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Literature summary extracted from

  • Zhang, J.; Yang, D.; Yan, Q.; Jiang, Z.
    Characterization of a novel L-phenylalanine oxidase from Coprinopsis cinereus and its application for enzymatic production of phenylpyruvic acid (2017), Process Biochem., 61, 102-109 .
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.4.3.2 FAD activates at 0.002 mM, inhibits at 0.004-0.008 mM Coprinopsis cinerea

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.3.2 DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3) Coprinopsis cinerea

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.2 2-mercaptoethanol
-
 Coprinopsis cinerea
1.4.3.2 Ca2+ slight inhibition Coprinopsis cinerea
1.4.3.2 Co2+ slight inhibition Coprinopsis cinerea
1.4.3.2 Cr3+ slight inhibition Coprinopsis cinerea
1.4.3.2 CTAB strong inhibition Coprinopsis cinerea
1.4.3.2 Cu2+ complete inhibition Coprinopsis cinerea
1.4.3.2 DTT slight inhibition Coprinopsis cinerea
1.4.3.2 EDTA
-
 Coprinopsis cinerea
1.4.3.2 FAD activates at 0.002 mM, inhibits at 0.004-0.008 mM Coprinopsis cinerea
1.4.3.2 Fe2+ strong inhibition Coprinopsis cinerea
1.4.3.2 Fe3+ slight inhibition Coprinopsis cinerea
1.4.3.2 K+
-
 Coprinopsis cinerea
1.4.3.2 Li+ slight inhibition Coprinopsis cinerea
1.4.3.2 Mg2+ slight inhibition Coprinopsis cinerea
1.4.3.2 Mn2+ slight inhibition Coprinopsis cinerea
1.4.3.2 Ni2+
-
 Coprinopsis cinerea
1.4.3.2 SDS complete inhibition Coprinopsis cinerea

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.3.2 Ba2+ activates slightly Coprinopsis cinerea
1.4.3.2 additional information no effect by NaCl Coprinopsis cinerea
1.4.3.2 Sr2+ activates slightly Coprinopsis cinerea
1.4.3.2 Triton X-100 activates slightly Coprinopsis cinerea
1.4.3.2 Zn2+ activates slightly Coprinopsis cinerea

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.3.2 L-phenylalanine + O2 + H2O Coprinopsis cinerea
-
 3-phenylpyruvic acid + ammonia + H2O2
-
 ?
1.4.3.2 L-phenylalanine + O2 + H2O Coprinopsis cinerea ATCC MYA-4618
-
 3-phenylpyruvic acid + ammonia + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.2 Coprinopsis cinerea A8NBN1
-
-
1.4.3.2 Coprinopsis cinerea ATCC MYA-4618 A8NBN1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.2 recombinant His-tagged enzyme 35fold from Escherichia coli strain Rosetta (DE3) by nickel affinity and hydrophbic interaction chromatography Coprinopsis cinerea

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.3.2 6.04
-
 purified recombinant enzyme, substrate L-phenylalanine, pH 8.5, 45°C Coprinopsis cinerea

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.2 L-phenylalanine + O2 + H2O
-
 Coprinopsis cinerea 3-phenylpyruvic acid + ammonia + H2O2
-
 ?
1.4.3.2 L-phenylalanine + O2 + H2O
-
 Coprinopsis cinerea ATCC MYA-4618 3-phenylpyruvic acid + ammonia + H2O2
-
 ?
1.4.3.2 additional information the enzyme specifically catalyzes the oxidation of L-phenylalanine with racemic NULL,L-phenylalanine mixture as substrate, substrate specificity, overview. The enzyme shows low activity with L-tyrosine and L-hhistidine besides L-phenylalanine, which is the preferred substrate Coprinopsis cinerea ?
-
 ?
1.4.3.2 additional information the enzyme specifically catalyzes the oxidation of L-phenylalanine with racemic NULL,L-phenylalanine mixture as substrate, substrate specificity, overview. The enzyme shows low activity with L-tyrosine and L-hhistidine besides L-phenylalanine, which is the preferred substrate Coprinopsis cinerea ATCC MYA-4618 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.3.2 ? x * 87100, recombinant His-tagged enzyme, SDS-PAGE Coprinopsis cinerea

Synonyms

EC Number Synonyms Comment Organism
1.4.3.2 CC-LPOX
-
 Coprinopsis cinerea
1.4.3.2 L-phenylalanine oxidase
-
 Coprinopsis cinerea

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.3.2 45
-
-
 Coprinopsis cinerea

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.4.3.2 30 55 activity range, profile overview Coprinopsis cinerea

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.3.2 40 60 thermal denaturing half-lives of the enzyme at 40, 45, 50, 55 and 60°C are 1855, 642, 332, 105 and 23 min, respectively Coprinopsis cinerea
1.4.3.2 55
-
 purified recombinant enzyme, pH 8.5, loss of 50% activity Coprinopsis cinerea
1.4.3.2 55
-
 purified recombinant enzyme, within pH range 7.0-9.5, stable up to Coprinopsis cinerea
1.4.3.2 65
-
 purified recombinant enzyme, pH 8.5, inactivation Coprinopsis cinerea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.2 8.5
-
-
 Coprinopsis cinerea

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.4.3.2 7.5 10.5 activity range, profile overview Coprinopsis cinerea

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.4.3.2 7.5 9.5 purified recombinant enzyme, highly stable at, 55°C, loss of about 50% activity at pH 3.0-6.0, loss of 40% activity at pH 11.0 Coprinopsis cinerea