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
-
b12-dependent
- adenosylcobalamin
-
adenosylcobalamin-dependent
-
cobiialamin
- 5'-deoxyadenosine
-
homolysis
- cobamide
-
corrin
-
5\'-deoxyadenosyl
-
adocbl
-
adocbl-dependent
-
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
results (
results (Subunits
Subunits on EC 4.3.1.7 - ethanolamine ammonia-lyase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dodecamer
hexamer
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functional protein is a hexamer of alpha-beta-dimers (alpha-subunit of 50000 Da and beta-subunit of 31000 Da)
oligomer
trimer
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determination by gel filtration, freshly prepared protein oligomerizes readily into trimers in the presence or absence of 5 mM beta-mercaptoethanol, monomer consists of 219-amino-acids
dodecamer
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6 * 35200 + 6 * 56900, the small subunit seems to be responsible for cobalamin binding, SDS-PAGE
dodecamer
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alpha6beta6, 6 * 35000 + 6 * 50000, SDS-PAGE
oligomer
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x * 36000 + x * 51000, the 2 subunits are probably present in equimolar proportions, SDS-PAGE
oligomer
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8-10 * 57000, equilibrium sedimentation after treatment with guanidinium hydrochloride
oligomer
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Two subunits are present in a EutB6EutC6 stoichiometry, EAL is composed of a 453-residue EutB protein subunit and a 286-residue EutC protein subunit, which are coded by the eutb and eutc genes. The positive charge at the terminus of the R160 side chain of EutB is required to achieve the native EutB protein fold and the oligomeric structure of EAL
oligomer
EutB and EutC monomers form the EutB-EutC heterodimer. Two heterodimers form a (EutB-EutC)2 homodimer, and three (EutB-EutC)2 homodimers form the biologically active oligomer. The model predicts that (EutB2)3 oligomer assembly occurs from isolated EutB, and that this hexameric structure templates the formation of the complete, native [(EutB-EutC)2]3 oligomer
