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Information on EC 6.3.1.15 - 8-demethylnovobiocic acid synthase
for references in articles please use BRENDA:EC6.3.1.15
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EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.1 Acid—ammonia (or amine) ligases (amide synthases)
6.3.1.15 8-demethylnovobiocic acid synthase
IUBMB Comments
The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
novobiocin ligase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
8-demethylnovobiocic acid synthetase
8-desmethyl-novobiocic acid synthetase
NovL
novobiocin ligase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxycoumarin = AMP + diphosphate + 8-demethylnovobiocic acid
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
clorobiocin biosynthesis, novobiocin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
3-dimethylallyl-4-hydroxybenzoate:3-amino-4,7-dihydroxycoumarin ligase (AMP-forming)
The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
AMP + diphosphate + novobiocic acid
ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxycoumarin
AMP + diphosphate + 8-demethylnovobiocic acid
ATP + 3-geranyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
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
ATP + 4-hydroxy-3-methylbenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
AMP + diphosphate + 3-[(2E)-but-2-en-1-yl]-N-(2,7-dihydroxy-8-methyl-4-oxo-4H-chromen-3-yl)-4-hydroxybenzylamide
ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
AMP + diphosphate + novobiocic acid
Substrates: 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
Products: -
Products: -
?
ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
AMP + diphosphate + novobiocic acid
Substrates: 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
Products: -
Products: -
?
ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
AMP + diphosphate + novobiocic acid
Substrates: 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
Products: -
Products: -
?
ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
AMP + diphosphate + novobiocic acid
Substrates: 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
Products: -
Products: -
?
ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxycoumarin
AMP + diphosphate + 8-demethylnovobiocic acid
-
Substrates: -
Products: -
Products: -
?
ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxycoumarin
AMP + diphosphate + 8-demethylnovobiocic acid
-
Substrates: the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin
Products: -
Products: -
?
ATP + 3-geranyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
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
Substrates: -
Products: -
Products: -
?
ATP + 3-geranyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
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
Substrates: -
Products: -
Products: -
?
ATP + 4-hydroxy-3-methylbenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
AMP + diphosphate + 3-[(2E)-but-2-en-1-yl]-N-(2,7-dihydroxy-8-methyl-4-oxo-4H-chromen-3-yl)-4-hydroxybenzylamide
Substrates: -
Products: -
Products: -
?
ATP + 4-hydroxy-3-methylbenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
AMP + diphosphate + 3-[(2E)-but-2-en-1-yl]-N-(2,7-dihydroxy-8-methyl-4-oxo-4H-chromen-3-yl)-4-hydroxybenzylamide
Substrates: catalytic efficiency for 3-methyl-4-hydroxybenzoate is 72fold lower compared to the natural substrate 4-hydroxy-3-dimethylbenzoate
Products: -
Products: -
?
ATP + 4-hydroxy-3-methylbenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
AMP + diphosphate + 3-[(2E)-but-2-en-1-yl]-N-(2,7-dihydroxy-8-methyl-4-oxo-4H-chromen-3-yl)-4-hydroxybenzylamide
Substrates: -
Products: -
Products: -
?
ATP + 4-hydroxy-3-methylbenzoate + 3-amino-4,7-dihydroxy-8-methylcoumarin
AMP + diphosphate + 3-[(2E)-but-2-en-1-yl]-N-(2,7-dihydroxy-8-methyl-4-oxo-4H-chromen-3-yl)-4-hydroxybenzylamide
Substrates: catalytic efficiency for 3-methyl-4-hydroxybenzoate is 72fold lower compared to the natural substrate 4-hydroxy-3-dimethylbenzoate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3-dimethylallyl-4-hydroxybenzoate + 3-amino-4,7-dihydroxycoumarin
AMP + diphosphate + 8-demethylnovobiocic acid
-
Substrates: the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
0.5 mM, reduces the enzyme activity to 1.4% of the maximal activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.36
4-hydroxy-3-methylbenzoate
pH 7.0, temperature not specified in the publication
0.0064
3-dimethylallyl-4-hydroxybenzoate
pH 7.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.47
3-dimethylallyl-4-hydroxybenzoate
pH 7.0, temperature not specified in the publication
0.36
4-hydroxy-3-methylbenzoate
pH 7.0, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
73.4
3-dimethylallyl-4-hydroxybenzoate
pH 7.0, temperature not specified in the publication
1
4-hydroxy-3-methylbenzoate
pH 7.0, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin
physiological function
the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin
physiological function
-
the enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A1V5JN80_9DELT
309
0
33749
TrEMBL
-
A0A2K8PP65_STRLA
514
0
53359
TrEMBL
-
A0A1J5T221_9ZZZZ
483
0
51535
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2K8P8J1_STRLA
523
0
56269
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pacholec, M.; Tao, J.; Walsh, C.T.
CouO and NovO: C-methyltransferases for tailoring the aminocoumarin scaffold in coumermycin and novobiocin antibiotic biosynthesis
Biochemistry
44
14969-14976
2005
Streptomyces niveus
brenda
Steffensky, M.; Li, S.M.; Heide, L.
Cloning, overexpression, and purification of novobiocic acid synthetase from Streptomyces spheroides NCIMB 11891
J. Biol. Chem.
275
21754-21760
2000
Streptomyces niveus (Q9L9F6), Streptomyces niveus NCIMB 11891 (Q9L9F6)
brenda
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
Proc. Natl. Acad. Sci. USA
101
10036-10041
2004
Streptomyces niveus (Q9L9F6), Streptomyces niveus NCIMB 11891 (Q9L9F6)
brenda
EXTERNAL LINKS (specific for EC-Number 6.3.1.15)
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Release 2023.1 (January 2023)
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