Ligand carbon monoxide

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Basic Ligand Information

Molecular Structure
Picture of carbon monoxide (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
CO
carbon monoxide
UGFAIRIUMAVXCW-UHFFFAOYSA-N
Synonyms:
CO

Show all pahtways known for Show all pathways known for carbon monoxide

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (12 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
CO + H2O + ferrocytochrome b-561 = CO2 + H+ + ferricytochrome b-561
show the reaction diagram
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In Vivo Product in Enzyme-catalyzed Reactions (93 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
1H-3-Hydroxy-4-oxoquinaldine + O2 = N-Acetylanthranilate + CO
show the reaction diagram
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1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)propanoate + formate + CO
show the reaction diagram
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1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)propanoate + formate + CO
show the reaction diagram
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acetyl-CoA + corrinoid protein = CoA + CO + methylcorrinoid protein
show the reaction diagram
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Substrate in Enzyme-catalyzed Reactions (67 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Product in Enzyme-catalyzed Reactions (269 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)propanoate + formate + CO
show the reaction diagram
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dichloromethane + NAD(P)H + O2 = CO + Cl- + NAD(P)+ + H2O
show the reaction diagram
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acetyl-SCoA + CO = acetyl-SCoA + CO
show the reaction diagram
tribromoacetic acid + H2O = carbon monoxide + carbon dioxide + HBr
show the reaction diagram
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octadecanal = heptadecane + CO
show the reaction diagram
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Activator in Enzyme-catalyzed Reactions (12 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
35% activation
-
atmosphere of 80% v/v with 20% v/v O2, 40% activation
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substrate lanosterol: required to inhibit 14alpha-methyl demethylase, 14alpha-demethylation of lanosterol. 14alpha-methyl demethylase activity is dominant over 24-reductase activity, and blockade or removal of 14alpha-methyl demethylase activity is absolutely required for the detection of maximal 24-reductase activity when lanosterol substrate is present. 24-reductase activity is activated in time-dependent manner when 14alpha-methyl demethylase is blocked by CO treatment
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stimulation
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two effects: stimulation and inhibition on CoA/acetylCoA exchange
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activates the enzyme in presence of glucose
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Inhibitor in Enzyme-catalyzed Reactions (329 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
potent inhibitor
-
light-dependent inhibition
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40% inhibition
-
0.02 mM, 50% inhibition
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dead end inhibitor, competitive for H2, uncompetetitive versus F0
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0.5 mM, 58% inhibition
-
oxygen consumption by RoxB is inhibited when carbon monoxide is added to an ongoing polyisoprene cleavage reaction
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7.5 mM, 50% inhibition
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inhibitory effect of CO is reversed by illumination
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photoreversible inhibition
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73% inhibition at CO:O2 ratio of 9:1, activity is partially restored by blue light
-
complete inhibition at 30 s bubbling
-
inhibition of dealkylation
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strong inhibition in the dark, effect is partly reversible by illumination
-
inhibition in the dark, effect is partly reversible upon illumination
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concentration dependent competitive inhibition, 77% inhibition at 90%
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the effect of carbon monoxide can be reversed by exposing the enzyme to 450 nanometer light during the incubation period
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an atmosphere of 100% CO completely inhibits enzyme activity in dark. Inhibition by carbon monoxide is partially reversible upon illumination with blue light
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inhibits in a white light-reversible manner in the presence of oxygen
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ratio CO:O2 of 9:1, 70% inhibition in the light, 80% inhibition under red light, 77% inhibition under blue light
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inhibition is reversible by blue and amber light
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blue light reversible inhibition
-
blue light reversible inhibition
-
the inhibition in the presence of 90% (v/v) CO and 10% (v/v) O2 is reversed to some extent by irradiation with blue light (450 nm)
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CO:O2 ratio of 9:1, photoreversible
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inhibition increases with increasing CO concentrations and is almost completely reversed with the aid of a light spurce between 420 and 450 nm
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complete inhibition; complete inhibition of the oxidation reactions
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60% inhibition in the dark, partially reversible by light
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90% inhibition
-
ratio CO:O2 of 9:1 leads to 88-96% inhibition
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ratio CO:O2 of 9:1 leads to 88-96% inhibition
-
blue-light reversible inhibition, an atmosphere of 80% CO plus 20% O2 inhibits (+)-germacrene A hydroxylase by 69%
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reversible by light
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CO:O2 ratio of 9:1, photoreversible
-
partial reverse activity after light exposure
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inhibition by CO and O2 in the ratio 9 to 1 in the dark, can be reversed by illumination with white light
-
complete inhibition
-
in darkness but not in light
-
inhibition can be partly reverted by blue light
-
partially reversible by irradiation with monochromatic light
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inhibits taxadiene hydroxylation in the dark, inhihibition is partially reversed by blue light at 450 nm
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0.0072 mM, 50% inhibition
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noncompetitive vs. amaranth
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20% residual activity
with reduced benzyl viologen as electron donor, reductase 1: irreversible inhibition by light, reductase 2 : reversible inhibition by light
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little blocking effect on the hydrogenase function of component A
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CO elicits hypofibrinolysis by enhancing alpha2-antiplasmin activity and decreasing plasmin activity
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90% inhibition at 0.8 mM
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inhibition of NilCo, reversible by photoactivation, no inhibition of NilFe
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forms stable complexes with Gyc-88E(1-597), inhibits 2.9fold
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49% inhibition
-
CO inhibits acetyl-CoA synthesis quite strongly and in a cooperative manner
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Metals and Ions (11 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
complexed with the enzyme, structure determination, binding kinetics
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slight inhibition
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3D Structure of Enzyme-Ligand-Complex (PDB) (80 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (15 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE

KM Value (19 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0107
-
pH 7.2, 25°C
0.00645
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Ki Value (18 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.01
-
pH 6.0, 40°C, under N2
-999
-
Ki value less than 1 microM
0.000032
-
-
0.006
-
-
0.0035
-
non competitive
5.6
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37°C under anaerobic conditions

References & Links

Links to other databases for carbon monoxide

ChEBI
PubChem
ChEBI
PubChem