Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.7 0.17
-
 (S)-2-aminopropanol binding to apo-EAL at 25°C in buffered aqueous solution Homo sapiens

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.7 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.7
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.7 (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

EC Number Synonyms Comment Organism
4.3.1.7 EAL
-
 Homo sapiens
4.3.1.7 ethanolamine ammonia-lyase
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.1.7 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

EC Number pH Minimum pH Maximum Comment Organism
4.3.1.7 6.6 8.2 broad pH-optimum Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.7 coenzyme B12 adenosylcobalamin Homo sapiens