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Literature summary 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)

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.128 0.0153
-
 7-methylxanthine in 50 mM potassium phosphate buffer (pH 7.5) at 30°C Pseudomonas putida

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.128 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
-
 ?
1.14.13.128 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
-
 ?
1.14.13.128 additional information Pseudomonas putida no activity toward caffeine or theobromine ?
-
 ?
1.14.13.128 additional information Pseudomonas putida CBB5 no activity toward caffeine or theobromine ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.128 Pseudomonas putida M1EY73
-
-
1.14.13.128 Pseudomonas putida CBB5 M1EY73
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.128 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
-
 ?
1.14.13.128 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
-
 ?
1.14.13.128 additional information no activity toward caffeine or theobromine Pseudomonas putida ?
-
 ?
1.14.13.128 additional information no activity toward caffeine or theobromine Pseudomonas putida CBB5 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.128 NdmC
-
 Pseudomonas putida

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.128 0.16
-
 7-methylxanthine in 50 mM potassium phosphate buffer (pH 7.5) at 30°C Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.128 NADH
-
 Pseudomonas putida

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.14.13.128 10.17
-
 7-methylxanthine in 50 mM potassium phosphate buffer (pH 7.5) at 30°C Pseudomonas putida