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Results 1 - 10 of 12 > >>
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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the reaction diagram Show all sequences 6.3.1.15ATP + 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 - ?
Display the reaction diagram Show all sequences 6.3.1.15ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin the formation of an acyl adenylate from ring A and ATP is demonstrated by an ATP-PPi exchange assay. The purified nzyme exhibits both activation and transferase activity, i.e. it catalyzed both the activation of ring A as acyl adenylate and the subsequent transfer of the acyl group to the amino group of ring B. The reaction is specific for ATP as nucleotide triphosphate Streptomyces niveus AMP + diphosphate + novobiocic acid - ?
Display the reaction diagram Show all sequences 6.3.1.15ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin the formation of an acyl adenylate from ring A and ATP is demonstrated by an ATP-PPi exchange assay. The purified nzyme exhibits both activation and transferase activity, i.e. it catalyzed both the activation of ring A as acyl adenylate and the subsequent transfer of the acyl group to the amino group of ring B. The reaction is specific for ATP as nucleotide triphosphate Streptomyces niveus NCIMB 11891 AMP + diphosphate + novobiocic acid - ?
Display the reaction diagram Show all sequences 6.3.1.15ATP + 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 - ?
Display the reaction diagram Show all sequences 6.3.1.15ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxycoumarin - Streptomyces niveus AMP + diphosphate + 8-demethylnovobiocic acid - ?
Display the reaction diagram Show all sequences 6.3.1.15ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxycoumarin the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin Streptomyces niveus AMP + diphosphate + 8-demethylnovobiocic acid - ?
Display the reaction diagram Show all sequences 6.3.1.15ATP + 3-geranyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin - Streptomyces niveus AMP + diphosphate + N-(2,7-dihydroxy-8-methyl-4-oxo-4H-chromen-3-yl)-4-hydroxy-3-[(2E)-6-methylhepta-2,5-dien-1-yl]benzamide - ?
Display the reaction diagram Show all sequences 6.3.1.15ATP + 3-geranyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin - Streptomyces niveus NCIMB 11891 AMP + diphosphate + N-(2,7-dihydroxy-8-methyl-4-oxo-4H-chromen-3-yl)-4-hydroxy-3-[(2E)-6-methylhepta-2,5-dien-1-yl]benzamide - ?
Display the reaction diagram Show all sequences 6.3.1.15ATP + 4-hydroxy-3-methylbenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin - 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 - ?
Display the reaction diagram Show all sequences 6.3.1.15ATP + 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 - ?
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