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Ligand trichloroacetonitrile

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Substrate (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.5.1

trichloroacetonitrile + 2 H2O = trichloroacetate + NH3

724954

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Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

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EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.5.5.1

0.01

-

pH 7.4, 70°C, wild-type enzyme

724954

3.5.5.1

0.225

-

pH 7.4, 70°C, mutant enzyme K96R

724954

3.5.5.1

2 entries

K_M Value (2 results)

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EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.5.5.1

0.0000000005

-

pH 7.4, 70°C, wild-type enzyme

724954

3.5.5.1

0.00000013

-

pH 7.4, 70°C, mutant enzyme K96R

724954

3.5.5.1

2 entries

References & Links

Literature References (1)

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BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

724954

16156792

The signature amidase from Sulfolobus solfataricus belongs to the CX3C subgroup of enzymes cleaving both amides and nitriles. Ser195 and Cys145 are predicted to be the active site nucleophiles

2005

Cilia, E.; Fabbri, A.; Uriani, M.; Scialdone, G.G., Ammendola, S.

FEBS J.

272

4716-4724

Links to other databases for trichloroacetonitrile

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Show Links (1 entry)

ChEBI

PubChem

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