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Literature summary for 1.14.13.128 extracted from

  • Summers, R.M.; Seffernick, J.L.; Quandt, E.M.; Yu, C.L.; Barrick, J.E.; Subramanian, M.V.
    Caffeine junkie: an unprecedented glutathione S-transferase-dependent oxygenase required for caffeine degradation by Pseudomonas putida CBB5 (2013), J. Bacteriol., 195, 3933-3939.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Pseudomonas putida

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0153
-
7-methylxanthine in 50 mM potassium phosphate buffer (pH 7.5) at 30°C Pseudomonas putida

Metals/Ions

Metals/Ions Comment Organism Structure
Iron contains a non-heme iron domain Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7-methylxanthine + O2 + NADH + H+ Pseudomonas putida the N7-demethylation reaction absolutely requires a unique, tightly bound protein complex composed of NdmC, NdmD, and NdmE. NdmE functions as a noncatalytic subunit that serves a structural role in the complexation of the oxygenase (NdmC) and Rieske domains (NdmD) xanthine + NAD+ + H2O + formaldehyde
-
?
7-methylxanthine + O2 + NADH + H+ Pseudomonas putida CBB5 the N7-demethylation reaction absolutely requires a unique, tightly bound protein complex composed of NdmC, NdmD, and NdmE. NdmE functions as a noncatalytic subunit that serves a structural role in the complexation of the oxygenase (NdmC) and Rieske domains (NdmD) xanthine + NAD+ + H2O + formaldehyde
-
?
additional information Pseudomonas putida no activity toward caffeine or theobromine ?
-
?
additional information Pseudomonas putida CBB5 no activity toward caffeine or theobromine ?
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas putida M1EY73
-
-
Pseudomonas putida CBB5 M1EY73
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and Sephacryl S200 gel filtration Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7-methylxanthine + O2 + NADH + H+ the N7-demethylation reaction absolutely requires a unique, tightly bound protein complex composed of NdmC, NdmD, and NdmE. NdmE functions as a noncatalytic subunit that serves a structural role in the complexation of the oxygenase (NdmC) and Rieske domains (NdmD) Pseudomonas putida xanthine + NAD+ + H2O + formaldehyde
-
?
7-methylxanthine + O2 + NADH + H+ the N7-demethylation reaction absolutely requires a unique, tightly bound protein complex composed of NdmC, NdmD, and NdmE. NdmE functions as a noncatalytic subunit that serves a structural role in the complexation of the oxygenase (NdmC) and Rieske domains (NdmD) Pseudomonas putida CBB5 xanthine + NAD+ + H2O + formaldehyde
-
?
additional information no activity toward caffeine or theobromine Pseudomonas putida ?
-
?
additional information no activity toward caffeine or theobromine Pseudomonas putida CBB5 ?
-
?

Synonyms

Synonyms Comment Organism
NdmC
-
Pseudomonas putida

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.16
-
7-methylxanthine in 50 mM potassium phosphate buffer (pH 7.5) at 30°C Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
NADH
-
Pseudomonas putida

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
10.17
-
7-methylxanthine in 50 mM potassium phosphate buffer (pH 7.5) at 30°C Pseudomonas putida