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Literature summary for 1.4.3.2 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

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

Cloned(Commentary)

Cloned (Comment) Organism
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

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Coprinopsis cinerea A8NBN1
-
-
Coprinopsis cinerea ATCC MYA-4618 A8NBN1
-
-

Purification (Commentary)

Purification (Comment) Organism
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]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + O2 + H2O
-
Coprinopsis cinerea 3-phenylpyruvic acid + ammonia + H2O2
-
?
L-phenylalanine + O2 + H2O
-
Coprinopsis cinerea ATCC MYA-4618 3-phenylpyruvic acid + ammonia + H2O2
-
?
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 ?
-
?
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

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

Synonyms

Synonyms Comment Organism
CC-LPOX
-
Coprinopsis cinerea
L-phenylalanine oxidase
-
Coprinopsis cinerea

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
55
-
purified recombinant enzyme, pH 8.5, loss of 50% activity Coprinopsis cinerea
55
-
purified recombinant enzyme, within pH range 7.0-9.5, stable up to Coprinopsis cinerea
65
-
purified recombinant enzyme, pH 8.5, inactivation Coprinopsis cinerea

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Coprinopsis cinerea

pH Range

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

pH Stability

pH Stability pH Stability Maximum Comment Organism
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