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Literature summary for 4.3.1.7 extracted from

  • Wang, M.; Warncke, K.
    Kinetic and thermodynamic characterization of Co(II)-substrate radical pair formation in coenzyme B12-dependent ethanolamine ammonia-lyase in a cryosolvent system by using time-resolved, full-spectrum continuous-wave electron paramagnetic resonance spectr (2008), J. Am. Chem. Soc., 130, 4846-4858.
    View publication on PubMed
Search for more literature for 4.3.1.7

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli overexpression strain incorporating the cloned Salmonella typhimurium EAL coding sequences Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
ethylene glycol inactivates the EAL holoenzyme Homo sapiens
methanol inactivates the EAL holoenzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.17
-
 (S)-2-aminopropanol binding to apo-EAL at 25°C in buffered aqueous solution Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ included in cofactor B12 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-2-aminopropanol building of a enzyme-coenzyme-substrate ternary complex, the steps are: radical pair separation, first hydrogen atom transfer, radical rearrangement, second hydrogen atom transfer, radical pair recombination, and product release/substrate binding Homo sapiens propanal + NH3
-
 r

Synonyms

Synonyms Comment Organism
EAL
-
 Homo sapiens
ethanolamine ammonia-lyase
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information Comparison of the rates of steady-state turnover of coenzyme B12-dependent enzymes (kcat 10-100 1/s at 25°C) with the rate of cleavage of the cobalt-carbon bond of coenzyme B12 in solution reveals that the enzyme increases the cleavage rate more than 100000000000fold Homo sapiens

pH Range

pH Minimum pH Maximum Comment Organism
6.6 8.2 broad pH-optimum Homo sapiens

Cofactor

Cofactor Comment Organism Structure
coenzyme B12 adenosylcobalamin Homo sapiens