Enzyme

4.3.1.7 - Ethanolamine ammonia-lyase

Alternative Name(s)

There are no alternative names for this Enzyme

Catalytic Activity

hanolamine = acetaldehyde + NH4(+)

Cofactors

Cob(II)alamin.

Reaction Mechanism

There are no Reaction Mechanism for this Enzyme

Reaction Parameters

There are no kinetic parameters information for this Enzyme

Associated Proteins

Protein name	Organism
Ethanolamine ammonia-lyase heavy chain	Escherichia coli (strain K12)
Ethanolamine ammonia-lyase light chain	Escherichia coli (strain K12)
Probable ethanolamine ammonia-lyase heavy chain	Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599)
Ethanolamine ammonia lyase large subunit	Clostridioides difficile
Ethanolamine ammonia lyase heavy chain	Rhodoferax antarcticus ANT.BR

Citations

Native and nonnative reactions in ethanolamine ammonia-lyase are actuated by different dynamics.
Localization and interaction studies of the Salmonella enterica ethanolamine ammonia-lyase (EutBC), its reactivase (EutA), and the EutT corrinoid adenosyltransferase.
Coenzyme B₁₂-dependent eliminases: Diol and glycerol dehydratases and ethanolamine ammonia-lyase.
Structural Insights into the Very Low Activity of the Homocoenzyme B₁₂ Adenosylmethylcobalamin in Coenzyme B₁₂ -Dependent Diol Dehydratase and Ethanolamine Ammonia-Lyase.
Reactivating chaperones for coenzyme B₁₂-dependent diol and glycerol dehydratases and ethanolamine ammonia-lyase.
Resolution and characterization of contributions of select protein and coupled solvent configurational fluctuations to radical rearrangement catalysis in coenzyme B₁₂-dependent ethanolamine ammonia-lyase.
Coupling of ethanolamine ammonia-lyase protein and solvent dynamics characterized by the temperature-dependence of EPR spin probe mobility and dielectric permittivity.
Deuterium Kinetic Isotope Effects Resolve Low-Temperature Substrate Radical Reaction Pathways and Steps in B₁₂-Dependent Ethanolamine Ammonia-Lyase.
Protein Configurational States Guide Radical Rearrangement Catalysis in Ethanolamine Ammonia-Lyase.
Control of Solvent Dynamics around the B₁₂-Dependent Ethanolamine Ammonia-Lyase Enzyme in Frozen Aqueous Solution by Using Dimethyl Sulfoxide Modulation of Mesodomain Volume.
Mesodomain and Protein-Associated Solvent Phases with Temperature-Tunable (200-265 K) Dynamics Surround Ethanolamine Ammonia-Lyase in Globally Polycrystalline Aqueous Solution Containing Dimethyl Sulfoxide.