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Literature summary for 1.16.3.1 extracted from

  • Boonen, F.; Vandamme, A.M.; Etoundi, E.; Pigneur, L.M.; Housen, I.
    Identification and characterization of a novel multicopper oxidase from Acidomyces acidophilus with ferroxidase activity (2014), Biochimie, 102, 37-46 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene Mco1, detailed sequence comparisons and phylogenetic analysis, recombinant expression of N-terminally His-tagged wild-type and truncated mutant enzymes in Escherichia coli Acidomyces acidophilus

Protein Variants

Protein Variants Comment Organism
additional information construction of a truncated enzyme mutant by deletion of the first 83 amino acids containing the putative N-terminal transmembrane helix in order to obtain a soluble protein. Expression of the DELTA-N-truncated protein leads to the production of an insoluble protein that presents a molecular weight estimated at 75 kDa. The truncated protein loses the N-terminal His-tag during or after renaturation step but retains to keep the expected molecular weight, the truncated enzyme shows slightly reduced activity compared to wild-type Acidomyces acidophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
Fe(II) recombinant wild-type enzyme, pH 5.0, 25°C Acidomyces acidophilus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane no predicted signal peptide, but a putative N-terminal transmembrane helix, from amino acid 61-83, is predicted from the enzyme sequence. AaMco1 presents a predicted N-terminal transmembrane helix and lacks the COOH-terminal transmembrane domain common to ferroxidases Acidomyces acidophilus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ a multicopper oxidase, dependent on copper for catalytic activity, sequence motifs for copper binding sites, overview Acidomyces acidophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4 Fe(II) + 4 H+ + O2 Acidomyces acidophilus
-
4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 Acidomyces acidophilus 26774
-
4 Fe(III) + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Acidomyces acidophilus M9PLY0
-
-
Acidomyces acidophilus 26774 M9PLY0
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His-tagged wild-type and truncated mutant enzymes from Escherichia coli by immobilized metal affinity chromatography first under denaturing conditions and second as renaturation step by metal affinity chromatography under native conditions Acidomyces acidophilus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.69
-
purified recombinant N-terminally truncated enzyme mutant, pH 5.0, 25°C Acidomyces acidophilus
0.702
-
purified recombinant wild-type enzyme, pH 5.0, 25°C Acidomyces acidophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 Fe(II) + 4 H+ + O2
-
Acidomyces acidophilus 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2
-
Acidomyces acidophilus 26774 4 Fe(III) + 2 H2O
-
?
additional information AaMco1 has ferroxidase activity. AaMco1 is also able to oxidize the N,N-dimethyl-pphenylenediamine dihydrochloride (DMPPDA) compound. Ferroxidase activity of the purified protein is measured by the ferrozine assay. No activity with 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) (ABTS), 2,6-dimethoxyphenol, and 2-L-ascorbic acid Acidomyces acidophilus ?
-
?
additional information AaMco1 has ferroxidase activity. AaMco1 is also able to oxidize the N,N-dimethyl-pphenylenediamine dihydrochloride (DMPPDA) compound. Ferroxidase activity of the purified protein is measured by the ferrozine assay. No activity with 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) (ABTS), 2,6-dimethoxyphenol, and 2-L-ascorbic acid Acidomyces acidophilus 26774 ?
-
?

Subunits

Subunits Comment Organism
More AaMco1 presents a predicted N-terminal transmembrane helix and lacks the COOH-terminal transmembrane domain common to ferroxidases, structure comparisons, overview Acidomyces acidophilus

Synonyms

Synonyms Comment Organism
MCO1
-
Acidomyces acidophilus
multicopper oxidase 1
-
Acidomyces acidophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Acidomyces acidophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
assay at Acidomyces acidophilus

General Information

General Information Comment Organism
evolution in addition to the classical classification, another cluster containing AaMco1 and filamentous ascomycete hypothetical proteins, putative multicopper oxidases (MCOs) or proteins called ascorbate oxidases is identified on the basis of sequence similarity. This group is named ascomycete MCOs. Neighbor joining tree of multicopper oxidase amino acid sequences, phylogenetic analysis, overview Acidomyces acidophilus