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Literature summary extracted from

  • Mori, K.; Oiwa, T.; Kawaguchi, S.; Kondo, K.; Takahashi, Y.; Toraya, T.
    Catalytic roles of substrate-binding residues in coenzyme B12-dependent ethanolamine ammonia-lyase (2014), Biochemistry, 53, 2661-2671.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.1.7 expressed in Escherichia coli as a His-tagged fusion protein Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.3.1.7 D362A mutant shows highly decreased kcat compared to wild-type, mutant undergoes quicker inactivation compared to wild-type Escherichia coli
4.3.1.7 D362E mutant shows highly decreased kcat compared to wild-type Escherichia coli
4.3.1.7 D362N mutant shows highly decreased kcat compared to wild-type Escherichia coli
4.3.1.7 E287A mutant shows highly decreased kcat compared to wild-type, mutant undergoes quicker inactivation compared to wild-type Escherichia coli
4.3.1.7 E287D mutant shows highly decreased kcat compared to wild-type Escherichia coli
4.3.1.7 E287H mutant shows highly decreased kcat compared to wild-type Escherichia coli
4.3.1.7 E287Q mutant shows highly decreased kcat compared to wild-type Escherichia coli
4.3.1.7 N193A mutant shows highly decreased kcat compared to wild-type, mutant undergoes quicker inactivation compared to wild-type Escherichia coli
4.3.1.7 N193D mutant shows decreased kcat compared to wild-type but mutant retains partial activity, Km (ethanolamine) increased compared to wild-type Escherichia coli
4.3.1.7 Q162A mutant shows highly decreased kcat compared to wild-type, mutant undergoes quicker inactivation compared to wild-type Escherichia coli
4.3.1.7 Q162E mutant shows decreased kcat compared to wild-type but mutant retains partial activity, Km (ethanolamine) increased compared to wild-type Escherichia coli
4.3.1.7 Q162H mutant shows decreased kcat compared to wild-type but mutant retains partial activity, Km (ethanolamine) increased compared to wild-type Escherichia coli
4.3.1.7 Q162K mutant shows highly decreased kcat compared to wild-type Escherichia coli
4.3.1.7 R160A mutant shows highly decreased kcat compared to wild-type, mutant undergoes quicker inactivation compared to wild-type Escherichia coli
4.3.1.7 R160K mutant shows decreased kcat compared to wild-type but mutant retains partial activity, Km (ethanolamine) increased compared to wild-type Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.7 0.0033
-
ethanolamine run 2, pH 8, 37°C, wild-type Escherichia coli
4.3.1.7 0.21
-
ethanolamine run 2, pH 8, 37°C, mutant N193D Escherichia coli
4.3.1.7 0.21
-
ethanolamine run 2, pH 8, 37°C, mutant R160K Escherichia coli
4.3.1.7 0.22
-
ethanolamine run 2, pH 8, 37°C, mutant Q162H Escherichia coli
4.3.1.7 0.73
-
ethanolamine run 2, pH 8, 37°C, mutant Q162E Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.7 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.7 using Ni-NTA chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.7 ethanolamine
-
Escherichia coli acetaldehyde + NH3
-
?

Synonyms

EC Number Synonyms Comment Organism
4.3.1.7 EAL
-
Escherichia coli
4.3.1.7 ethanolamine ammonia-lyase
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.1.7 37
-
assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.1.7 0.036
-
ethanolamine run 1, pH 8, 37°C, mutant E287A Escherichia coli
4.3.1.7 0.038
-
ethanolamine run 2, pH 8, 37°C, mutant D362N Escherichia coli
4.3.1.7 0.051
-
ethanolamine run 2, pH 8, 37°C, mutant Q162K Escherichia coli
4.3.1.7 0.066
-
ethanolamine run 2, pH 8, 37°C, mutant E287H Escherichia coli
4.3.1.7 0.085
-
ethanolamine run 1, pH 8, 37°C, mutant D362A Escherichia coli
4.3.1.7 0.086
-
ethanolamine run 2, pH 8, 37°C, mutant E287Q Escherichia coli
4.3.1.7 0.67
-
ethanolamine run 2, pH 8, 37°C, mutant D362E Escherichia coli
4.3.1.7 1
-
ethanolamine run 1, pH 8, 37°C, mutant R160A Escherichia coli
4.3.1.7 1.3
-
ethanolamine run 1, pH 8, 37°C, mutant N193A Escherichia coli
4.3.1.7 2.1
-
ethanolamine run 2, pH 8, 37°C, mutant E287D Escherichia coli
4.3.1.7 3 6 ethanolamine run 2, pH 8, 37°C, mutant N193D Escherichia coli
4.3.1.7 6
-
ethanolamine run 2, pH 8, 37°C, mutant Q162H Escherichia coli
4.3.1.7 20
-
ethanolamine run 1, pH 8, 37°C, mutant Q162A Escherichia coli
4.3.1.7 79
-
ethanolamine run 2, pH 8, 37°C, mutant R160K Escherichia coli
4.3.1.7 110
-
ethanolamine run 2, pH 8, 37°C, mutant Q162E Escherichia coli
4.3.1.7 440
-
ethanolamine run 2, pH 8, 37°C, wild-type Escherichia coli
4.3.1.7 770
-
ethanolamine run 1, pH 8, 37°C, wild-type Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.1.7 8
-
assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.7 adenosylcobalamin
-
Escherichia coli