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Literature summary for 4.3.1.7 extracted from

  • Warncke, K.; Schmidt, J.C.; Ke, S.
    Identification of a rearranged-substrate, product radical intermediate and the contribution of a product radical trap in vitamin B12 coenzyme-dependent ethanolaminene deaminase catalysis (1999), J. Am. Chem. Soc., 121, 10522-10528.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ 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 Salmonella enterica subsp. enterica serovar Typhimurium

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
500000
-
calculated holoenzyme molecular mass Salmonella enterica subsp. enterica serovar Typhimurium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ethanolamine Salmonella enterica subsp. enterica serovar Typhimurium 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 acetaldehyde + NH3
-
ir
additional information Salmonella enterica subsp. enterica serovar Typhimurium the radical intermediate is a substrate radical ?
-
?

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Salmonella enterica subsp. enterica serovar Typhimurium

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
activity of the purified enzyme with aminoethanol as substrate is 20-30 micromol/min/mg. Salmonella enterica subsp. enterica serovar Typhimurium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ethanolamine 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 Salmonella enterica subsp. enterica serovar Typhimurium acetaldehyde + NH3
-
ir
additional information the radical intermediate is a substrate radical Salmonella enterica subsp. enterica serovar Typhimurium ?
-
?

Synonyms

Synonyms Comment Organism
ethanolamine ammonia-lyase
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Salmonella enterica subsp. enterica serovar Typhimurium
ethanolamine deaminase
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Salmonella enterica subsp. enterica serovar Typhimurium

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
22
-
ethanolamine at 0°C Salmonella enterica subsp. enterica serovar Typhimurium
55
-
ethanolamine at 22 °C Salmonella enterica subsp. enterica serovar Typhimurium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.45
-
assay at Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

Cofactor Comment Organism Structure
adenosylcobalamin vitamine B12 coenzyme Salmonella enterica subsp. enterica serovar Typhimurium