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Information on EC 6.2.1.11 - biotin-CoA ligase
for references in articles please use BRENDA:EC6.2.1.11
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EC Tree 6 Ligases
6.2 Forming carbon-sulfur bonds
6.2.1 Acid-thiol ligases
6.2.1.11 biotin-CoA ligase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
showSynonyms
biotinyl-coa synthetase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Biotinyl CoA synthetase
-
-
-
-
Biotinyl coenzyme A synthetase
-
-
-
-
Biotinyl-CoA synthetase
-
-
-
-
Synthetase, biotinyl coenzyme A
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + biotin + CoA = AMP + diphosphate + biotinyl-CoA
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
biotin:CoA ligase (AMP-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
37318-60-8
-
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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 + alpha-dehydrobiotin + CoA
AMP + diphosphate + alpha-dehydrobiotinyl-CoA
-
Substrates: 27% of the activity relative to biotin
Products: -
Products: -
?
ATP + biotin + CoA
?
-
Substrates: first enzyme involved in biotin degradation
Products: -
Products: -
?
ATP + n-caprylate + CoA
AMP + diphosphate + n-capryloyl-CoA
-
Substrates: 19% of the activity relative to biotin
Products: -
Products: -
?
ATP + n-decanoate + CoA
AMP + diphosphate + n-decanoyl-CoA
-
Substrates: 14% of the activity relative to biotin
Products: -
Products: -
?
ATP + n-laurate + CoA
AMP + diphosphate + n-lauroyl-CoA
-
Substrates: 11% of the activity relative to biotin
Products: -
Products: -
?
ATP + (+/-)-dethiobiotin + CoA
AMP + diphosphate + dethiobiotinyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + (+/-)-dethiobiotin + CoA
AMP + diphosphate + dethiobiotinyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + 5-(2-thienyl)-n-valerate + CoA
AMP + diphosphate + 5-(2-thienyl)-n-valeryl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + 5-(2-thienyl)-n-valerate + CoA
AMP + diphosphate + 5-(2-thienyl)-n-valeryl-CoA
-
Substrates: 19% of the activity relative to biotin
Products: -
Products: -
?
ATP + 5-(2-thienyl)-n-valerate + CoA
AMP + diphosphate + 5-(2-thienyl)-n-valeryl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + actithiazic acid + CoA
AMP + diphosphate + actithiazyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + actithiazic acid + CoA
AMP + diphosphate + actithiazyl-CoA
-
Substrates: 59% of the activity relative to biotin
Products: -
Products: -
?
ATP + actithiazic acid + CoA
AMP + diphosphate + actithiazyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + biotin + CoA
AMP + diphosphate + biotinyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + biotin + CoA
AMP + diphosphate + biotinyl-CoA
-
Substrates: highly specific for ATP
Products: -
Products: -
?
ATP + biotin + CoA
AMP + diphosphate + biotinyl-CoA
-
Substrates: highly specific for ATP
Products: -
Products: -
?
ATP + biotin + CoA
AMP + diphosphate + biotinyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + biotin + CoA
AMP + diphosphate + biotinyl-CoA
Soil bacterium
-
Substrates: -
Products: -
Products: -
?
ATP + dethiobiotin + CoA
AMP + diphosphate + dethiobiotinyl-CoA
-
Substrates: 52% of the activity relative to biotin
Products: -
Products: -
?
ATP + dethiobiotin + CoA
AMP + diphosphate + dethiobiotinyl-CoA
-
Substrates: 26% of the activity relative to biotin
Products: -
Products: -
?
ATP + dethiobiotin + CoA
AMP + diphosphate + dethiobiotinyl-CoA
-
Substrates: 52% of the activity relative to biotin
Products: -
Products: -
?
ATP + dethiobiotin + CoA
AMP + diphosphate + dethiobiotinyl-CoA
-
Substrates: 26% of the activity relative to biotin
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 + biotin + CoA
?
-
Substrates: first enzyme involved in biotin degradation
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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.
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). F8GQ99_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
267
0
28711
TrEMBL
-
Q0K0D6_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
267
0
28762
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
production of alpha-dehydrobiotin, an antibiotic, from biotinyl-CoA with biotinyl-CoA synthetase and acyl-CoA oxidase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanaka, M.; Izumi, Y.; Yamada, H.
Microbial metabolism and production of biotin
Vitamins (Kyoto)
62
305-315
1988
Mycoplana sp., Mycoplana sp. No. 166
-
brenda
Christner, J.E.; Schlesinger, M.J.; Coon, M.J.
Enzymatic activation of biotin. Biotinyl adenylate formation
J. Biol. Chem.
239
3997-4005
1964
Soil bacterium, Sus scrofa
brenda
Yamada, H.; Osakai, M.; Izumi, Y.
Formation of biotinyl-CoA synthetase, the first enzyme involved in microbial biotin degradation
Agric. Biol. Chem.
48
2039-2045
1984
Mycoplana sp., Mycoplana sp. No. 166
-
brenda
Tanaka, M.; Yamamoto H.; Izumi, Y.; Yamada, H.
Purification and properties of biotinyl-CoA synthetase from Mycoplana sp. No. 166
Arch. Biochem. Biophys.
251
479-486
1986
Mycoplana sp.
brenda
Tanaka, M.; Yamamoto, H.; Izumi, Y.; Yamada, H.
Enzymatic production of alpha-dehydrobiotin from biotin
J. Biotechnol.
5
209-220
1987
Mycoplana sp.
-
brenda
Tanaka, M.; Izumi, Y.; Yamada, H.
Enzymatic assay for biotin using biotinyl-CoA synthetase
Agric. Biol. Chem.
51
2585-2586
1987
Mycoplana sp.
-
brenda
EXTERNAL LINKS (specific for EC-Number 6.2.1.11)
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