Ligand glyoxylate

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Basic Ligand Information

Molecular Structure
Picture of glyoxylate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C2H2O3
glyoxylate
HHLFWLYXYJOTON-UHFFFAOYSA-N
Synonyms:
CHO-COOH, glyocylate, glyoxalate, glyoxalic acid, glyoxylic acid, oxoacetic acid
Pathway Source
Pathways


Show all pahtways known for Show all BRENDA pathways known for glyoxylate

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
glyoxylic acid + O2 + H2O = oxalate + H2O2
-
show the reaction diagram
glyoxylate + NH3 + NADH = glycine + H2O + NAD+
-
show the reaction diagram
propanoyl-CoA + glyoxylate = 2-hydroxyglutarate + CoA
-
show the reaction diagram
butanoyl-CoA + H2O + glyoxylate = 3-ethylmalate + CoA
-
show the reaction diagram
glyoxylate + L-aspartate = glycine + oxaloacetate
-
show the reaction diagram
glyoxylate + L-glutamate = glycine + 2-oxoglutarate
-
show the reaction diagram
an aromatic amino acid + glyoxylate = an aromatic oxo acid + glycine
-
show the reaction diagram
4-aminobutanoate + glyoxylate = succinate semialdehyde + glycine
-

In Vivo Product in Enzyme-catalyzed Reactions (54 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
nitrilotriacetate + FMNH2 + H+ + O2 = iminodiacetate + glyoxylate + FMN + H2O
-
-
show the reaction diagram
glyoxal + H2O + O2 = glyoxylate + H2O2
-
-
show the reaction diagram
glycine + H2O + NAD+ = glyoxylate + NH3 + NADH + H+
-
show the reaction diagram
glycine + ferricytochrome c = glyoxylate + ferrocytochrome c + NH3
-
-
show the reaction diagram
Gly + H2O + O2 = glyoxylate + NH3 + H2O2
-
-
show the reaction diagram
allantoate + 3 H2O = glyoxylate + 4 NH3 + 2 CO2
-
-
show the reaction diagram
4-Hydroxy-2-oxoglutarate = Pyruvate + glyoxylate
-

Substrate in Enzyme-catalyzed Reactions (368 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
glyoxylate + NADPH = glycolate + NADP+
-
show the reaction diagram
glyoxylate + NADPH + H+ = glycolate + NADP+
-
show the reaction diagram
glyoxylate + NADH + H+ = 2-hydroxypropanoate + NAD+
-
show the reaction diagram
glyoxylic acid + NADPH + H+ = ? + NADP+
-
show the reaction diagram
glyoxylate + NAD(P)H = glycolic acid + NAD(P)+
-
show the reaction diagram
glyoxylate + O2 = oxalate + H2O2
-
show the reaction diagram
glyoxylate + acceptor = oxalate + reduced acceptor
-
show the reaction diagram
glyoxylate + NAD+ = ? + NADH
-
show the reaction diagram
glyoxylate + NADH = glyoxal + NAD+
-
show the reaction diagram
glyoxylic acid + NAD+ + H2O = 2-phenylbenzoate + NADH + H+
-
show the reaction diagram
glyoxylic acid + NAD+ + H2O = oxalic acid + NADH
-
show the reaction diagram
glyoxylate + O2 = CO2 + CO2
-
show the reaction diagram
glyoxylic acid + H2O + O2 = ?
-
show the reaction diagram
glyoxylic acid + O2 + H2O = oxalate + H2O2
-
show the reaction diagram
glyoxylate + CoA + 2 oxidized methyl viologen = ?
-
show the reaction diagram
glyoxylate + methyl viologen = ?
-
show the reaction diagram
glyoxylate + CoA + 2 oxidized methyl viologen = formyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
show the reaction diagram
glyoxylate + CoA + oxidized ferredoxin = formyl-CoA + CO2 + reduced ferredoxin
-
show the reaction diagram
glyoxylate + benzyl viologen = oxalic acid + reduced benzyl viologen
-
show the reaction diagram
L-Arg + glyoxylate + NADPH = ?
-
show the reaction diagram
L-Ala + glyoxylate + NADH = ?
-
show the reaction diagram
Taurine + glyoxylate + NADH = ?
-
show the reaction diagram
L-ornithine + glyoxylic acid + NADPH + H+ = ? + NADP+ + H2O
-
show the reaction diagram
glyocylate + methylamine + NADPH + H+ = sarcosine + NADP+
-
show the reaction diagram
L-Met + glyoxylate + NADH = ?
-
show the reaction diagram
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + glyoxylate + NADPH + H+ = ? + NADP+ + H2O
-
show the reaction diagram
L-lysine + glyoxylate + NADH = ?
-
show the reaction diagram
glyoxylate + 2-oxoglutarate = 5-hydroxy-4-oxopentanoic acid + 2 CO2
-
show the reaction diagram
acetyl-CoA + glyoxylate + H2O = ?
-
show the reaction diagram
pentanoyl-CoA + glyoxylate + H2O = 3-propylmalate + CoA
-
show the reaction diagram
butanoyl-CoA + H2O + glyoxylate = 3-ethylmalate + CoA
-
show the reaction diagram
phosphoenolpyruvate + glyoxylate = S-4-hydroxy-2-oxo-1,5-pentanedioate + R-4-hydroxy-2-oxo-1,5-pentanedioate + phosphate
-
show the reaction diagram
(S)-ureidoglycine + glyoxylate = N-carbamoyl-2-oxoglycine + glycine
-
show the reaction diagram
6-aminohexanoate + glyoxylate = 6-oxohexanoate + glycine
-
show the reaction diagram
L-alanine + glyoxylate = pyruvate + glycine
-
show the reaction diagram
L-ornithine + glyoxylate = DELTA1-pyrroline-5-carboxylate + glycine
-
show the reaction diagram
4-aminobutanoate + glyoxylate = 4-oxobutanoate + glycine
-
show the reaction diagram
L-tryptophan + glyoxylate = 3-indole-2-oxopropanoate + glycine
-
show the reaction diagram
L-histidine + glyoxylate = imidazol-5-yl-pyruvate + glycine
-
show the reaction diagram
(R)-3-amino-2-methylpropanoate + glyoxylate = 2-methyl-3-oxopropanoate + glycine
-
show the reaction diagram
L-glutamine + glyoxalate = 2-oxoglutaramate + glycine
-
show the reaction diagram
L-phenylalanine + glyoxylate = phenylpyruvate + glycine
-
show the reaction diagram
glyoxylate + (S)-(-)-1-phenylethylamine = ?
-
show the reaction diagram
taurine + glyoxylate = 2-sulfoacetaldehyde + glycine
-
show the reaction diagram
glyoxylate + L-aspartate = glycine + oxaloacetate
-
show the reaction diagram
L-alanine + glyoxylate = pyruvate + glycine
-
show the reaction diagram
Pyruvate + glyoxylate = ?
-
show the reaction diagram
Pyruvate + glyoxylate = ?
-
show the reaction diagram
Oxaloacetate + glyoxylate = 3-Oxalomalate
-
show the reaction diagram
pyruvate + glyoxylate = 4-hydroxy-2-oxoglutarate
-
show the reaction diagram
ATP + glyoxalate + CoA = ?
-

Product in Enzyme-catalyzed Reactions (219 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
glycolate + ferricytochrome c = glyoxylate + ferrocytochrome c
-
-
show the reaction diagram
glycolate + O2 = glyoxylate + H2O2
-
-
show the reaction diagram
glycine + O2 = oxoacetic acid + NH3
-
show the reaction diagram
trichloroethylene + O2 + NADPH = formate + glyoxylate + NADP+
-
show the reaction diagram
oxalate + NADH = glyoxylate + NAD+
-
-
show the reaction diagram
glyoxal + NAD+ + H2O = glyoxylate + NADH
-
-
show the reaction diagram
glyoxal + NAD+ + H2O = glyoxylate + NADH + H+
-
-
show the reaction diagram
glyoxal + H2O + O2 = glyoxylate + H2O2
-
-
show the reaction diagram
glyoxal + H2O + O2 = glyoxylate + H2O2
-
-
show the reaction diagram
glyoxal + ferricyanide = oxoacetic acid + ferrocyanide + H+
-
-
show the reaction diagram
glycine + H2O + O2 = glyoxylate + NH3 + H2O2
-
-
show the reaction diagram
dichloroacetate + glutathione = glyoxylate + HCl + ?
-
-
show the reaction diagram
glycine + 2-oxoglutarate = glyoxylate + L-glutamate
-
show the reaction diagram
2-oxoglutaramate + glycine = L-glutamine + glyoxylate
-
show the reaction diagram
pyruvate + glycine = L-alanine + glyoxylate
-
show the reaction diagram
glycine + 2-oxoglutarate = glyoxylate + glutamate
-
-
show the reaction diagram
dTDP-4-dehydro-6-deoxy-D-glucose + glycine = dTDP-4-amino-4,6-dideoxy-D-galactose + glyoxylate
-
-
show the reaction diagram
glycine + pyruvate = glyoxylate + L-alanine
-
-
show the reaction diagram
glycine + 4,5-dioxopentanoate = 5-aminolevulinate + glyoxylate
-
-
show the reaction diagram
glycine + 2-oxoglutarate = glyoxalate + L-glutamate
-
-
show the reaction diagram
pyruvate + glycine = L-alanine + glyoxylate
-
show the reaction diagram
(-)-ureidoglycolate = glyoxylate + urea
-
-
show the reaction diagram
allantoate + 3 H2O = glyoxylate + 4 NH3 + 2 CO2
-
-
show the reaction diagram
chlorofluoroacetic acid + ? = glyoxylate + ?
-

Activator in Enzyme-catalyzed Reactions (4 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (120 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
non-competitive inhibition, Ki: 83 mM
-
competitive inhibition
-
competitive inhibition, about 60% activity at 2 mM
-
slight inhibition
-
with oxaloacetate, concomitantly added
-
18% inhibition at 5 mM, mixed type inhibition together with oxaloacetate, completely at 5 mM each
-
20% inhibition at 1 mM, presence of 1 mM oxaloacetate results in 50% inhibition
-
plus oxaloacetate
-
10 mM, 55% inhibition of NADH linked hydroxypyruvate reduction, 15% of NADPH linked reduction, 80% of NAD+ linked glycerate oxidation
inhibition by excess substrate
substrate inhibition at concentrations above 4 mM
strain CETC 978, competitive inhibition
-
79% residual activity at 1 mM
-
strong, competitive to glycolate
-
competitive vs. pyruvate
-
inhibitory only in the absence of thiol reagents, competitive with respect to pyruvate
-
noncompetitive vs. pyruvate
-
weak
-
2-oxoglutarate dehydrogenase complex
-
competitive inhibitor
-
competitive inhibitor
-
1 mM, 33% inhibition
-
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
20 mM, about 40% of the original activity is lost. 2 mM glyoxylate inhibits 6%
-
weak
-
5 mM, 30% inhibition of reductive amination
-
at 20 mM, 30% inhibition
-
20 mM, more than 60% inhibition
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
-
inhibitor of octopine formation
-
weak
-
isozyme AHAS II
-
competitive, analysis of pH-dependence of inhibition
-
slight reduction of enzyme activity at high concentrations of glyoxylate
alpha-keto acid acceptor, inhibitor at high concentrations
-
at high concentration, transamination between albizziin and glyoxylate
-
weak
-
at high concentrations
-
competitive inhibition
-
above 5 mM
amino acid substrates partially protect
-
competitive vs. pyruvate
-
inhibited by glyoxylate above 6 mM
-
irreversible inhibition only in the presence of NH4+, inactivation in the absence of amino acid substrates
-
presence of D-serine protects against inhibition
-
5 mM, 79% of activity remaining; 5 mM, 83% of activity remaining
-
in combination with oxaloacetate
-
isoenzyme II, french bean
-
at concentrations greater than 0.05 mM
-
50% activity loss with 0.02 mM glycolate for 10 min at 30°C; strong inhibitor, 50% inhibition at 0.02 mM
-
complete inhibition
-
irreversible
-
mechanism-based inhibitor
-
7.2% residual activity at 8 mM
-
12% inhibition at 4 mM
-
competitive inhibition
-
linear competitive inhibitor
bovine enzyme inhibited at lower concentrations than E. coli enzyme
-
Ki: 1.5 mM
-
bovine enzyme inhibited at lower concentrations than E. coli enzyme
-
substrate inhibition. Glyoxylate competes for, and inhibits aldolase activity by reacting with, the one active-site lysine residue/subunit
-
competitive inhibition
-
determmination of an enzyme crystal structure with the inhibitor bound to the active Cys residue of the enzyme as a hemithioacetal, detailed binding structure analysis, overview
-
20 mM: 54.1% inhibition, not reversed by 5 mM AMP
-
20 mM, about 50% inhibition. Inhibition is not reversed by AMP
-
20 mM, 27% inhibition
-
-
-
32% residual activity at 10 mM
-
inhibits the activity in the acetate-forming direction
-
Ki: 0.04 mM
-

3D Structure of Enzyme-Ligand-Complex (PDB) (215 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (117 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
pH 6.5, 25°C
19
-
mutant T335A, cosubstrate NADH, pH 6.2, 25°C
59
-
mutant T335A, cosubstrate NADPH, pH 6.2, 25°C
0.52
-
mutant T335D, cosubstrate NADH, pH 6.2, 25°C
75
-
mutant T335D, cosubstrate NADPH, pH 6.2, 25°C
0.92
-
pH 7.0, 30°C, recombinant E141N/Q313E mutant formate dehydrogenase
2.3
-
pH 7.0, 37°C
1.35
-
pH 7.8, 22°C, recombinant His6-tagged enzyme
13
-
wild-type, cosubstrate NADH, pH 6.2, 25°C
68
-
wild-type, cosubstrate NADPH, pH 6.2, 25°C
0.56
-
30°C, pH 5.5, mutant enzyme N97D
50
-
30°C, pH 5.5, wild-type enzyme
270
-
pH 7.0, 30°C, recombinant enzyme
37°C, cofactor: NADH
67
-
37°C, cofactor: NADPH
27
-
isoform GLYR1, at pH 6.5 and 25°C
33.7
-
isoform GLYR1, at pH 7.5 and 25°C
30.9
-
isoform GLYR1, at pH 7.8 and 25°C
28.4
-
isoform GLYR2, at pH 7.1 and 25°C
10.8
-
isoform GLYR2, at pH 7.3 and 25°C
19.1
-
isoform GLYR2, at pH 7.8 and 25°C
18.4
-
pH 6.7, 45°C, cofactor NADH, purified recombinant enzyme
76000
-
pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme
65000
-
pH 7.5, 37°C, recombinant enzyme, with NADH
67
-
pH 7.5, 37°C, recombinant enzyme, with NADPH
27
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
22
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
11
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E
0.0052
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R
0.051
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
6.06
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
86.4
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
67.8
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enyzme
3407
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
54.6
-
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C
22.5
-
with as NADH as cofactor, pH 6.7, 45°C
760000
-
with as NADPH as cofactor, pH 6.7, 45°C
650000
-
with as NADPH as cofactor, pH 7.6, 30°C
22.5
-
with NADH as cosubstrate, at pH 4.0 and 45°C
530
-
with NADPH as cosubstrate, at pH 4.0 and 45°C
570
-
cosubstrate NADH, pH 7, 30°C
166
-
cosubstrate NADH, pH 7, 37°C
cosubstrate NADPH, pH 7, 30°C
52
-
cosubstrate NADPH, pH 7, 37°C
88
-
mutant E141N, 30°C, pH 7.0
0.36
-
mutant E141Q, 30°C, pH 7.0
0.023
-
wild-type, 30°C, pH 7.0
0.007
-
pH 6.9, 85°C, under argon
0.0133
-
pH 8.0, 22°C
0.074
-
at pH 6.5 and 37°C
5.29
-
L104V mutant
0.6
-
L81A mutant
0.19
-
L81V mutant
0.21
-
wild type LiCMS
0.51
-
wild-type
0.51
-
Y144L mutant
0.005
-
Y144V mutant
0.03
-
mutant C617S, pH 8.0, 37°C
42.4
-
mutant R338K, pH 8.0, 37°C
3.19
-
N-terminal malate synthase-active domain GCE(13-573) of glyoxylate cycle enzyme, at 25°C, pH not specified in the publication
14
-
wild type enzyme, at pH 7.5 and 25°C
23
-
wild type full-length glyoxylate cycle enzyme, at 25°C, pH not specified in the publication
17
-
wild-type, pH 8.0, 37°C
48.1
-
in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
9.7
-
pH 9, 25°C, fixed substrate: 4-aminobutanoate
pH 7.5, 30°C
48.2
-
TAT-peptide fusion protein, pH 7.4, 25°C
16
-
wild-type, pH 7.4, 25°C
42
-
F152I, pH not specified in the publication, temperature not specified in the publication
39
-
G41R, pH not specified in the publication, temperature not specified in the publication
20.5
-
G41V, pH not specified in the publication, temperature not specified in the publication
18.3
-
G82E, pH not specified in the publication, temperature not specified in the publication
0.068
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
45
-
major allele wild mutant enzyme F152A
22.6
-
major allele wild mutant enzyme F152I
39
-
major allele wild type enzyme
45
-
minor allele mutant enzyme F152I
40
-
minor allele wild type enzyme
37
-
mutant G82E, 25°C
0.068
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
37
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
40
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
11.1
-
pH 7.0, 50°C, L-alanine as amino donor
pH 7.4, 25°C, mutant enzyme G82E
0.068
-
pH 7.4, 25°C, wild-type enzyme
45
-
recombinant mutant F238S, pH 7.4, 25°C
35
-
recombinant mutant F240S, pH 7.4, 25°C
20
-
recombinant mutant I56N-Ma, pH 7.4, 25°C
30
-
recombinant mutant I56N-Mi, pH 7.4, 25°C
22
-
recombinant mutant P11R-Ma, pH 7.4, 25°C
23
-
recombinant mutant P11R/I56N-Ma, pH 7.4, 25°C
22
-
recombinant mutant R118A, pH 7.4, 25°C
19
-
recombinant wild-type enzyme AGT-Ma, pH 7.4, 25°C
45
-
recombinant wild-type enzyme AGT-Mi, pH 7.4, 25°C
wild-type, 25°C
45
-
-
113
-
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.71
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
3.64
-
pH 7.5, 38°C
0.19
-
pH 7.5, 45°C
263
-
forward reaction with 4-aminobutanoate, pH 9.0, 30°C
9.7
-
pH 9.0, 25°C
0.74
-
reverse reaction with L-alanine, pH 9.0, 30°C
12.1
-
mutant E52Q
19.7
-
mutant V51D
0.25
-
mutant V51E
2.9
-
mutant V51S
18.5
-
wild-type enzyme
18.9
-
pH 7.5, 25°C, recombinant enzyme
3.6
-

KM Value (288 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
-
0.38
-
pH 6.5, 25°C
18.9
-
mutant T335A, cosubstrate NADH, pH 6.2, 25°C
15.195
-
mutant T335A, cosubstrate NADPH, pH 6.2, 25°C
16.589
-
mutant T335D, cosubstrate NADH, pH 6.2, 25°C
9.727
-
mutant T335D, cosubstrate NADPH, pH 6.2, 25°C
18.011
-
NADH, peroxisomal enzyme type with preference for hydroxypyruvate and NADH as substrates
10
25
NADPH
1.25
-
NADPH, cytosolic enzyme
0.07
0.11
NADPH, cytosolic enzyme type with preference for hydroxypyruvate as substrate
1.1
-
pH 6.5, 50°C
0.73
-
pH 7.0, 30°C, recombinant E141N/Q313E mutant formate dehydrogenase
7.4
-
pH 7.0, 37°C
2.5
-
pH 7.5, 70°C, recombinant enzyme and native enzyme from xylose-grown cell extract
5
-
pH 7.8, 22°C, recombinant His6-tagged enzyme
0.0045
-
wild-type, cosubstrate NADH, pH 6.2, 25°C
17.366
-
wild-type, cosubstrate NADPH, pH 6.2, 25°C
17.996
-
30°C, pH 5.5, mutant enzyme N97D
72
-
30°C, pH 5.5, wild-type enzyme
5.4
-
pH 7.0, 30°C, recombinant enzyme
pH 8.0, 70°C
46
-
37°C, cofactor: NADH
1
-
37°C, cofactor: NADPH
0.24
-
cofactor NADH
1.1
-
cofactor NADPH
isoenzyme 1
13
-
isoform GLYR1, at pH 6.5 and 25°C
0.0532
-
isoform GLYR1, at pH 7.5 and 25°C
0.0141
-
isoform GLYR1, at pH 7.8 and 25°C
0.0232
-
isoform GLYR2, at pH 7.1 and 25°C
0.0191
-
isoform GLYR2, at pH 7.3 and 25°C
0.0239
-
isoform GLYR2, at pH 7.8 and 25°C
0.0193
-
isoform GR1, with NADH as cosubstrate, at pH 7.4 and 30°C
0.2677
-
isoform GR1, with NADPH as cosubstrate, at pH 7.4 and 30°C
0.0304
-
isoform GR2, with NADH as cosubstrate, at pH 7.4 and 30°C
0.1446
-
isoform GR2, with NADPH as cosubstrate, at pH 7.4 and 30°C
0.0721
-
pH 6.7, 45°C, cofactor NADH, purified recombinant enzyme
1.2
-
pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme
0.5
-
pH 7.5, 37°C, recombinant enzyme, with NADH
1
-
pH 7.5, 37°C, recombinant enzyme, with NADPH
0.24
-
pH 7.5, 50°C, recombinant enzyme, with NADPH
4.1
-
pH 7.8, temperature not specified in the publication, recombinant truncated enzyme
0.016
-
pH 7.8, temperature not specified in the publication, value determined with the use of a double beam spectrophotometer
0.0045
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
3
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
12.4
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E
0.033
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R
0.061
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
0.088
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
0.181
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
4.6
-
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
0.018
-
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C
0.034
-
recombinant protein from Escherichia coli
0.0045
-
with as NADH as cofactor, pH 6.7, 45°C
1.2
-
with as NADPH as cofactor, pH 6.7, 45°C
0.5
-
with as NADPH as cofactor, pH 7.6, 30°C
0.034
-
with NADH as cosubstrate, at pH 4.0 and 45°C
0.58
-
with NADPH as cosubstrate, at pH 4.0 and 45°C
0.38
-
cosubstrate NADH, pH 7, 30°C
22
-
cosubstrate NADH, pH 7, 37°C
cosubstrate NADPH, pH 7, 30°C
18
-
cosubstrate NADPH, pH 7, 37°C
11
-
K0.5 value, Hill coefficient 1.48, pH 7.5, 25°C
80
-
K0.5 value, Hill coefficient 1.83, pH 7.5, 25°C
12.3
-
cofactor NADH
3.3
-
cofactor NADPH
8
-
cosubstrate: 2,4-dinitrophenyl hydrazone
1.78
-
cosubstrate: O2
1.41
-
mutant E141N, 30°C, pH 7.0
4.6
-
mutant E141Q, 30°C, pH 7.0
2.6
-
wild-type, 30°C, pH 7.0
7.5
-
isoform A
1
-
aerobic aerated bacilli - AB
4.3
-
anaerobic resting bacilli - RB
5.4
-
pH 8.5, 22°C, recombinant enzyme
5.5
-
L-Met and NADH as cosubstrate
8.8
-
pH 8.0, 22°C
3
-
at pH 7.0
6.4
-
at pH 6.5 and 37°C
3.2
-
L104V mutant
2.898
-
L81A mutant
10.6
-
L81V mutant
7.225
-
wild type LiCMS
1.47
-
wild-type
1.47
-
Y144L mutant
3.498
-
Y144V mutant
1.023
-