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
-
adenosylcobalamin
-
adenosylcobalamin-dependent
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cobiialamin
-
5'-deoxyadenosine
-
homolysis
-
cobamide
-
corrin
-
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
-
eseem
- 4.3.1.7
-
b12-dependent
- adenosylcobalamin
-
adenosylcobalamin-dependent
-
cobiialamin
- 5'-deoxyadenosine
-
homolysis
- cobamide
-
corrin
-
5\'-deoxyadenosyl
-
adocbl
-
adocbl-dependent
-
cobalt-carbon
- aminoethanol
-
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
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Metals Ions
Metals Ions on EC 4.3.1.7 - ethanolamine ammonia-lyase
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Co2+
K+
Co2+
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cobalt-carbon bond cleavage depends obligatorily on substrate binding in all adenosylcobalamin-dependent enzymes, with the exception of ribonucleotide triphosphate reductase, which can cleave the bond upon binding a nucleotide triphosphate activator
Co2+
-
included in the cofactor, essential for enzyme binding
Co2+
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substrate binding is required for cobalt-carbon bond cleavage in the native system.