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Literature summary for 1.8.1.20 extracted from

  • Khairy, H.; Wubbeler, J.; Steinbuchel, A.
    The NADH flavin oxidoreductase Nox from Rhodococcus erythropolis MI2 is the key enzyme of 4,4'-dithiodibutyric acid degradation (2016), Lett. Appl. Microbiol., 63, 434-441 .
    View publication on PubMed
Search for more literature for 1.8.1.20

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) pLysS cells Rhodococcus erythropolis

Inhibitors

Inhibitors Comment Organism Structure
Co2+
-
 Rhodococcus erythropolis
Ni2+
-
 Rhodococcus erythropolis
Zn2+
-
 Rhodococcus erythropolis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.6
-
 4,4'-disulfanediyldibutanoate at pH 8.0 and 37°C Rhodococcus erythropolis

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no metal cofactors are required Rhodococcus erythropolis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4,4'-disulfanediyldibutanoate + NADH + H+ Rhodococcus erythropolis the enzyme shows high substrate specificity 4-mercaptobutyric acid + NAD+
-
 ?
4,4'-disulfanediyldibutanoate + NADH + H+ Rhodococcus erythropolis MI2 the enzyme shows high substrate specificity 4-mercaptobutyric acid + NAD+
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodococcus erythropolis
-
-
-
Rhodococcus erythropolis MI2
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Rhodococcus erythropolis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.36
-
 at pH 8.0 and 37°C Rhodococcus erythropolis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4,4'-disulfanediyldibutanoate + NADH + H+ the enzyme shows high substrate specificity Rhodococcus erythropolis 4-mercaptobutyric acid + NAD+
-
 ?
4,4'-disulfanediyldibutanoate + NADH + H+ the enzyme shows high substrate specificity Rhodococcus erythropolis MI2 4-mercaptobutyric acid + NAD+
-
 ?
additional information no activity with NADPH Rhodococcus erythropolis ?
-
 ?
additional information the enzyme has very low activity with 3,3'-dithiodipropionic acid (8.0%), 3,3'-thiodipropionic acid (7.6%), and 5,5'-dithiobis(2-nitrobenzoic acid) (8.0%) Rhodococcus erythropolis ?
-
 ?
additional information no activity with NADPH Rhodococcus erythropolis MI2 ?
-
 ?
additional information the enzyme has very low activity with 3,3'-dithiodipropionic acid (8.0%), 3,3'-thiodipropionic acid (7.6%), and 5,5'-dithiobis(2-nitrobenzoic acid) (8.0%) Rhodococcus erythropolis MI2 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 45000, SDS-PAGE Rhodococcus erythropolis
? x * 43573, calculated from amino acid sequence Rhodococcus erythropolis

Synonyms

Synonyms Comment Organism
NADH:flavin oxidoreductase
-
 Rhodococcus erythropolis
NOX
-
 Rhodococcus erythropolis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65 85 after heating the enzyme for 15 min at 85°C, it retains about 48% of its original activity, however, a stable activity could be recorded at 65°C Rhodococcus erythropolis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5
-
 4,4'-disulfanediyldibutanoate at pH 8.0 and 37°C Rhodococcus erythropolis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Rhodococcus erythropolis

Cofactor

Cofactor Comment Organism Structure
FMN
-
 Rhodococcus erythropolis
NADH the enzyme is highly specific for NADH Rhodococcus erythropolis

pI Value

Organism Comment pI Value Maximum pI Value
Rhodococcus erythropolis calculated from amino acid sequence
-
 8.8