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Literature summary for 6.3.1.15 extracted from

  • Pi, N.; Meyers, C.L.; Pacholec, M.; Walsh, C.T.; Leary, J.A.
    Mass spectrometric characterization of a three-enzyme tandem reaction for assembly and modification of the novobiocin skeleton (2004), Proc. Natl. Acad. Sci. USA, 101, 10036-10041.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.1.15

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0064
-
 3-dimethylallyl-4-hydroxybenzoate pH 7.0, temperature not specified in the publication Streptomyces niveus
0.36
-
 4-hydroxy-3-methylbenzoate pH 7.0, temperature not specified in the publication Streptomyces niveus

Organism

Organism UniProt Comment Textmining
Streptomyces niveus Q9L9F6
-
-
Streptomyces niveus NCIMB 11891 Q9L9F6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin in the sequential bi-bi catalytic mechanism, NovL binds to the benzoic acid moiety and the aminocoumarin ring to form a ternary complex, catalyzes the ligation between substrates inside the complex, and subsequently releases the reaction products, novobiocic acid and water Streptomyces niveus AMP + diphosphate + novobiocic acid
-
 ?
ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin in the sequential bi-bi catalytic mechanism, NovL binds to the benzoic acid moiety and the aminocoumarin ring to form a ternary complex, catalyzes the ligation between substrates inside the complex, and subsequently releases the reaction products, novobiocic acid and water Streptomyces niveus NCIMB 11891 AMP + diphosphate + novobiocic acid
-
 ?
ATP + 4-hydroxy-3-methylbenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin catalytic efficiency for 3-methyl-4-hydroxybenzoate is 72fold lower compared to the natural substrate 4-hydroxy-3-dimethylbenzoate Streptomyces niveus AMP + diphosphate + 3-[(2E)-but-2-en-1-yl]-N-(2,7-dihydroxy-8-methyl-4-oxo-4H-chromen-3-yl)-4-hydroxybenzylamide
-
 ?
ATP + 4-hydroxy-3-methylbenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin catalytic efficiency for 3-methyl-4-hydroxybenzoate is 72fold lower compared to the natural substrate 4-hydroxy-3-dimethylbenzoate Streptomyces niveus NCIMB 11891 AMP + diphosphate + 3-[(2E)-but-2-en-1-yl]-N-(2,7-dihydroxy-8-methyl-4-oxo-4H-chromen-3-yl)-4-hydroxybenzylamide
-
 ?

Synonyms

Synonyms Comment Organism
8-demethylnovobiocic acid synthetase
-
 Streptomyces niveus
8-desmethyl-novobiocic acid synthetase
-
 Streptomyces niveus
NovL
-
 Streptomyces niveus
novobiocin ligase
-
 Streptomyces niveus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.36
-
 4-hydroxy-3-methylbenzoate pH 7.0, temperature not specified in the publication Streptomyces niveus
0.47
-
 3-dimethylallyl-4-hydroxybenzoate pH 7.0, temperature not specified in the publication Streptomyces niveus

General Information

General Information Comment Organism
physiological function the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin Streptomyces niveus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1
-
 4-hydroxy-3-methylbenzoate pH 7.0, temperature not specified in the publication Streptomyces niveus
73.4
-
 3-dimethylallyl-4-hydroxybenzoate pH 7.0, temperature not specified in the publication Streptomyces niveus