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Literature summary for 1.16.3.4 extracted from

  • Classen, T.; Pietruszka, J.; Schuback, S.M.
    A new multicopper oxidase from Gram-positive bacterium Rhodococcus erythropolis with activity modulating methionine rich tail (2013), Protein Expr. Purif., 89, 97-108.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
apo- and holo-form of CueO are expressed in Escherichia coli Rhodococcus erythropolis
apo- and holo-form of CueO are expressed in Escherichia coli as His-tagged fusion proteins Rhodococcus erythropolis

Protein Variants

Protein Variants Comment Organism
additional information truncated enzyme with a deleted methionine-rich C-terminal tail region shows a decreased turnover and a slightly lower Km value. Ki (Cu+) value increased compared to wild-type. Catalytic efficacy similar to wild-type Rhodococcus erythropolis

Inhibitors

Inhibitors Comment Organism Structure
Cu+
-
Rhodococcus erythropolis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00002
-
Cu+ pH 5.5, 30°C, mutant containing a deleted methionine-rich C-terminal tail Rhodococcus erythropolis
0.00008
-
Cu+ pH 5.5, 30°C, wild-type Rhodococcus erythropolis

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ upon incubation with Cu2+ ions, low active apo-CueOR is converted into the active holo-CueOR in vivo Rhodococcus erythropolis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
SDS-PAGE Rhodococcus erythropolis
55000
-
SDS-PAGE, apo-CueO Rhodococcus erythropolis

Organism

Organism UniProt Comment Textmining
Rhodococcus erythropolis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulphonic acid + Cu(I) + O2
-
Rhodococcus erythropolis ?
-
?
2,6-dimethoxyphenol + Cu(I) + O2
-
Rhodococcus erythropolis ?
-
?
Cu+ + H+ + O2
-
Rhodococcus erythropolis Cu2+ + H2O
-
?

Synonyms

Synonyms Comment Organism
CueO
-
Rhodococcus erythropolis
More enzyme possesses EC 1.10.3.2 laccase activity Rhodococcus erythropolis
multicopper oxidase
-
Rhodococcus erythropolis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Rhodococcus erythropolis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25 45 holo CueO Rhodococcus erythropolis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.038
-
Cu+ pH 5.5, 30°C, mutant containing a deleted methionine-rich C-terminal tail Rhodococcus erythropolis
0.155
-
Cu+ pH 5.5, 30°C, wild-type Rhodococcus erythropolis
22.15
-
2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulphonic acid pH 5.5, 30°C Rhodococcus erythropolis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
assay at Rhodococcus erythropolis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000039
-
Cu+ pH 5.5, 30°C, wild-type Rhodococcus erythropolis
0.00008
-
Cu+ pH 5.5, 30°C, mutant containing a deleted methionine-rich C-terminal tail Rhodococcus erythropolis