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Literature summary extracted from

  • Freel Meyers, C.L.; Oberthür, M.; Xu, H.; Heide, L.; Kahne, D.; Walsh, C.T.
    Characterization of NovP and NovN: completion of novobiocin biosynthesis by sequential tailoring of the noviosyl ring (2004), Angew. Chem. Int. Ed. Engl., 43, 67-70.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.285 expression in Escherichia coli Streptomyces niveus
2.1.3.12 expression in Escherichia coli Streptomyces niveus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.285 0.0095
-
 demethyldecarbamoylnovobiocin pH 8.5, 22°C Streptomyces niveus
2.1.3.12 0.0046
-
 decarbamoylnovobiocin pH 8.5, 22°C Streptomyces niveus
2.1.3.12 0.0051
-
 Carbamoyl phosphate pH 8.5, 22°C Streptomyces niveus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.285 S-adenosyl-L-methionine + demethyldecarbamoylnovobiocin Streptomyces niveus the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic, novobiocin S-adenosyl-L-homocysteine + decarbamoylnovobiocin
-
 ?
2.1.3.12 carbamoyl phosphate + decarbamoylnovobiocin Streptomyces niveus the enzyme is involved in the biosynthesis of the aminocoumarin antibiotics, novobiocin phosphate + novobiocin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.285 Streptomyces niveus
-
-
-
2.1.3.12 Streptomyces niveus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.285 His6-tagged protein Streptomyces niveus
2.1.3.12 N-His6-tagged protein Streptomyces niveus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.285 S-adenosyl-L-methionine + demethyldecarbamoylnovobiocin
-
 Streptomyces niveus S-adenosyl-L-homocysteine + decarbamoylnovobiocin
-
 ?
2.1.1.285 S-adenosyl-L-methionine + demethyldecarbamoylnovobiocin the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic, novobiocin Streptomyces niveus S-adenosyl-L-homocysteine + decarbamoylnovobiocin
-
 ?
2.1.3.12 carbamoyl phosphate + decarbamoylnovobiocin
-
 Streptomyces niveus phosphate + novobiocin
-
 ?
2.1.3.12 carbamoyl phosphate + decarbamoylnovobiocin the enzyme is involved in the biosynthesis of the aminocoumarin antibiotics, novobiocin Streptomyces niveus phosphate + novobiocin
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.285 NovP
-
 Streptomyces niveus
2.1.3.12 NovN
-
 Streptomyces niveus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.285 22
-
 assay at room temperature Streptomyces niveus
2.1.3.12 22
-
 assay at room temperature Streptomyces niveus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.285 0.4
-
 demethyldecarbamoylnovobiocin pH 8.5, 22°C Streptomyces niveus
2.1.3.12 4.1
-
 decarbamoylnovobiocin pH 8.5, 22°C Streptomyces niveus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.285 8.5
-
 assay at Streptomyces niveus
2.1.3.12 8.5
-
 assay at Streptomyces niveus

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.3.12 ATP activation, carbamoyltransferase activity of NovN is dependent upon Mg-ATP Streptomyces niveus

General Information

EC Number General Information Comment Organism
2.1.1.285 physiological function the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic, novobiocin Streptomyces niveus
2.1.3.12 physiological function the enzyme is involved in the biosynthesis of the aminocoumarin antibiotics, novobiocin Streptomyces niveus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.1.1.285 42.1
-
 demethyldecarbamoylnovobiocin pH 8.5, 22°C Streptomyces niveus
2.1.3.12 891
-
 decarbamoylnovobiocin pH 8.5, 22°C Streptomyces niveus