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BRENDA support

Ligand L-cysteine

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Basic Ligand Information

Molecular Structure
Picture of L-cysteine (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Molfile
C3H7NO2S
L-cysteine
XUJNEKJLAYXESH-REOHCLBHSA-N
 Download
Synonyms:
(R)-cysteine, beta-mercaptoalanine, Cys, cystein, cysteine, L-Cys, L-cystein

Related pathways

Pathway Source
Pathways
BRENDA
alanine metabolism, coenzyme A metabolism, coenzyme M biosynthesis, cysteine metabolism, glutathione metabolism more
KEGG
Aminoacyl-tRNA biosynthesis, Biosynthesis of amino acids, Biosynthesis of cofactors, Biosynthesis of plant secondary metabolites, Biosynthesis of secondary metabolites more
MetaCyc
anguibactin biosynthesis, apratoxin A biosynthesis, arachidonate metabolites biosynthesis, bacillithiol biosynthesis, bis(guanylyl molybdopterin) cofactor sulfurylation more


Show all pahtways known for Show all BRENDA pathways known for L-cysteine

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (57 results)

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EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
hercynine + L-cysteine + O2 = S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
-
L-Cys + H2O + O2 = 2-oxo-3-mercaptopropanoic acid + NH3 + H2O2
show the reaction diagram
-
L-cysteine + 2-oxoglutarate = L-glutamate + beta-mercaptopyruvate
show the reaction diagram
-
L-cysteine + activated tRNA = L-serine + tRNA containing a thionucleotide
show the reaction diagram
-
ATP + L-cysteine + tRNAPro = AMP + diphosphate + L-cysteinyl-tRNAPro
show the reaction diagram
-
ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys
show the reaction diagram
-
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + L-cysteine + ATP = 1-O-[2-(L-cysteinamido)-2-deoxy-alpha-D-glucopyranosyl]-1D-myo-inositol + AMP + diphosphate
show the reaction diagram
-
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O = 3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
show the reaction diagram
-

In Vivo Product in Enzyme-catalyzed Reactions (28 results)

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EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
4beta-(S-cysteinyl)-epicatechin + NADPH + H+ = epicatechin + cysteine + NADP+
show the reaction diagram
-
-
L-cystine + NADH + H+ = 2 L-cysteine + NAD+
show the reaction diagram
-
-
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O = (2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
-
-
cystine + GSH = cysteine + GSSG
show the reaction diagram
-
-
O-acetyl-L-serine + sulfide = L-cysteine + acetate
show the reaction diagram
-
-
O-acetyl-L-serine + S2- = L-cysteine + acetic acid
show the reaction diagram
-
-
Cys-Gly + H2O = Cys + Gly
show the reaction diagram
-
-
N-acetyl-L-cysteine + H2O = acetate + L-cysteine
show the reaction diagram
-
-
N-carbamoyl-L-cysteine + H2O = L-cysteine + CO2 + NH3
show the reaction diagram
-
-
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine = CTP + (R)-4'-phosphopantothenate + L-cysteine
show the reaction diagram
-
-

Substrate in Enzyme-catalyzed Reactions (333 results)

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EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
cysteine + H2O2 = ? + H2O
show the reaction diagram
-
L-cysteine + H2O2 = cystine + 2 H2O
show the reaction diagram
-
L-cysteine + O2 = 3-sulfinoalanine
show the reaction diagram
-
L-cysteine + 2-oxoglutarate + O2 = ?
show the reaction diagram
-
p-hydroxyphenylacetaldoxime + [reduced NADPH-hemoprotein reductase] + cysteine + O2 = S-(benzohydroximoyl)-L-cysteine + [oxidized NADPH-hemoprotein reductase] + 2 H2O
show the reaction diagram
-
starch + cysteine + O2 = malto-oligosaccharide aldonic acid + cystine + H2O
show the reaction diagram
-
tamarind xyloglucan + 2 cysteine + O2 = ? + cystine + H2O
show the reaction diagram
-
L-cysteine + H2O + NAD+ = 3-mercapto-2-oxopropanoate + NH3 + NADH
show the reaction diagram
-
L-cysteine + H2O + NAD+ = 3-mercapto-2-oxopropanoate + NH3 + NADH
show the reaction diagram
-
L-cysteine + H2O + 2 cytochrome b = 2-oxo-3-thiopropanoate + NH3 + 2 reduced cytochrome b
show the reaction diagram
-
L-Cys + pyruvate + NADH = ?
show the reaction diagram
-
L-Cys + pyruvate + NADH = N-[1-(R)-(Carboxy)ethyl]-(S)-Cys + NAD+
show the reaction diagram
-
L-cysteine + NADPH = L-cystine + NADP+
show the reaction diagram
-
cysteine + homocystine = cystine + 2 homocysteine
show the reaction diagram
-
L-cysteine + protein disulfide = cystine + protein-dithiol
show the reaction diagram
-
L-Cys + dehydroascorbate = ? + ascorbate
show the reaction diagram
-
sulfide + cysteine + coenzyme Q1 = cysteine persulfide + reduced coenzyme Q1
show the reaction diagram
-
L-cysteine + 2-(glutathione-S-yl)-trichloro-p-hydroquinone = glutathionyl cysteinyl disulfide + trichloro-p-hydroquinone
show the reaction diagram
-
hydrogen sulfide + cysteine + coenzyme Q1 = ?
show the reaction diagram
-
L-arginine + L-cysteine = N-amidino-L-cysteine + L-ornithine
show the reaction diagram
-
L-cysteine + KCN = ?
show the reaction diagram
-
L-cysteine + dithiothreitol = S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + sulfide
show the reaction diagram
-
L-cysteine + 2-oxoglutarate = 3-mercaptopyruvate + L-glutamate
show the reaction diagram
-
2-oxosuccinamic acid + L-cysteine = L-asparagine + 3-mercapto-2-oxopropanoate
show the reaction diagram
-
L-cysteine + 2-oxoglutarate = L-glutamate + beta-mercaptopyruvate
show the reaction diagram
-
L-cysteine + pyruvate = 3-mercapto-2-oxopropanoate + L-alanine
show the reaction diagram
-
L-cysteine + 2-oxoglutarate = 3-mercapto-2-oxopropanoate + L-glutamate
show the reaction diagram
-
cysteine + pyruvate = 3-mercapto-2-oxo-propanoate + L-alanine
show the reaction diagram
-
cysteine + pyruvate = ?
show the reaction diagram
-
L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate
show the reaction diagram
-
L-cysteine + glutathione = ?
show the reaction diagram
-
L-cysteine = L-alanine + sulfide
show the reaction diagram
-
3'-phosphoadenylylsulfate + cysteine = adenosine 3',5'-bisphosphate + 2-amino-3-sulfosulfanyl-propionic acid
show the reaction diagram
-
cysteine + adenosine = AdoCys
show the reaction diagram
-
10-undecenoic acid + L-cysteine = 10-undecenoyl-L-cysteine + H2O
show the reaction diagram
-
L-Cys = ?
show the reaction diagram
-
2-Oxobutanoate + L-Cys = ?
show the reaction diagram
-
L-cysteine = ?
show the reaction diagram
-
L-cysteine = ?
show the reaction diagram
-
L-cysteine = ?
show the reaction diagram
-
L-Cys = ?
show the reaction diagram
-
L-cysteine + reduced acceptor = ?
show the reaction diagram
-
L-cysteine + H2O = 2-oxopropanoate + NH3 + ?
show the reaction diagram
-
scrambled RNAse + cysteine = ?
show the reaction diagram
-
ATP + L-cysteine + tRNASer = AMP + diphosphate + L-cysteinyl-tRNASer
show the reaction diagram
-
Ile-tRNAIle + cysteine = tRNAIle + isoleucylcysteine
show the reaction diagram
-
ATP + L-cysteine + tRNALys = AMP + L-cysteinyl-tRNALys + diphosphate
show the reaction diagram
-
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + L-cysteine + ATP = 1-O-[2-(L-cysteinamido)-2-deoxy-alpha-D-glucopyranosyl]-1D-myo-inositol + AMP + diphosphate
show the reaction diagram
-
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
show the reaction diagram
-
ATP + gamma-L-glutamyl-L-cysteine + L-Cys = ?
show the reaction diagram
-
ATP + UDP-N-acetylmuramate + L-Cys = ADP + phosphate + UDP-N-acetylmuramoyl-L-Cys
show the reaction diagram
-
ATP + L-asparagine + L-cysteine = ADP + phosphate + L-asparaginyl-L-cysteine
show the reaction diagram
-
ATP + H2O + L-cysteine/out = ADP + phosphate + L-cysteine/in
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (116 results)

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EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
S-sulfanyl-L-cysteine + O2 = L-cysteine + sulfite
show the reaction diagram
-
-
4beta-(S-cysteinyl)-epicatechin + NADPH + H+ = epicatechin + cysteine + NADP+
show the reaction diagram
-
-
cystine + NADPH + H+ = 2 cysteine + NADP+
show the reaction diagram
-
-
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O = (2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
-
-
cysteine-glutathione + GSH = cysteine + GSSG
show the reaction diagram
-
-
cystine + glutathione = cysteine + glutathione disulfide
show the reaction diagram
-
-
gamma-Glu-Cys + Gly-Gly = Cys + 5-L-glutamyl-Gly-Gly
show the reaction diagram
-
-
O-acetyl-L-serine + sulfide = L-cysteine + acetate
show the reaction diagram
-
-
L-glutamine + 3-mercaptopyruvate = 2-oxoglutaramate + L-cysteine
show the reaction diagram
-
L-kynurenine + mercaptopyruvate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-cysteine
show the reaction diagram
-
-
L-cysteine methyl ester + H2O = L-cysteine + methanol
show the reaction diagram
-
Gly-L-Cys + H2O = Gly + L-Cys
show the reaction diagram
-
-
2-aminobenzoyl-Phe-Arg-Cys + H2O = 2-aminobenzoyl-Phe-Arg + Cys
show the reaction diagram
-
-
ubiquitin-Cys + H2O = ubiquitin + Cys
show the reaction diagram
-
N-acetylcysteine + H2O = acetate + cysteine
show the reaction diagram
-
-
Nalpha-acetyl-L-cysteine + H2O = L-cysteine + acetate
show the reaction diagram
-
-
N-acetyl-L-cysteine + H2O = acetic acid + L-cysteine
show the reaction diagram
-
Nalpha-benzyloxycarbonyl-L-Cys + H2O = benzyl alcohol + CO2 + L-Cys
show the reaction diagram
-
N-carbamoyl-L-cysteine + H2O = L-cysteine + CO2 + NH3
show the reaction diagram
-
-
O-Acetyl-L-serine + H2S = Cysteine + acetate
show the reaction diagram
-
L-cystine = pyruvate + NH4+ + S2- + L-cysteine
show the reaction diagram
-
-
AMP + diphosphate + L-cysteinyl-tRNACys = ATP + L-cysteine + tRNACys
show the reaction diagram
-
-
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine = CTP + (R)-4'-phosphopantothenate + L-cysteine
show the reaction diagram
-
-
ATP + H2O + L-cysteine/out = ADP + phosphate + L-cysteine/in
show the reaction diagram
-
-

Activator in Enzyme-catalyzed Reactions (335 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
fructose reduction at pH 7.4, inhibits at pH 9.0
-
5fold activation at 1.3 mM
-
restoring, also other sulfhydryl compounds, NADH-linked to a greater extent than the NADPH-linked activity
-
cysteine or glutathione required
-
activates
-
1 mM, increases activity by 29%
-
in mM-concentration, no activation of the reverse reaction
-
10 mM, activates
-
L-cysteine is associated with the highest boost in the rate of cyanide formation in the LPO/H2O2/acetonitrile system, achieving 156.7% of the rate of cyanide production of the control
-
cysteine increases activity at low glutathione concentrations
-
addition of L-cysteine significantly enhances the rate of chloroacetonitrile oxidation and cyanide release by the myeloperoxidase/H2O2/Cl- system (45.4% increase at 5 mM)
-
increase of activity
-
stimulated by 2 mM
-
activates
-
can reduce the inactive ferric form of the enzyme to the active ferrous form
-
enzyme has a specific requirement for L-cysteine (6.7 mM), required to restore full activity after dialysis or treatment with chelating agents
-
activation
-
can replace ascorbate
-
1 mM
-
0.1 mM, slight stimulation, inhibition at 1 mM
-
stimulates
-
in absence of thiols or ascorbate, no NO generation is detected from xanthine oxidase mediated organic nitrate reduction
-
activates, 2-oxoglutarate dehydrogenase complex
-
10 mM, 2.8fold activation of the oxidation of D-glyceraldehyde 3-phosphate
-
required for maximal activity
-
activation
-
activates
-
10 mM, activates
-
activates
-
activates, optimal concentration: 1 mM
-
reversibly activates GAPOR purified from M9/Mo+ cultures
-
activates
-
activation
-
recombinant enzyme FlaR (rFlaR) FAD-dependent NADP-reductase is activated in the presence of cysteine, cysteine significantly stimulates rFlaR NADP+-reductase activity
-
stimulates
-
5 mM, 5.6fold stimulation
-
enhances activity, can replace NADH
-
2 mM required for maximal activity
-
enzyme activity is strongly enhanced in presence of 5 mM L-cysteine
-
NADH-oxidation with free lipoic acid is strongly dependent on the addition of NAD+, EDTA, Mg2+ and cysteine, the reverse reaction with reduced lipoic acid and NAD+ does not show any requirement for cofactors
-
redox active disulfide at the catalytic site
-
fungus is not able to use L-Cys as sulfur source instead of sulfate. Presence of L-Cys induces production of an excessive amount of both intracellular and extracellular enzyme
-
enhances activity, optimal concentration 10 mM
-
stimulation at low concentration
-
slight activatory effect
-
relative activity 103%
-
activation, 10 mM
-
activation
-
2fold activation
-
dependent on
-
activates at 0.01 M
-
stimulates the activity via conformational changes that occur upon binding to the amino acid-binding-domain
-
reducing reagent is required for maximal activity
-
stimulation
-
detergent required for maximal activity
-
10 mM, slight activation
-
activates
-
activation, together with SDS or guanidine hydrochloride
-
complete reactivation at 3.3 mM but inhibition at 33 mM
-
at 1.25 mM, 3fold stimulation, at 10 mM, 70% inhibition
-
activation
-
omission of cysteine decreases the reaction rate by 40%
-
slight activation
-
activates
-
activation, can replace dithiothreitol
-
5 mM, 2-4fold stimulation
-
stimulates
-
activates
-
activation
-
slight activation, at high concentration
-
essential for optimal activity
-
1 mM, 117% of initial activity
-
intraperitoneal administration of 7 mg/kg/day for 14 days, increase in enzyme activity by 185% and increase of total antioxidant status. L-cysteine given before a toxic dose of cadmium results in increase of enzyme activity up to 85%, a total antioxidant status similar to the control values, and survival of the treated animals
-
stimulation
-
protects the enzyme against traces of heavy metals
-
activation
-
activates
-
stimulates
-
reverses glyoxylate inhibition
-
dependent
-
1 mM
-
stimulation
-
5 mM, 202% of initial activity
-
maximal activation at 0.6 mM, 15% of the activation with 2-mercaptoethanol
-
105% activity at 1 mM
-
1 mM, 132% of initial activity
-
0.01 M, 1.05fold activation
-
0.01 M, 1.05fold activation
-
slight stimulation at 1 or 10 mM
-
1-10 mM, activates
-
60% activation
-
30% stimulation
-
10 mM, 150.34% of initial activity
-
activation to 152.2% at 5 mM
-
slight activation
-
1 mM, 18% stimulation
-
10 fold activation
-
weak activation
-
activates
-
increases activity
-
activation, 4 mM
-
inactive unless treated with
-
5-10 mM activate refolded protein
-
activation
-
activates
-
the enzyme is completely dependent on preactivation with cysteine
-
2 milliM, pH 5.0, 48 h, 37°C, enzymatic activity depends on reducing agents
-
20 mM used in assay conditions
-
stimulates
-
128.15% activity at 100 mM
-
1 mM, activation 33%
-
slight activation
-
slight stimulation
-
effect of cysteine on arginase activity, effect of increasing concentrations of cysteine alone or in combination with iron (II) sulfate on the enhancement of arginase activity in human sickle erythrocytes or purified arginase-1 from Bos taurus liver
-
induction
-
in a concentration range of 0.02 mM to 1000 mM
-
activation
-
enzyme activity increases 2-4fold in presence of both Fe2+ and cysteine. 0.1-1 mM Fe2+ and 0.05-0.5 mM cysteine
-
required. The optimal concentration of L-Cys is 0.5-2.0 mM
-
sulfhydryl compound is required for maximal activity
-
increases activity
-
activation
-
low concentration of cellular cysteine leads to elevation of cystathionine gamma-lyase
-
optimum activity at 6 mM L-cysteine
-
slight stimulation
-
enzyme activity depends on the presence of a reducing compound to a final concentration of 0.1mM
-
metal chelator required
-
required for in vitro activity
-
stimulates 2fold
-
stimulates
-
stimulates
-
activates the enzyme and mutant lacking 100 residues
-
200% increase of Cd2+ transport across plasma membranes at 50 mM. Cd transport across tonoplasts is stimulated up to 120% by 50 mM L-cysteine
-
slight activation
-

Inhibitor in Enzyme-catalyzed Reactions (506 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
competitive
-
the addition of cysteine (more than 2 mM) inactivates human L-xylulose reductase and is accompanied by a 10fold decrease in catalytic efficiency, the activity of the cysteine-inactivated enzyme is not recovered by the addition of 10 mM dithiothreitol and 2-mercaptoethanol
-
82% inhibition at 20 mM
-
0.5 mM, complete inhibition
-
40% inhibition at 10 mM
-
1mM, 18.5% residual activity
-
47% inhibition of oxidation and 11% inhibition of reduction at 10 mM
-
complete inhibition at 10 mM
-
competitive against L-serine, noncompetitive against NADP+
-
1 mM, together with 2-mercaptoethanl, up to 50% inhibition
-
53.3% inhibition at 1 mM
-
slight
-
isoenzyme 1, 1 mM, 29% inhibition
-
at 294 mM
-
2 mM, 12% residual activity
-
70% residual activity at 0.5 mM
-
28-38% inhibition of glycolate oxidation at 1 mM
-
20% inhibition at 0.5 mM
-
12.2% inhibition at 0.1 mM
-
33.9% inhibition at 0.02 mM, complete inhibition at 0.1 mM
-
35% inhibition at 3.3 mM
-
complete inhibition at 0.05 mM, reversible by increasing I- concentration
-
GPx-1 is inhibited by 0.5 mM cysteine
-
concentrations of cysteine of 2 mM and above are inhibitory in assays of purified cysteine dioxygenase
-
preincubation with substrate protects against inactivation
-
inhibition not reversed by glutathione
-
marked decrease in enzyme activity
-
2 mM, 42% inhibition
-
pMMO
-
not marked
-
100% inhibition at 0.2 mM
-
51% inhibition at 5 mM cysteine in the growth medium
-
in the reverse reaction
-
59% inhibition at 1 mM
-
60% inhibition at 1 mM
-
2.7 mM, 50% inhibition
-
inhibitory above 7 mM
-
significant inhibitor
-
10 mM, 41% inhibition
-
complete inhibition of both isoforms at 5 mM
-
complete inhibition at 0.1 mM
-
77% inactivation at 10 mM
-
1 mM, 54% inhibition
-
1 mM, 87% residual activity
-
at high concentration
-
1 mM, significant inhibition
-
10% inhibition at 250 mM, with dimethylglycine
-
slight inhibition
-
1.8 mM, 50% inhibition
-
10 mM, 90% inhibition, noncompetitive vs. ornithine
-
50% inhibition at 0.01 mM
-
weak
-
competitive to L-serine
-
85% inhibition
-
5 mM, 50% inhibition
-
1 mM, 86% inhibition
-
competitive, forms a nonproductive external aldimine with the pyridoxal 5'-phosphate cofactor
-
0.5 mM, 14% inhibition
-
10 mM, 35% inhibition
-
10 mM, inhibits activity with isoleucine and tyrosine by 22 and 34%, respectively
-
90% inhibition
-
about 35% inhibition
-
strong
-
docking study with wild-type and mutant enzymes
-
dokcing sturdy with wild-type and mutant enzymes
-
1 mM, 49% inhibition
-
2 mM, slight
-
inhibits reaction with 3-mercaptopyruvate
-
above 0.5 mM
-
38% inhibition at 1 mM
-
inhibits the enzyme activity in presence of TNF-alpha
-
80% inhibition at 25 mM
-
10 mM, 15% inhibition
-
25 mM, 26% inhibition
-
3.3 mM, 15 min at 37°C, 52% inhibition
-
0.001 M, 7% loss of activity
-
0.001 M, 7% loss of activity
-
31% inhibition at 0.02 mM
-
32% inhibition at 10 mM
-
10 mM, 68% residual activity
-
1 mM, 27% inhibition
-
1 mM, 6% inactivation
-
non-competitive, 7.3% residual activity at 5 mM
-
lowers dose-dependently recombinant CN1 efficiency
-
90% inhibition at 1 mM, 40% inhibition at 0.1 mM
-
inhibition of prekallikrein activation
-
weak
-
complete inhibition at 1.25 mM
-
strongly inhibits
-
1 mM, complete inhibition
-
47.4% residual activity at 20 mM
-
5 mM, reduces activity to 52%
-
50 mM: 100% inhibition
-
complete inhibition
-
25 mM, complete inhibition
-
competitive inhibition, 10 mM
-
in presence of p-chloromercuribenzoate, 0.05 mM
-
liver enzyme
-
activity is decreased to 20% of the original by treatment with cysteine plus mercaptoethanol. Most of the loss is regained on incubation with pyridoxal 5'-phosphate
-
65% inhibition at 10 mM
-
23% inhibition at 2.5 mM
-
35% inhibition at 50 mM
-
slight
-
mixed type inhibition
-
almost complete inhibition of isoforms LCDII and LCDIII
-
linear noncompetitive inhibitor
-
competitive
-
39% loss of activity after 90 min, 83% loss of activity after 240 min
-
competitive inhibition of prolylation. A 40fold excess over L-proline concentration reduces the prolylation activity by 80%, no inhibition of mutant P100A
-
-
-
weak
-
5 mM: 15% inhibition
-
weak
-
poor
-
inhibits the Mg2+-ATPase activity by 15%, in addition with lanthanum by 25%
-

Metals and Ions (2 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activates
-
5 mM, 90% residual activity
-

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (221 results)

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EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
3.3
-
pH 8.0, 26°C, with L-histidine
52300
-
pH 7.5, 20°C
0.056
-
pH 5.2, 40°C
94
-
pH 7.4, 25°C
0.37
-
pH 6.5, 30°C
6.6
-
37°C, pH 7.8
0.22
-
pH 7.4
16.89
-
at pH 7.4 and 30°C
0.03
-
for the L-cysteine desulfurase domain, 2 mM DTT, pH 9.3, 37°C
0.11
-
-
0.155
-
pH 7.5, 37°C, recombinant enzyme
2
-
pH 7.4, 30°C, mutant T385D sDAPL
930
-
pH 10.0, 35°C, recombinant His-tagged enzyme
0.00077
-
pH 7.0, 35°C
0.078
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.133
-
under saturating conditions
2.9
-
at pH 7.6 and 37°C
20
-
-

KM Value (428 results)

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EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.35
-
pH 8.0, 26°C, with L-histidine
5.4
-
with pyruvate and NADPH as cosubstrate
28
-
-
2.5
-
pyruvate and NADH as cosubstrates
15.1
-
pH 5.2, 40°C
0.27
-
-
2
3
pH 7.4, 25°C
1.97
-
pH 6.5, 30°C
2
3
at pH 7.4 and 37°C
33
-
-
22.2
-
-
1
-
pH 7.4, Km value of L-cysteine is decreased by 40fold and 200fold in comparison with those of L-alanine and L-serine
12.22
-
at pH 7.4 and 30°C
0.03
-
pH 8, 37°C
0.05
-
for the L-cysteine desulfurase domain, 2 mM DTT, pH 9.3, 37°C
35
-
-
1.32
-
pH 7.5, 37°C, recombinant enzyme
0.284
-
pH 7.4, 30°C, mutant T385D sDAPL
8.3
-
-
4.9
-
pH 7.0, 35°C
29
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
3.8
-
-

Ki Value (72 results)

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EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
6.7
-
non-competitive inhibition
0.3
-
-
0.99
-
-
2
10
-
6.2
-
pH pH 9.0, 37°C
0.32
-
pH 7.4, 38°C
7.9
-
at pH 6.5 and 75°C
0.31
-
-
0.000025
-
recombinant enzyme, at 37°C
0.27
-
pH 7.0, 37°C
0.53
-
-
1.5
-
pH 8.4, 30°C
5.22
-
26°C, pH 9.8
0.766
-
substrate CTP, pH 7.6, 37°C

IC50 Value (42 results)

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EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.027
-
at pH 6.0 and 25°C
2.6
-
pH pH 9.0, 37°C
0.748
-
in Tris-HCl buffer 33 mM pH 8.8, at 37°C
0.47
-
-
0.061
-
recombinant enzyme

References & Links

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Links to other databases for L-cysteine

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EXTERNAL LINKS
ChEBI
PubChem
UniChem