphinidin 3-O-beta-D-glucoside = CoA + delphinidin 3-O-(6-malonyl-beta-D-glucoside)
-
show the reaction diagram
malonyl-CoA + benzoyl-CoA = CoA + 3,5-dihydroxybiphenyl + CO2
-
show the reaction diagram
4-coumaroyl-CoA + malonyl-CoA + H2O = 2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
show the reaction diagram
malonyl-CoA + 2-aminobenzoyl-CoA = 2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
show the reaction diagram
malonyl-CoA + 5 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = 10-deoxymethynolide + 6 CoA + 6 CO2 + 5 NADP+ + 2 H2O
-
show the reaction diagram
malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = narbonolide + 7 CoA + 7 CO2 + 5 NADP+ + 2 H2O
-
show the reaction diagram
acetyl-CoA + malonyl-CoA + [2-methylbutanoate polyketide synthase] + 2 NADPH + 2 H+ + S-adenosyl-L-methionine = (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] + 2 CoA + CO2 + 2 NADP+ + S-adenosyl-L-homocysteine + H2O
-
show the reaction diagram
malonamoyl-[OxyC acyl-carrier protein] + malonyl-CoA = 18-carbamoyl-3,5,7,9,11,13,15,17-octaoxooctadecanoyl-[OxyC acyl-carrier protein] + CO2 + CoA
-
show the reaction diagram
4-coumaroyl-CoA + malonyl-CoA = naringenin chalcone + CoA + CO2
show the reaction diagram
acetyl-CoA + malonyl-CoA + NADH + NADPH = ?
-
show the reaction diagram
4-coumaroyl-CoA + malonyl-CoA = 3,4',5-trihydroxystilbene + CoA + CO2
-

In Vivo Product in Enzyme-catalyzed Reactions (6 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
show the reaction diagram
acetyl-CoA + malonate = acetate + malonyl-CoA
-
-
show the reaction diagram
ATP + acetyl-CoA + HCO3- = ADP + malonyl-CoA + phosphate
-

Substrate in Enzyme-catalyzed Reactions (345 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
malonyl-CoA + NADPH = malonate-semialdehyde + CoA + NADP+
-
show the reaction diagram
S-adenosyl-L-methionine + malonyl-CoA = S-adenosyl-L-homocysteine + malonyl-CoA methyl ester
-
show the reaction diagram
malonyl-CoA + anthranilate = CoA + N-malonylanthranilate
-
show the reaction diagram
malonyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole = CoA + N-malonyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
show the reaction diagram
malonyl-CoA + L-carnitine = malonyl-L-carnitine + CoA
-
show the reaction diagram
isovaleryl-CoA + malonyl-CoA = phloroisovalerophenone + CO2 + CoA
-
show the reaction diagram
malonyl-CoA + 4-coumaroyl-CoA + NADPH + H+ = CoA + isoliquiritigenin + CO2 + NADP+ + H2O
-
show the reaction diagram
malonyl-CoA + dephospho-CoA = CoA + malonyl-dephospho-CoA
-
show the reaction diagram
malvidin 3-O-beta-D-glucoside + malonyl-CoA = CoA + malvidin 3-O-(6-O-malonyl)-beta-D-glucoside
-
show the reaction diagram
malonyl-CoA + 2-aminobenzoyl-CoA = 2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
show the reaction diagram
malonyl-CoA + 5 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = 10-deoxymethynolide + 6 CoA + 6 CO2 + 5 NADP+ + 2 H2O
-
show the reaction diagram
malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = narbonolide + 7 CoA + 7 CO2 + 5 NADP+ + 2 H2O
-
show the reaction diagram
acetyl-CoA + malonyl-CoA + [2-methylbutanoate polyketide synthase] + 2 NADPH + 2 H+ + S-adenosyl-L-methionine = (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] + 2 CoA + CO2 + 2 NADP+ + S-adenosyl-L-homocysteine + H2O
-
show the reaction diagram
malonamoyl-[OxyC acyl-carrier protein] + malonyl-CoA = 18-carbamoyl-3,5,7,9,11,13,15,17-octaoxooctadecanoyl-[OxyC acyl-carrier protein] + CO2 + CoA
-
show the reaction diagram
malonyl-CoA + (S)-1-aminoethylphosphonic acid = CoA + ?
-
show the reaction diagram
4-nitrobenzoyl-CoA + malonyl-CoA + 4 (S)-methylmalonyl-CoA + 4 NADPH + 4 H+ = demethylluteothin + 5 CO2 + 6 CoA + 4 NADP+ + 3 H2O
-
show the reaction diagram
4-nitrobenzoyl-CoA + malonyl-CoA + 6 (S)-methylmalonyl-CoA + 6 NADPH + 4 H+ = demethyldeoxyspectinabilin + 7 CO2 + 8 CoA + 6 NADP+ + 5 H2O
-
show the reaction diagram
lauroyl-CoA + malonyl-CoA = ?
-
show the reaction diagram
malonyl-CoA + L-homoserine = CoA + O-malonyl-L-homoserine
-
show the reaction diagram
malonyl-CoA + L-(-)carnitine = malonylcarnitine + CoASH
-
show the reaction diagram
malonyl-CoA + an [acyl-carrier protein] = CoA + a methylmalonyl-[acyl-carrier protein]
-
show the reaction diagram
2-oxo-3-methylbutanoate + malonyl-CoA + H2O = 2-hydroxy-3-metylbutane-11,2-tricarboxyl acid + CoA
-
show the reaction diagram
malonyl-CoA + malonate = malonyl-CoA + malonate
-
show the reaction diagram
malonyl-CoA = malonate + CoA
-
show the reaction diagram
malonyl-CoA + H2O = malonate + CoA
-
show the reaction diagram
malonyl-CoA + H2O = malonate + CoA
-
show the reaction diagram
malonyl-CoA + H2O = malonate + CoA
-
show the reaction diagram
malonyl-CoA + H2O = CoA + malonate
-
show the reaction diagram
malonyl-CoA + H2O = ?
-
show the reaction diagram
malonyl-CoA + H+ = acetyl-CoA + CO2
-
show the reaction diagram
Malonyl-CoA = Acetyl-CoA + CO2
-

Product in Enzyme-catalyzed Reactions (28 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
malonate semialdehyde + coenzyme A + NADP+ = malonyl-CoA + NADPH + H+
-
show the reaction diagram
acetyl-CoA + oxaloacetate = malonyl-CoA + pyruvate
-
-
show the reaction diagram
acetyl-CoA + malonate = malonyl-CoA + acetate
-
-
show the reaction diagram
apiin + malonyl-CoA = apigenin 7-O-apiosylglucoside -6''-O-malonylester + malonyl-CoA
-
-
show the reaction diagram
malonyl-L-carnitine + CoA = malonyl-CoA + L-carnitine
-
-
show the reaction diagram
malonylcarnitine + CoASH = malonyl-CoA + L-(-)carnitine
-
-
show the reaction diagram
ATP + malonate + CoA = ADP + phosphate + malonyl-CoA
-
show the reaction diagram
ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA
-
-
show the reaction diagram
ATP + acetyl-CoA + HCO3- = ADP + malonyl-CoA + phosphate
-

Activator in Enzyme-catalyzed Reactions (4 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (89 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
2.4 mM, no inhibition of NADP+-dependent reaction, 14% inhibition of NAD+-dependent reaction
-
inhibition of mitochondrial enzyme and cytosolic enzyme to a much lower extent than with acetyl-CoA
-
non-competitive
-
noncompetitive inhibitor
-
product inhibition
-
regulatory role, enzyme belongs to the group of malonyl-CoA inhibitable carnitine acyltransferases with highly conserved residues being involved in the inhibition, i.e. Thr314, Asn464, Ala478, Met593, and Cys608, amino acid sequence comparison with enzymes from other species
-
double mutant H131A/H340A is insensitive to malonyl-CoA
-
inhibits the purified enzyme, inhibition is affected by buffer, pH, substrate and presence or absence of bovine serum albumin
-
microsomal COT, no inhibition of the mitochondrial enzyme
-
IC50: 0.0005 mM for the recombinant wild-type enzyme, IC50: 0.00052 mM for the recombinant revertant A305C, IC50 values of recombinant mutant isozymes M-CPT I, overview
-
inhibition of isoform L-CPT I is increased by 2[6-(4-chlorophenoxy)hexyl]oxirane-2-carboxylic acid
-
inhibition is pH-dependent; inhibition is temperature dependent
-
IC50: 906 nM
-
IC50: 0.0123 for wild-type enzyme, 0.015 mM for mutant enzyme T314S, 0.0087 mM for mutant enzyme N464D, 0.0395 mM for mutant enzyme A478G, 0.0275 mM for mutant enzyme C608A, 0.319 mM for mutant enzyme M593 mM, 0.155 mM for mutant enzyme M593A, 0.22 mM for mutant enzyme M593E
-
IC50: 0.0073 mM for the recombinant wild-type isozyme CPT1A, IC50: 0.0384 mM for CPT1A mutant R243T, IC50 values of other mutants, overview, determination of two binding sites, the A site and the O site, the latter involved residue Arg243, binding structure, interactions between N- and C-terminal residues are involved in malonyl-CoA binding to the A site, isozyme CPT1A in malonyl-CoA molecular docking, overview
-
IC50: 0.00339 mM for wild-type enzyme, 0.00021 mM for mutant enzyme E590A, 0.00039 mM for mutant enzyme E590Q, 0.00025 mM for mutant enzyme E590K
-
CPTo
-
IC50 for wild-type L-CPT-1 is 0.0298 mM; IC50 for wild-type M-CPT-1 is 0.010 mM
-
Triton X-100 protects
-
CPT II not inhibited; mitochondrial isozyme CPT I, sensitivity against malonyl-CoA is mediated by a 86 kDa malonyl-CoA binding protein complexed with CPT and other proteins of the beta-oxidation, detergent and salt sensitive
-
has a regulatory role in vivo
-
Glu3, Leu23, and Ser24 in M-CPTI are important for malonyl-CoA inhibition and binding but not for calalysis. IC50: 0.00007 mM for wild-type enzyme, 0.01 mM for mutant enzyme E3A, 0.00015 for mutant enzyme H5A, 0.01 mM for mutant enzyme E3A/V19A/L23A/S24A, 0.0068 mM for mutant enzyme E3A/H5A/V19A/L23A/S24A
-
differences in sensitivity of hepatic and heart enzyme; inhibits CPT I not CPT II; isoforms L-CPT I and M-CPT I
-
differences in sensitivity of hepatic and heart enzyme
-
inhibition of soluble peroxisomal form, no inhibition of enzyme from inner mitochondrial membrane
-
inhibits CPT I not CPT II; isoforms L-CPT I and M-CPT I
-
inhibits CPT I not CPT II; regulatory role in vivo
-
L-CPT I
-
L-CPT I, recombinant enzyme from Saccharomyces cerevisiae is inhibited only in intact mitochondria, not as solubilized enzyme
-
mitochondrial isozyme CPT I, sensitivity against malonyl-CoA is mediated by a 86 kDa malonyl-CoA binding protein complexed with CPT and other proteins of the beta-oxidation, detergent and salt sensitive
-
mitochondrial isozyme CPT I, sensitivity against malonyl-CoA is mediated by a 86 kDa malonyl-CoA binding protein complexed with CPT and other proteins of the beta-oxidation, detergent and salt sensitive; regulatory role in vivo
-
no inhibition
-
overview: recombinant chimeric proteins of L-CPT I and M-CPT I
-
partial proteolysis of CPT I greatly diminishes the inhibitory effect
-
phosphorylation of the CKII site in the C-terminal end of CPT-I leads to decreased malonyl-CoA sensitivity
-
reversible inhibition
-
sensitivity to inhibition of deletion and chimeric L-CPT I mutants
-
similar inhibition of wild-type CPT I and mutants A381D and H473A
-
the activity of CPT I is largely controlled by cytosolic levels of its biological inhibitor malonyl-CoA, being a key regulator of fatty acid partitioning in skeletal muscle by virtue of its ability to inhibit CPT I
-
benzyl alcohol, isoamyl alcohol and 2-(2-methoxyethoxy)ethyl-8-(cis-2-n-octylpropyl)octanoate decrease the ability of malonyl-CoA to inhibit CPT I; inhibition is temperature dependent
-
a malonyl-CoA insensitive enzyme and a malonyl-CoA sensitive enzyme
-
a malonyl-CoA insensitive enzyme and a malonyl-CoA sensitive enzyme; enzyme from liver mitochondrial inner membrane becomes inhibitable by malonyl-CoA if reconstituted with outer membrane malonyl-CoA binding protein; mitochondrial isozyme CPT I, sensitivity against malonyl-CoA is mediated by a 86 kDa malonyl-CoA binding protein complexed with CPT and other proteins of the beta-oxidation, detergent and salt sensitive; no inhibition
-
a physiological CPT1 inhibitor
-
allosteric inhibition
-
CPT II not inhibited; CPT I, native and reconstituted in phospholipid micelles
-
complete inhibition at 0.05 mM; complete inhibition at 0.05 mM; complete inhibition at 0.05 mM; complete inhibition at 0.05 mM
-
CPT I, sensitivity is reduced in vivo during gamma-linolenic acid treatment; membrane or micelle composition and properties influence the sensitivity of CPT I to inhibition
-
CPT I; membrane or micelle composition and properties influence the sensitivity of CPT I to inhibition; regulatory role in vivo
-
CPT I; regulatory role in vivo
-
CPT I; CPT I catalytic activity and malonyl-CoA sensitivity is located on 1 single polypeptide; CPT II not inhibited; recombinant CPT I is highly sensitive, recombinant CPT II not
-
CPT I; isoforms L-CPT I and M-CPT I
-
CPT I; inhibition is very pH-dependent: malonyl-CoA concentrations causing 50% inhibition at pH 6.0, 6.5, 7.0, 7.5 and 8.0 are 0.00004, 0.001, 0.009, 0.04 and 0.2 mM, respectively
-
CPT I; CPT II not inhibited; reversible inhibition
-
CPT I; CPT I, inhibition depends on age; inhibition is temperature dependent; regulatory role in vivo
-
CPT I; CPT II not inhibited; regulatory role in vivo
-
inhibition of MCT1 at 0.01 mM and inhibition of both isozymes at 0.02 mM and 0.04 mM; inhibits both MCT1 and MCT2
0.1 mM, 11 inhibtion
-
substrate inhibition above 0.05 mM
competitive, malonyl-transferase reaction
0.4 mM, 70% inhibition
-
0.2 mM, 83% residual activity
-
inhibition at higher concentrations; inhibition at higher concentrations
-
competitive versus ATP, uncompetitive versus pantothenate
-
feedback inhibition, regulatory function, isozyme PanK3, slight inhibition of isozyme PanK1beta
-
effective inhibitor
-
0.075 mM, complete inhibition of PAK I
-
competitive inhibition
competitive
-
competitive inhibition versus acetyl-CoA
-
product inhibition, competitive to acetyl-CoA; product inhibition, competitive to acetyl-CoA
-
product inhibition, competitive to acetyl-CoA
-
inhibits acetyl-CoA carboxylase activity 50 to 57% and propionyl-CoA carboxylase activity 11 to 13%
-
0.5 mM, 50-57% inhibition of acetyl-CoA carboxylase
-
0.5 mM, 60% inhibition of propionyl-CoA carboxylase
-
activity on propanoyl-CoA is more strongly inhibited than activity of acetyl-CoA
-

3D Structure of Enzyme-Ligand-Complex (PDB) (16 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (124 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
55°C, pH 7.8
50
-
per subunit, pH 7.8, 65°C
2
8
cosubstrate genistein 7-O-glucoside, pH 7.2, 30°C
pH 7.0, 30°C
pH 7.0, 30°C, recombinant His-tagged BPS
0.058
-
-
8.8
-
pH 7.0, 30°C, value is obtained by measurement of formation of pelargonidin 3-O-(6'-O-malonyl-beta-D-glucoside)
7.3
-
cyanidin 3-O-[[2-O-(2-O-sinapoyl)-beta-D-xylosyl]-6-O-(6-O-(4-coumaroyl)-beta-D-glucoside)] 5-O-beta-D-glucoside as co-substrate, pH 7.1, 25°C
0.0013
-
cyanidin 3-O-[[2-O-beta-D-xylosyl]-6-O-(6-O-(4-coumaroyl)-beta-D-glucoside)] 5-O-beta-D-glucoside as co-substrate, pH 7.1, 25°C
0.2
-
R206G mutant protein, donor lauroyl-CoA, 0.1 mM lauroyl-CoA, pH 6.5, 25°C
0.022
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.042
-
at pH 9.5 and 50°C
0.008
-
pH 8.0, 30°C, recombinant wild-type enzyme
0.0296
-
pH 9.5, 35°C
0.0077
-
pH 8.5, temperature not specified in the publication
0.55
-
pH 6.5, 30°C
0.92
-
pH 7.5, 37°C, recombinant enzyme
0.0112
-
pH 7.0, 30°C
0.0582
-
pH 7.0, 35°C, mutant T135L enzyme
0.0068
-
pH 7.0, 35°C, wild-type enzyme
0.055
-
native enzyme, at pH 7.0 and 30°C
0.55
-
recombinant enzyme, at pH 7.0 and 30°C
0.76
-
pH 7.8, 22°C
1.7
-
at pH 7.5 and 22°C
0.008
-
in 100 mM Tris-HCl (pH 7.5), 1 mM EDTA, 1 mM 2-mercaptoethanol, at 30°C
0.013
-
mutant enzyme C171S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
46.5
-
mutant enzyme C184S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
79.2
-
mutant enzyme Y224C, at pH 7.4 and 30°C
0.005
-
mutant enzyme Y224F, at pH 7.4 and 30°C
0.018
-
mutant enzyme Y224L, at pH 7.4 and 30°C
mutant enzyme Y224M, at pH 7.4 and 30°C
0.002
-
wild type enzyme, at pH 7.4 and 30°C
wild type enzyme, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
45.7
-
pH 7.5, 24°C, mutant enzyme C160S
0.0029
-
pH 7.5, 24°C, wild-type enzyme
0.0135
-
at pH 7.5 and 37°C
0.4
-
mutant enzyme A289R, pH and temperature not specified in the publication
0.13
-
mutant enzyme K210L, pH and temperature not specified in the publication
0.21
-
mutant enzyme K210L/Y256R, pH and temperature not specified in the publication
0.11
-
mutant enzyme Y256R, pH and temperature not specified in the publication
0.2
-
mutant enzyme Y256R/A289R, pH and temperature not specified in the publication
0.08
-
pH and temperature not specified in the publication
0.17
-
wild type enzyme, pH and temperature not specified in the publication
0.12
-
cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C
0.4
-
mutant enzyme S726F, at pH 7.0 and 30°C
0.102
-
mutant enzyme R206G, at pH 8.5 and 25°C
0.021
-
wild type enzyme, at pH 8.5 and 25°C
0.042
-
25°C, pH 7.5
0.12
-
acyl carrier protein mutant E20A, pH 7.5, 25°C
0.00027
-
acyl carrier protein mutant Q66R, pH 7.5, 25°C
0.0015
-
acyl carrier protein mutant Q67R, pH 7.5, 25°C
0.0011
-
acyl carrier protein mutant T65A, pH 7.5, 25°C
0.00032
-
hexahistidine-tagged fusion protein, reaction with E. coli acyl-carrier-protein
420
-
hexahistidine-tagged fusion protein, reaction with Streptomyces coelicolor acyl-carrier-protein
450
-
mutant enzyme R117A, pH and temperature not specified in the publication
8.5
-
pH 6.8, recombinant mutant A197D
70
-
pH 6.8, recombinant mutant F200A
0.94
-
pH 6.8, recombinant mutant F200S
0.15
-
pH 6.8, recombinant mutant F200Y
3
6
pH 6.8, recombinant mutant M126I
3
-
pH 6.8, recombinant mutant M137L
0.3
-
pH 6.8, recombinant mutant Q9A
0.7
-
pH 6.8, recombinant mutant R122A
0.35
-
pH 6.8, recombinant mutant R122K
11
-
pH 6.8, recombinant mutant T57V
25
-
pH 6.8, recombinant mutant V98Q
95
-
pH 6.8, recombinant mutants G198A
12
-
pH 6.8, recombinant mutants G198Y
0.4
-
pH 6.8, recombinant wild-type enzyme
100
-
R606A mutant
0.01
-
R606K mutant
0.12
-
reaction with E. coli acyl-carrier-protein
1580
-
wild type enzyme, pH and temperature not specified in the publication
2100
-
wild-type
1.2
-
wild-type acyl carrier protein, pH 7.5, 25°C
0.00047
-
wild-type enzyme, pH and temperature not specified in the publication
2100
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
0.35
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.12
-
cosubstrate 5-aminosalicylate, pH 7.5, temperature not specified in the publication
9.7
-
at pH 7.5 and 40°C
0.071
-
in the absence of chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C
0.59
-
in the presence of 0.001 mM chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C
0.14
-
mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication
0.038
-
mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication
0.055
-
mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication
0.063
-
pH 9.5, 35°C
0.071
-
wild type enzyme, at pH 8.0, temperature not specified in the publication
0.082
-
cosubstrate kanamycin A, pH 7.6, 25°C
5.7
-
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
9
-
didomain construct bearing mutation R606A, pH not specified in the publication, 25°C
5
-
didomain construct, pH not specified in the publication, 25°C
15.6
-
mutant enzyme K1699A
0.32
-
mutant enzyme K1699Q
0.3
-
R606A mutant
0.00167
-
R606K mutant
0.0002
-
wild-type enzyme
pH 7.5, 22°C
-
0.014
-
at pH 7.5 and 30°C
0.017
-
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
3.3
-
pH 7.5, 37°C
9.6
-
wild-type protein, pH7.5, 25°C
0.066
-
-
47.3
-
full-length and N-terminal truncated apo-hMCD
13
28
pH 8.5, temperature not specified in the publication, mutant C206S, 0.2 M H2O2
114.2
-
pH 8.5, temperature not specified in the publication, mutant C206S, 00.1 M H2O2
141.2
-
pH 8.5, temperature not specified in the publication, mutant C206S, no H2O2
117.1
-
pH 8.5, temperature not specified in the publication, mutant C206S/C243S, 0.1 M H2O2
175.4
-
pH 8.5, temperature not specified in the publication, mutant C206S/C243S, 0.2 M H2O2
167.1
-
pH 8.5, temperature not specified in the publication, mutant C206S/C243S, no H2O2
162.5
-
pH 8.5, temperature not specified in the publication, mutant C243S, 0.1 M H2O2
137.5
-
pH 8.5, temperature not specified in the publication, mutant C243S, 0.2 M H2O2
208.3
-
pH 8.5, temperature not specified in the publication, mutant C243S, no H2O2
94.6
-
pH 8.5, temperature not specified in the publication, mutant E302G, no H2O2
13.3
-
pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.05 M H2O2
128.3
-
pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.1 M H2O2
135
-
pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.2 M H2O2
109.2
-
pH 8.5, temperature not specified in the publication, wild-type enzyme, no H2O2
141.2
-

KM Value (261 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
55°C, pH 7.8
0.03
-
pH 7.8, 65°C
-
0.035
-
pH 6.0
1.9
-
cosubstrate genistein 7-O-glucoside, pH 7.2, 30°C
-
0.005
-
isozyme PDSTS2
0.006
-
isozyme PDSTS3
0.024
-
mutant T135L
0.0087
-
pH 7.0, 30°C, recombinant His-tagged BPS
0.01638
-
pH 7.0, 35°C, recombinant enzyme
0.0231
-
wild-type
0.031
-
2-(3,4-dihydroxyphenyl)-3-[[6-O-[(2E)-3-[4-(beta-D-glucopyranosyloxy)phenyl]prop-2-enoyl]-beta-D-glucopyranosyl-(1-6)-[2-O-[(2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoyl]-beta-D-xylopyranosyl-(1-2)]-beta-D-glucopyranosyl]oxy]-7-hydroxychromenium-5-yl beta-D-glucopyranoside as cosubstrate
0.0021
-
2-(3,4-dihydroxyphenyl)-3-[[6-O-[(2E)-3-[4-(beta-D-glucopyranosyloxy)phenyl]prop-2-enoyl]-beta-D-glucopyranosyl-(1-6)-[beta-D-xylopyranosyl-(1-2)]-beta-D-glucopyranosyl]oxy]-7-hydroxychromenium-5-yl beta-D-glucopyranoside as cosubstrate
0.0153
-
-
0.033
-
isozyme I
0.013
-
isozyme II
0.005
-
partially purified enzyme
0.0328
-
pH 7.0, 30°C
0.0188
-
cyanidin 3-O-[[2-O-(2-O-sinapoyl)-beta-D-xylosyl]-6-O-(6-O-(4-coumaroyl)-beta-D-glucoside)] 5-O-beta-D-glucoside as co-substrate, pH 7.1, 25°C
0.0021
-
cyanidin 3-O-[[2-O-beta-D-xylosyl]-6-O-(6-O-(4-coumaroyl)-beta-D-glucoside)] 5-O-beta-D-glucoside as co-substrate, pH 7.1, 25°C
0.0153
-
pH 7, 30°C, bisdemalonylsalvianin as cosubstrate
0.057
-
pH 7, 30°C, shisonin as cosubstrate, D171A mutant Ss5MaT1
0.071
-
pH 7, 30°C, shisonin as cosubstrate, H167A mutant Ss5MaT1
0.0064
-
pH 7, 30°C, shisonin as cosubstrate, K258A mutant Ss5MaT1
0.02
-
pH 7, 30°C, shisonin as cosubstrate, N315A mutant Ss5MaT1
0.025
-
pH 7, 30°C, shisonin as cosubstrate, native Ss5MaT1
0.0141
-
pH 7, 30°C, shisonin as cosubstrate, Q150A mutant Ss5MaT1
0.014
-
pH 7, 30°C, shisonin as cosubstrate, R301A mutant Ss5MaT1
0.035
-
pH 7, 30°C, shisonin as cosubstrate, recombinant Ss5MaT1
0.0219
-
pH 7, 30°C, shisonin as cosubstrate, wild-type Ss5MaT1
0.022
-
pH 7, 30°C, shisonin as cosubstrate, Y45A mutant Ss5MaT1
0.013
-
pH 7.0, 35°C
pH 7.0, 37°C
-
0.0055
-
R206G mutant protein, donor lauroyl-CoA, 0.1 mM lauroyl-CoA, pH 6.5, 25°C
0.0283
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.51
-
-
0.05
-
pH 7.0
0.016
-
pH 8.0, 25°C
0.028
-
pH 8.0, 30°C, reaction with acetyl-CoA and malonyl-CoA
0.028
-
pH 8.0, 30°C, reaction with malonyl-CoA, without acetyl-CoA
0.028
-
pH 6.5-7.0, 35°C, BIS1
0.0062
-
pH 6.5-7.0, 35°C, BIS2
0.01
-
pH 6.5-7.0, 35°C, BIS3
0.0101
-
at pH 9.5 and 50°C
0.04117
-
pH 8.0, 30°C
0.001
-
pH 8.0, 30°C, recombinant wild-type enzyme
0.0233
-
pH 9.5, 35°C
0.041
-
pH 8.5, temperature not specified in the publication
0.0069
-
pH 6.5, 30°C
0.588
-
pH 7.5, 37°C, recombinant enzyme
0.0084
-
pH 7.0, 30°C
0.0164
-
pH 7.0, 35°C, mutant T135L enzyme
0.0087
-
pH 7.0, 35°C, wild-type enzyme
0.0313
-
pH 7.0, 37°C
0.0028
-
native enzyme, at pH 7.0 and 30°C
0.0069
-
recombinant enzyme, at pH 7.0 and 30°C
0.0046
-
pH 7.8, 22°C
0.0027
-
pH 7.5, 37°C
0.104
-
pH and temperature not specified in the publication
0.0487
-
at pH 7.5 and 22°C
0.00358
-
in 100 mM Tris-HCl (pH 7.5), 1 mM EDTA, 1 mM 2-mercaptoethanol, at 30°C
0.93
-
mutant enzyme C171S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
0.0085
-
mutant enzyme C184S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
0.0014
-
mutant enzyme Y224C, at pH 7.4 and 30°C
0.012
-
mutant enzyme Y224F, at pH 7.4 and 30°C
0.0095
-
mutant enzyme Y224L, at pH 7.4 and 30°C
mutant enzyme Y224M, at pH 7.4 and 30°C
0.0171
-
wild type enzyme, at pH 7.4 and 30°C
wild type enzyme, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
0.0023
-
pH 7.5, 24°C, mutant enzyme C160S
0.13
-
pH 7.5, 24°C, wild-type enzyme
0.015
-
at pH 7.5 and 37°C
0.013
-
mutant enzyme A289R, pH and temperature not specified in the publication
0.0101
-
mutant enzyme K210L, pH and temperature not specified in the publication
0.0119
-
mutant enzyme K210L/Y256R, pH and temperature not specified in the publication
0.0135
-
mutant enzyme Y256R, pH and temperature not specified in the publication
0.0112
-
mutant enzyme Y256R/A289R, pH and temperature not specified in the publication
0.0103
-
pH and temperature not specified in the publication
0.0056
-
wild type enzyme, pH and temperature not specified in the publication
0.0131
-
cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C
0.05
-
mutant enzyme S726F, at pH 7.0 and 30°C
0.1176
-
mutant enzyme R206G, at pH 8.5 and 25°C
0.0283
-
wild type enzyme, at pH 8.5 and 25°C
0.51
-
25°C, pH 7.5
0.017
-
acyl carrier protein mutant E20A, pH 7.5, 25°C
0.02
-
acyl carrier protein mutant Q66R, pH 7.5, 25°C
0.049
-
acyl carrier protein mutant Q67R, pH 7.5, 25°C
0.033
-
acyl carrier protein mutant T65A, pH 7.5, 25°C
0.034
-
hexahistidine-tagged fusion protein, reaction with E. coli acyl-carrier-protein
0.327
-
hexahistidine-tagged fusion protein, reaction with Streptomyces coelicolor acyl-carrier-protein
0.06
-
mutant enzyme R117A, pH and temperature not specified in the publication
0.08
-
mutant H90A, Vmax (RFU/min): 39.65
0.0191
-
mutant N155A, Vmax (RFU/min): 63.06
0.0175
-
pH 6.8, 28°C
0.0228
-
pH 6.8, 28°C, recombinant enzyme
0.019
-
pH 6.8, recombinant mutant A197D
0.034
-
pH 6.8, recombinant mutant F200A
0.083
-
pH 6.8, recombinant mutant F200S
0.05
-
pH 6.8, recombinant mutant F200Y
0.095
-
pH 6.8, recombinant mutant M126I
0.023
-
pH 6.8, recombinant mutant M137L
0.015
-
pH 6.8, recombinant mutant Q9A
0.2
-
pH 6.8, recombinant mutant R122A
0.15
-
pH 6.8, recombinant mutant R122K
0.7
-
pH 6.8, recombinant mutant T57V
0.4
-
pH 6.8, recombinant mutant V98Q
0.032
-
pH 6.8, recombinant mutants G198Y and G198A
0.06
-
pH 6.8, recombinant wild-type enzyme
0.019
-
pH 7.5, 37°C
0.016
-
ping-pong mechanism
R606A mutant
0.0162
-
R606K mutant
0.0013
-
reaction with E. coli acyl-carrier-protein
0.25
-
recombinant enzyme
0.0126
-
recombinant enzyme, pH 6.8, temperature not specified in the publication
0.01733
-
S97A mutant
0.0239
-
sequential mechanism
wild type enzyme, pH and temperature not specified in the publication
0.06
-
wild-type
0.0019
-
wild-type acyl carrier protein, pH 7.5, 25°C
0.049
-
wild-type and mutant
0.011
-
wild-type enzyme
0.0208
-
wild-type enzyme, pH and temperature not specified in the publication
0.06
-
wild-type enzyme, Vmax (RFU/min): 123
0.0167
-
-
0.0055
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
0.009
-
in presence of [acyl-carrier-protein]
0.004
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.153
-
without [acyl-carrier-protein]
0.016
-
cosubstrate 5-aminosalicylate, pH 7.5, temperature not specified in the publication
0.486
-
37°C, pH 7.2
35
-
at pH 7.5 and 40°C
0.02283
-
isozyme AI
0.002
-
isozyme AII
0.0019
-
mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication
0.0579
-
mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication
0.0397
-
mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication
0.0374
-
pH 7.0, 35°C, mutant enzyme L263M/F265Y/S338G
0.0099
-
pH 7.0, 35°C, wild-type enzyme
0.0108
-
pH 7.0, 37°C
0.0128
-
pH 9.5, 35°C
0.2283
-
wild type enzyme, at pH 8.0, temperature not specified in the publication
0.0308
-
cosubstrate kanamycin A, pH 7.6, 25°C
0.234
-
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.477
-
pH 8.0, 30°C, cosubstrate: sisomycin
0.58
-
reaction with tobramycin, wild-type enzyme
0.82
-
25°C, pH 7.0, mutant enzyme K1699A
0.003
-
25°C, pH 7.0, mutant enzyme K1699Q
0.001
-
25°C, pH 7.0, wild-type enzyme
0.006
-
alcohol-fed animals
0.1
-
didomain construct bearing mutation R606A, pH not specified in the publication, 25°C
0.018
-
didomain construct, pH not specified in the publication, 25°C
0.00128
-
R606A mutant
0.0162
-
R606K mutant
0.0013
-
wild-type enzyme
0.0019
-
-
0.04
-
in presence of polysaccharide
0.0096
-
malonyl-CoA decarboxylation
0.031
-
malonyl-CoA decarboxylation, P375G mutant enzyme
0.022
-
P375G mutant enzyme
0.00086
-
-
0.5
-
pH 7.5, 22°C
pH 7.8, 30°C, cosubstrate 3-hydroxy-3-methylglutarate
0.52
-
pH 7.8, 30°C, cosubstrate adipate
0.33
-
pH 7.8, 30°C, cosubstrate glutarate
0.13
-
pH 7.8, 30°C, cosubstrate methylmalonate
0.7
-
pH 7.8, 30°C, cosubstrate succinate
0.55
-
pH 8.5, 30°C, cosubstrate 3-hydroxy-3-methylglutarate
0.37
-
pH 6.0, 30°C
0.7
-
-
0.1423
-
at pH 7.5 and 30°C
0.188
-
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.14
-
pH 7.5, 37°C
0.0232
-
wild-type protein, pH7.5, 25°C
0.28
-
full-length and N-terminal truncated apo-hMCD
0.33
0.52
gastrocnemius after 5 min of contraction
0.119
-
gastrocnemius, relaxed
0.19
-
in 100 mM potassium phosphate buffer (pH 8.5) and 1 mM thiophenol, at 60°C
0.202
-
in presence of 150 mM PO43-
0.065
-
in presence of 40 mM PO43-
0.146
-
pH 7, recombinant MCD
0.068
-
pH 8.5, temperature not specified in the publication, mutant C206S, 0.2 M H2O2
0.79
-
pH 8.5, temperature not specified in the publication, mutant C206S, 00.1 M H2O2
1.04
-
pH 8.5, temperature not specified in the publication, mutant C206S, no H2O2
0.73
-
pH 8.5, temperature not specified in the publication, mutant C206S/C243S, 0.1 M H2O2
0.99
-
pH 8.5, temperature not specified in the publication, mutant C206S/C243S, 0.2 M H2O2
0.8
1
pH 8.5, temperature not specified in the publication, mutant C206S/C243S, no H2O2
1.16
-
pH 8.5, temperature not specified in the publication, mutant C243S, 0.1 M H2O2
0.68
-
pH 8.5, temperature not specified in the publication, mutant C243S, 0.2 M H2O2
0.56
-
pH 8.5, temperature not specified in the publication, mutant C243S, no H2O2
0.58
-
pH 8.5, temperature not specified in the publication, mutant E302G, no H2O2
0.22
-
pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.05 M H2O2
0.46
-
pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.1 M H2O2
0.42
-
pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.2 M H2O2
0.35
-
pH 8.5, temperature not specified in the publication, wild-type enzyme, no H2O2
0.83
-
-
0.016
-
pH 8.0, recombinant mutant enzymes
0.75
-
pH 8.0, recombinant subunits AccA and AccD
pH 8.0, recombinant wild-type enzyme
0.075
-
at 20 mM NaCl
0.035
-

Ki Value (13 results)

COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
24°C, pH 7.8, inhibition of NAD+-dependent reaction
0.4
-
-
0.021
-
pH and temperature not specified in the publication
0.021
-
peroxisomal COT
0.0064
-
pH 6.8
0.0035
-
pH 7.4
0.106
-
KI-values: 0.00064 mM and 0.0007 mM malony-CoA (from secondary Dixon plots)
0.00067
-
pH 6.0, 30°C
0.6
-
recombinant enzyme, pH 8.0, 30°C
1.6
-
pH and temperature not specified in the publication
66.63
-
-
0.009
-

IC50 Value (54 results)

COMMENTARY
EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
LITERATURE
pH 7.5, 30°C
2
-
mitochondrial isolate from liver, high saturated fat diet
0.00011
-
IC50: 0.0005 mM for the recombinant wild-type enzyme
0.0005
-
IC50: 0.00052 mM for the recombinant revertant A305C, IC50 values of recombinant mutant isozymes M-CPT I overview
0.00052
-
IC50: 0.00339 mM for wild-type enzyme, 0.00021 mM for mutant enzyme E590A, 0.00039 mM for mutant enzyme E590Q, 0.00025 mM for mutant enzyme E590K
0.00339
-
IC50: 0.0073 mM for the recombinant wild-type isozyme CPT1A, IC50: 0.0384 mM for CPT1A mutant R243T, IC50 values of other mutants, overview, determination of two binding sites, the A site and the O site, the latter involved residue Arg243, binding struct
0.0073
0.0384
IC50: 0.0123 for wild-type enzyme
0.0123
-
IC50: 906 nM
0.000906
-
mitochondria isolated from 24-h-old, fasted pig, pH 7.2, 30°C
0.00053
-
mitochondria isolated from 24-h-old, fed pig, pH 7.2, 30°C
0.00026
-
mitochondria isolated from adult pig, pH 7.2, 30°C
0.00021
-
mitochondria isolated from newborn pig, pH 7.2, 30°C
0.00019
-
mitochondrial isolate
0.0768
-
mitochondrial isolate from liver, control diet
0.00012
-
mitochondrial isolate from liver, high polyunsaturated fat diet
0.00007
-
IC50 for wild-type M-CPT-1 is 0.010 mM
0.01
-
mitochondrial isolate from red muscle, control diet
0.00119
-
mitochondrial isolate from red muscle, high polyunsaturated fat diet
0.00035
-
mitochondrial isolate from red muscle, high saturated fat diet
0.00183
-
mitochondrial isolate, after incubation with protein kinase A
0.1103
-
protein with deletion of residue 1-18, mitochondrial preparation
0.03556
-
protein with deletion of residue 1-28, mitochondrial preparation
0.03919
-
wild-type protein, 0.198 mM carnitine, mitochondrial preparation
0.00055
-
wild-type protein, 0.683 mM carnitine, mitochondrial preparation
0.000117
-
wild-type protein, 1 mM carnitine, mitochondrial preparation
without pre-incubation with malonyl-CoA
0.1058
-
IC50 for wild-type L-CPT-1 is 0.0298 mM
0.0298
-
10 min pre-incubation with malonyl-CoA
0.0252
-
at 0.035 mM palmitoyl-CoA
at 0.07 mM palmitoyl-CoA
chimeric protein: residues 1-128 of human enzyme recombined with pig enzyme, mitochondrial preparation
0.000359
-
chimeric protein: residues 1-128 of pig enzyme recombined with human enzyme, mitochondrial preparation
0.000325
-
chimeric protein: residues 1-50 of human enzyme recombined with pig enzyme, mitochondrial preparation
0.000457
-
chimeric protein: residues 1-50 of pig enzyme recombined with human enzyme, mitochondrial preparation
0.00019
-
CPT I, heart
0.0004
-
CPT I, liver
0.000079
-
CPT I, red muscle
0.00055
-
CPT I, white muscle
0.00037
-
D17E mutant protein, 0.770 mM carnitine, mitochondrial preparation
0.000246
-
D17E mutant protein, 1 mM carnitine, mitochondrial preparation
0.000279
-
E17D mutant protein, 0.606 mM carnitine, mitochondrial preparation
0.000284
-
E17D mutant protein, 1 mM carnitine, mitochondrial preparation
0.000297
-
Glu3, Leu23, and Ser24 in M-CPTI are important for malonyl-CoA inhibition and binding but not for calalysis. IC50: 0.00007 mM for wild-type enzyme, 0.01 mM for mutant enzyme E3A, 0.00015 for mutant enzyme H5A, 0.01 mM for mutant enzyme E3A/V19A/L23A/S24A,
0.00007
-
IC50 0.0087 mM for mutant enzyme N464D
0.0087
-
IC50 0.015 mM for mutant enzyme T314S
0.015
-
IC50 0.0275 mM for mutant enzyme C608A
0.0275
-
IC50 0.0395 mM for mutant enzyme A478G
0.0395
-
IC50 0.155 mM for mutant enzyme M593A
0.155
-
IC50 0.319 mM for mutant enzyme M593 mM
0.319
-

References & Links