4.3.1.7: ethanolamine ammonia-lyase
This is an abbreviated version!
For detailed information about ethanolamine ammonia-lyase, go to the full flat file.
Word Map on EC 4.3.1.7
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4.3.1.7
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b12-dependent
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adenosylcobalamin
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adenosylcobalamin-dependent
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cobiialamin
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5'-deoxyadenosine
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homolysis
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cobamide
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corrin
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5\'-deoxyadenosyl
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adocbl
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adocbl-dependent
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cobalt-carbon
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aminoethanol
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x-band
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full-spectrum
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metabolosome
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2h-labeled
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carbon-cobalt
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cryotrapped
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cryosolvent
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2-aminoethanols
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corrinoids
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eseem
- 4.3.1.7
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b12-dependent
- adenosylcobalamin
-
adenosylcobalamin-dependent
-
cobiialamin
- 5'-deoxyadenosine
-
homolysis
- cobamide
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corrin
-
5\'-deoxyadenosyl
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adocbl
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adocbl-dependent
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cobalt-carbon
- aminoethanol
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x-band
-
full-spectrum
-
metabolosome
-
2h-labeled
-
carbon-cobalt
-
cryotrapped
-
cryosolvent
- 2-aminoethanols
- corrinoids
-
eseem
Reaction
Synonyms
AEL, ammonia-lyase, ethanolamine, EAL, ethanolamine ammonia lyase, ethanolamine ammonia-lyase, ethanolamine ammonia-lyase BMC, ethanolamine deaminase, ethanolamine-ammonia lyase, eut-L, EutB, eutBC
ECTree
4.3.1.7 ethanolamine ammonia-lyaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 4.3.1.7 - ethanolamine ammonia-lyase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(S)-1-amino-2-propanol
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inactive substrate analogue
adenosylmethylcobalamin
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0.1% coenzyme activity compared to adenosylcobalamin, holoenzyme with adenosylmethylcobalamin undergoes rapid inactivation
hydroxyethylhydrazine
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the latter suicide inhibitor effects a stoichiometric conversion of enzyme-bound adenosylcobalamin into its cleaved form cob(II)alamin
p-hydroxymercuribenzoate
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0.0001 mM, 50% inhibition; even in the presence of ethanolamine
additional information
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the holoenzyme of adenosylcobalamin-dependent ethanolamine ammonia lyase undergoes suicidal inactivation during catalysis as well as inactivation in the absence of substrate. The inactivation involves the irreversible cleavage of the Co-C bond of the coenzyme. Inactivated holoenzyme undergoes rapid and continuous reactivation in the presence of ATP, Mg2+ and free adensosylcobalamin. EutA is essential for reactivation. Reactivation and activation occur through the exchange of modified coenzyme for free intact adenosylcobalamin
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