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
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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
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2h-labeled
-
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
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KM Value
KM Value on EC 4.3.1.7 - ethanolamine ammonia-lyase
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0.17
(S)-2-aminopropanol
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binding to apo-EAL at 25°C in buffered aqueous solution
0.022
ethanolamine
reconstituted EAL (from EutB and EutC subunits), pH 7.5, 25°C
0.0316
ethanolamine
purified EAL, pH 7.5, 25°C
0.41
ethanolamine
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R160K EAL shows a 30fold increase relative to wild-type enzyme
additional information
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truncated enzymes, value between 0.000041 and 0.000078
additional information
ethanolamine
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truncated enzymes, value between 0.0059 and 0.0076
additional information
additional information
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a dissociation constant for coenzyme B12 binding to EAL of 0.0005 mM is estimated from the Michaelis constant, which indicates that the free cofactor represents 4% of the total cofactor in the sample
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additional information
additional information
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the transient decay reaction kinetics of the 1,1,2,2-2H4-aminoethanol generated CoII-substrate radical pair catalytic intermediate involve sequential passage through the rearrangement step substrate radical to product radical, and the step product radical to diamagnetic product involves hydrogen atom transfer from carbon C5' of the adenosine moiety of the cofactor to the product radical C2 center. The decay kinetics for the 2H-substrate radical over 190-207 K represent two non-interacting populations. The fast observed rate constant kobs represents the rate constant for the radical rearrangement, and this step is the rate determining step in substrate radical decay
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