Ligand propionate

acts as a cofactor, it has a high Log D at pH 5.0. The increase in the activity of the enzyme with propanoic acid around 10-50Â°C is due to the peroxidation step because high activity in the nonenzymatic oxidative bromination step is maintained at low temperature, which suppresses the decomposition of the active species generated by the reaction between peracid and Br-

764075

1.14.14.18

the enzyme requires only a single propionate interacting with the buried terminus of Lys16 to exhibit full activity, and it tolerates the existence of a propionate at the exposed 8-position

726996

1.3.3.6

increase in propionate concentration lead to increase of enzyme amount

significant activation

increase in propionate concentration lead to increase of enzyme amount

694994

3.1.2.1

hydrolase increases 50-70% by 250 mM propionate

if a carboxylic acid, such as acetate, is omitted from the reaction using the pure enzyme, no enzyme activity is found. As soon as an carboxylic acid is added, the decarboxylation starts immediately. The enzyme activity is increased with the number of carbon atoms, rising from formate to butyrate. Above four carbon atoms, the activity decreases. Pimelate, butyrate and propionate are the strongest activators

activates

strong activation of mutant K202A

651110

Inhibitor in Enzyme-catalyzed Reactions (61 results)

5 mM, pH 8.5, 25Â°C, 9% inhibition

competitive

92 mM, pH 8, very slight inhibition

390024

1.14.13.230

10 mM, 41% residual activity. Incubation of alkane-grown cells with butanoate or propanoate leads to irreversible time- and O2-dependent loss of butane monooxygenase activity. Propanoate-dependent inactivation involves interaction with the catalytic site. Butane monooxygenase is protected from propanoate-dependent inactivation by the presence of its natural substrate, butane

739008

1.14.15.3

0.01 mM, strong inhibition

about 50% inhibition at 20 mM

765024

2.1.1.157

10% inhibition at 250 mM, with dimethylglycine

slight inhibition

competitive inhibition versus oxaloacetate, mixed type inhibition versus acetyl-CoA; substrate acetyl-CoA, competitive; substrate oxaloacetate, competitive

inhibits alanine transamination and lysine transamination

80% inhibition at 11 mM

80% residual activity at 0.5 mM

competitive inhibition

209476, 32148

3.6.1.15

39% relative activity at a concentration of 0.5 mM, 63% relative activity at a concentration of 0.05 mM

696153

3oyp, 3D-view

3.6.1.5

61% inhibition at 0.5 mM

696153

4.2.1.84

competitive inhibitor; competitive inhibitor

at 50 mM and above

butyryl-CoA formation

557

6.2.1.17

inhibits acetate activation and butyrate activation

inhibition of wild-type enzyme

651110

3D Structure of Enzyme-Ligand-Complex (PDB) (77 results)

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (34 results)

108

pH 7.5, 25Â°C

737742

2.7.2.18

172

at pH 5.7 and 37Â°C

14.2

pH 7.0, 25Â°C

190

at pH 7.3 and 37Â°C

5.6

pH 8.5, 45Â°C

190

pH 7.3, 37Â°C, propionyl-CoA-forming direction, with propionate

744820

K_M Value (72 results)

14.3

pH 7.5, 30Â°C

cosubstrate glutaconyl-CoA

3.2

pH 7.5, 25Â°C

628

3850

pH 7.0, 25Â°C

pH 8.5, 30Â°C, recombinant enzyme

690837

6.2.1.36

0.12

pH 8.5, 45Â°C

pH 7.3, 37Â°C, propionyl-CoA-forming direction, with propionate

744820

K_i Value (17 results)

250

pH 6.5, 30Â°C

0.003

9.9

pH 7.6, 25Â°C, recombinant wild-type enzyme

648457

5.1.1.1

2 entries

IC₅₀ Value (5 results)

at pH 8.0 and 30Â°C

0.025

IC50: 0.025 mM

657030

References & Links

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Show Reference (240 entries)

Links to other databases for propionate

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Ligand propionate

Basic Ligand Information

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (8 results)

In Vivo Product in Enzyme-catalyzed Reactions (16 results)

Substrate in Enzyme-catalyzed Reactions (55 results)

Product in Enzyme-catalyzed Reactions (271 results)

Activator in Enzyme-catalyzed Reactions (19 results)

Inhibitor in Enzyme-catalyzed Reactions (61 results)

3D Structure of Enzyme-Ligand-Complex (PDB) (77 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (34 results)

KM Value (72 results)

Ki Value (17 results)

IC50 Value (5 results)

References & Links

Literature References (240)

Links to other databases for propionate

k_cat Value (Turnover Number) (34 results)

K_M Value (72 results)

K_i Value (17 results)

IC₅₀ Value (5 results)