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Literature summary for 1.4.1.20 extracted from

  • Villalonga, R.; Fujii, A.; Shinohara, H.; Asano, Y.; Cao, R.; Tachibana, S.; Ortiz, P.
    Supramolecular-mediated immobilization of L-phenylalanine dehydrogenase on cyclodextrin-coated Au electrodes for biosensor applications (2007), Biotechnol. Lett., 29, 447-452.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 (DE3)/pBBNH cells Bacillus badius

General Stability

General Stability Organism
2.5 mM L-Phe after 21 days of incubation at 4°C in 50 mM sodium phosphate buffer, pH 7.0 Bacillus badius
the enzyme-coated Au-CD electrode is highly stable, retaining about 97% of its initial electrocatalytic response toward Bacillus badius

Organism

Organism UniProt Comment Textmining
Bacillus badius
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-affinity column chromatography Bacillus badius

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
the enzyme immobilized on Au-CD electrodes has a specific activity of 10.3 U/mg representing about 56% and 73% of the initial catalytic activity of native and adamantane-modified PheDH, respectively Bacillus badius

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Phe + H2O + NAD+
-
Bacillus badius phenylpyruvate + NH3 + NADH
-
?

Synonyms

Synonyms Comment Organism
PheDH
-
Bacillus badius

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Bacillus badius