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
-
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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Specific Activity
Specific Activity on EC 4.3.1.7 - ethanolamine ammonia-lyase
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additional information
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truncated enzymes, after purificaton, value between 12.45 and 63.1
additional information
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activity of the purified enzyme with aminoethanol as substrate is 20-30 micromol/min/mg.
additional information
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enzyme activity is determined by using the coupled assay with alcohol dehydrogenase/NADH, the specific activity of the purified enzyme with aminoethanol as substrate was 20-30 micromol/min/mg
additional information
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Externally added guanidine hydrochloride leads to significant R160A EAL enzyme activity under Vmax conditions, the activity of R160A EAL increases with guanidine hydrochloride concentration and reaches a maximum at 10 mM, which represents 2.3% of the activity of the wild-type control. The resurrection of enzyme activity in R160A EAL by externally added guanidine hydrochloride provides strong support that a positively charged arginine side chain in the active site is catalytically essential.
additional information
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specific activity is 30-45 micromol ethanolamine/min/mg of EAL at 25°C, determined by the EAL-alcohol dehydrogenase coupled assay
additional information
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specific activity of the purified enzyme with aminoethanol as the substrate is 35-45 micromol/min/mg, determined by using the coupled assay with alcohol dehydrogenase/NADH