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Literature summary 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)

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.3.1.7 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.7 500000
-
calculated holoenzyme molecular mass Salmonella enterica subsp. enterica serovar Typhimurium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.1.7 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
4.3.1.7 additional information Salmonella enterica subsp. enterica serovar Typhimurium the radical intermediate is a substrate radical ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.7 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.7
-
Salmonella enterica subsp. enterica serovar Typhimurium

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.1.7 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.7 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
4.3.1.7 additional information the radical intermediate is a substrate radical Salmonella enterica subsp. enterica serovar Typhimurium ?
-
?

Synonyms

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.1.7 22
-
ethanolamine at 0°C Salmonella enterica subsp. enterica serovar Typhimurium
4.3.1.7 55
-
ethanolamine at 22 °C Salmonella enterica subsp. enterica serovar Typhimurium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.1.7 7.45
-
assay at Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

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