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.
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 |
|