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
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adenosylcobalamin-dependent
-
cobiialamin
- 5'-deoxyadenosine
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homolysis
- cobamide
-
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
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2h-labeled
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carbon-cobalt
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cryotrapped
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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 (Substrates Products
Substrates Products on EC 4.3.1.7 - ethanolamine ammonia-lyase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S)-2-aminopropanol
propionaldehyde + ?
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deamination with retention of configuration
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?
(R)-2-aminopropanol
propanal + NH3
-
-
-
-
?
(S)-1-amino-2-propanol
propanal + NH3
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inactive substrate analogue, which binds to the substrate binding site in EAL but does not form the cob(II)alamin-substrate radical pair state
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-
?
acetaldehyde + NH3
ethanolamine
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by selectively deuterating the substrate (ethanolamine) and/or the beta-carbon of the 5'-deoxyadenosyl moiety of the intrinsiccoenzyme B12, it is possible to experimentally probe both the forward and reverse hydrogen atom transfers between the 5'-deoxyadenosyl radical and substrate during single turnover stopped-flow measurements
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-
r
ethanolamine
?
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first enzyme in ethanolamine degradation
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-
?
(S)-2-aminopropanol
propanal + NH3
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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
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-
r
(S)-2-aminopropanol
propanal + NH3
-
-
-
-
?
ethanolamine
acetaldehyde + NH3
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Escherichia coli has evolved specialized organelles (microcompartments) for the degradation of small molecular compounds such as ethanolamine and propanediol
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-
?
ethanolamine
acetaldehyde + NH3
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assay at pH 8.0, 37°C, reaction terminated by adding potassium citrate buffer
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-
?
ethanolamine
acetaldehyde + NH3
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ethanolamine ammonia-lyase and coenzyme B12 are necessary and sufficient to grow on ethanolamine
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-
?
ethanolamine
acetaldehyde + NH3
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by selectively deuterating the substrate (ethanolamine) and/or the beta-carbon of the 5'-deoxyadenosyl moiety of the intrinsic coenzyme B12, it is possible to experimentally probe both the forward and reverse hydrogen atom transfers between the 5'-deoxyadenosyl radical and substrate during single turnover stopped-flow measurements
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-
r
ethanolamine
acetaldehyde + NH3
-
-
-
?
ethanolamine
acetaldehyde + NH3
-
-
-
?
ethanolamine
acetaldehyde + NH3
-
-
-
?
ethanolamine
acetaldehyde + NH3
-
-
-
?
ethanolamine
acetaldehyde + NH3
-
-
-
-
?
ethanolamine
acetaldehyde + NH3
-
-
-
?
ethanolamine
acetaldehyde + NH3
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insights into the molecular mechanism of the radical rearrangement and radical migration reactions in ethanolamine deaminase
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-
?
ethanolamine
acetaldehyde + NH3
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elimination of ammonia from the vicinal position of short chain amino alcohol to give the corresponding oxo product
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-
?
ethanolamine
acetaldehyde + NH3
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The family of vitamin B12 coenzyme-dependent enzymes catalyzes the radical-mediated cleavage of unactivated C-H bonds and associated 1,2-cross-migrations of hydrogen and alkyl, carbonyl, hydroxyl, or amino groups
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-
ir
ethanolamine
acetaldehyde + NH3
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two dynamical regimes of the substrate radical rearrangement reaction in B12-dependent ethanolamine ammonia-lyase resolve contributions of native protein configurations and collective configurational fluctuations to catalysis
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-
?
additional information
?
-
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ethanolamine ammonia-lyase microcompartment is composed of five different shell proteins that have been proposed to assemble into symmetrically shaped polyhedral particles of varying sizes
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-
?
additional information
?
-
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the radical intermediate is a substrate radical
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-
?
