Information on EC 2.8.1.6 - biotin synthase

New: Word Map on EC 2.8.1.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.8.1.6
-
RECOMMENDED NAME
GeneOntology No.
biotin synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfur atom transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
biotin biosynthesis
-
-
biotin biosynthesis from 8-amino-7-oxononanoate I
-
-
biotin biosynthesis from 8-amino-7-oxononanoate II
-
-
Biotin metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
dethiobiotin:sulfur-(sulfur carrier) sulfurtransferase
The enzyme binds a [4Fe-4S] and a [2Fe-2S] cluster. In every reaction cycle, the enzyme consumes two molecules of AdoMet, each producing 5'-deoxyadenosine and a putative dethiobiotinyl carbon radical. Reaction with another equivalent of AdoMet results in abstraction of the C6 methylene pro-S hydrogen atom from 9-mercaptodethiobiotin, and the resulting carbon radical is quenched via formation of an intramolecular C-S bond, thus closing the biotin thiophane ring. The sulfur donor is believed to be the [2Fe-2S] cluster, which is sacrificed in the process, so that in vitro the reaction is a single turnover. In vivo, the [2Fe-2S] cluster can be reassembled by the Isc or Suf iron-sulfur cluster assembly systems, to allow further catalysis.
CAS REGISTRY NUMBER
COMMENTARY hide
153554-27-9
synthetase, biotin (Saccharomyces cerevisiae strain 20B-12 clone pUCH2.4 gene BIO2 reduced) /biotin synthase (Saccharomyces cerevisiae strain 20B-12 clone pUCH2.4 gene BIO2)
174764-24-0
synthase, biotin (Arabidopsis thaliana clone lambdaBIO2 gene bioB) /BIO2 protein (Arabidopsis thaliana clone pMP101 gene BIO2 reduced) /genBank U24147-derived protein /genBank U31806-derived protein GI 1403662 /synthetase, biotin (Arabidopsis thaliana clone pMP101 gene BIO2 reduced) /synthetase, biotin (Arabidopsis thaliana clone pYESCBS1 gene bioB)
179608-56-1
synthetase, biotin (Bacillus subtilis clone pBIO100/pBIO350/pBIO201 gene bioB) /biotin synthetase (Bacillus subtilis gene bioB) /genBank AF008220-derived protein GI 2293187 /genBank U51869-derived protein GI 1277029 /genBank Z99119-derived protein GI 2635504 /Synthetase, biotin (Bacillus subtilis gene bioB)
204794-88-7
biotin synthetase (Aquifex aeolicus gene bioB) /genBank AE000716-derived protein GI 2983482
209603-31-6
biotin synthase (Treponema pallidum gene TP0228) /genBank AE001204-derived protein GI 3322497
215108-34-2
biotin synthetase (Chlamydia trachomatis gene birA) /genBank AE001343-derived protein GI 3329182
80146-93-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
Lavandula vera
-
-
-
Manually annotated by BRENDA team
strain W303-1A, W303-1B, BY4742
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
biotin synthase catalyzes the final step in the biosynthesis of biotin
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
9-mercaptodethiobiotin + S-adenosyl-L-methionine
biotin + ?
show the reaction diagram
-
presence of S-adenosyl-L-methionine is required
-
-
?
9-mercaptodethiobiotin + sulfur
biotin
show the reaction diagram
-
-
-
?
9-mercaptodethiobiotin + [S] + S-adenosyl-L-methionine
biotin + ?
show the reaction diagram
-
-
-
-
?
9-mercaptodethiobiotin + [S] + S-adenosyl-L-methionine
biotin + L-methionine + 5'-deoxyadenosine
show the reaction diagram
-
-
-
-
ir
dethiobiotin + Na2S
biotin
show the reaction diagram
-
-
-
-
?
dethiobiotin + Na2Se
selenobiotin
show the reaction diagram
-
enzyme depleted of iron and sulfur and reconstituted with FeCl3 and Na2Se yielding an [2Fe-2Se]2+ cluster. Activity with Na2Se is lower than that of the as-isolated enzyme with Na2S
-
-
?
dethiobiotin + S-adenosyl-L-methionine
biotin + ?
show the reaction diagram
-
-
-
-
?
dethiobiotin + sulfur
biotin
show the reaction diagram
dethiobiotin + sulfur + 2 S-adenosyl-L-methionine
biotin + 2 L-methionine + 2 5'-deoxyadenosine
show the reaction diagram
dethiobiotin + sulfur + S-adenosyl-L-methionine
biotin + L-methionine + 5'-deoxyadenosine
show the reaction diagram
-
-
-
-
?
dethiobiotin + [S] + 2 S-adenosyl-L-methionine
biotin + 2 L-methionine + 2 5'-deoxyadenosine
show the reaction diagram
-
-
-
-
ir
dethiobiotin + [S] + S-adenosyl-L-methionine
9-mercaptodethiobiotin + L-methionine + 5'-deoxyadenosine
show the reaction diagram
-
9-mercaptodethiobiotin is generated as a ligand to the [2Fe-2S]2+ cluster during the reaction
-
-
ir
dethiobiotin + [S] + S-adenosyl-L-methionine
biotin + L-methionine + 5'-deoxyadenosine
show the reaction diagram
L-cysteine
L-alanine + sulfide
show the reaction diagram
-
enzyme displays cysteine desulfurase activity, providing it with the ability to mobilize sulfur from free cysteine
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dethiobiotin + sulfur
biotin
show the reaction diagram
dethiobiotin + sulfur + 2 S-adenosyl-L-methionine
biotin + 2 L-methionine + 2 5'-deoxyadenosine
show the reaction diagram
dethiobiotin + sulfur + S-adenosyl-L-methionine
biotin + L-methionine + 5'-deoxyadenosine
show the reaction diagram
-
-
-
-
?
additional information
?
-
Q9HF48
rate-limiting enzyme for biotin synthesis
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
enhances activity
Fe-S center
Ferredoxin
-
required
-
flavodoxin
-
required
-
iron-sulfur centre
-
-
S-adenosyl-L-methionine
-
-
thiamine diphosphate
-
required
additional information
-
not: pyridoxal 5-phosphate
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
enhances activity
Mn2+
-
enhances activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-deoxyadenosine
acidomycin
-
structural analog of biotin, complete inhibition at 0.4 mM, 50% inhibition at 0.035 mM
Cd2+
-
1 mM, almost complete inhibition
Co2+
-
1 mM, almost complete inhibition
Cu2+
-
1 mM, almost complete inhibition
Fe2+
-
above 1 mM
Hg2+
-
1 mM, almost complete inhibition
L-methionine
-
product inhibition. The combination of both products in equimolar concentrations results in more than simple additive inhibition, suggesting that they bind cooperatively to the enzyme.
NaBH4
-
decreases cysteine desulfurase and biotin synthase activity
S-adenosyl-L-homocysteine
-
potent inhibitor
sinefungin
-
-
Zn2+
-
1 mM, almost complete inhibition
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
amino acid
-
one of the amino acids: Asn, Asp, Gln or Ser
asparagine
-
required
D-fructose 1,6-bisphosphate
-
enhances biotin formation
dithiothreitol
flavodoxin
-
-
-
flavodoxin reductase
fructose 1,6-diphosphate
-
-
L-cysteine
MioC
-
essential, may function as an electron transport protein
-
NifS
-
a member of the Nif protein family stimulates biotin production
-
NifU
-
a member of the Nif protein family stimulates biotin production
-
Pyridine nucleotide
-
required, NADPH being most effective
-
pyridoxal 5'-phosphate
-
required for cysteine desulfurase activity of the enzyme
S-adenosyl-L-methionine
thiamine diphosphate-dependent protein
-
required
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 0.2
9-Mercaptodethiobiotin
0.0016 - 0.03
dethiobiotin
0.03
L-cysteine
-
pH 8, 37C
0.01
S-adenosyl-L-methionine
-
in 50 mM Tris-HCl, 100 mM KCl, and 5 mM dithiothreitol, pH 8.0, at 37C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000005 - 13.9
dethiobiotin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00065
S-adenosyl-L-homocysteine
-
in 50 mM Tris-HCl, 100 mM KCl, and 5 mM dithiothreitol, pH 8.0, at 37C
0.075
sinefungin
-
in 50 mM Tris-HCl, 100 mM KCl, and 5 mM dithiothreitol, pH 8.0, at 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
pH 7: about 50% of maximal activity, pH 9: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 40
-
35C: about 70% of maximal activity, 40C: about 60% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Lavandula vera
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Methanosarcina barkeri (strain Fusaro / DSM 804)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
Adx1 isozyme, SDS-PAGE
38650 - 39670
-
wild-type and mutant enzymes, electrospray mass spectrometry
41650
-
calculated from nucleotide sequence
45000
-
His6-BioB, determined by SDS-PAGE and Western blot analysis
50000
AdxR isozyme, SDS-PAGE
75000
-
gel filtration
76000
-
dimeric form
80000
-
gel filtration
82630
-
homodimer, theoretical
90680
-
homodimer, determined by analytical ultracentrifugation
104000
-
at least 3 forms of the enzyme: 82000 Da, 104000 Da, 160000 Da
160000
-
at least 3 forms of the enzyme: 82000 Da, 104000 Da, 160000 Da
165300
-
homotetramer, theoretical
173900
-
homotetramer, determined by analytical ultracentrifugation, non-physiological form
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 38000, SDS-PAGE
homodimer
monomer
-
enzyme exists in 2 forms: a dimer and a monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complexed with S-adenosyl-L-methionine and dethiobiotin; in complex with S-adensyl-L-methionine and dethiobiotin
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
The loss of each FeS cluster results in a corresponding moderate decrease in the thermal stability, loss of the [4Fe-4S]2+ cluster and the bound substrates results in a 7C decrease in stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loses all its clusters if the purification is carried out with buffers that have not been saturated with argon
-
loss of the [2Fe-2S]2+ cluster from BioB does not result in global unfolding of the polypeptide chain at 20C and does not result in significant destabilization of the dimer interface
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen sensitive
-
645582
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His6-BioB is purified from Escherichia coli K12 WT strain BW25113, or from knockout strains lacking HscA, HscB, or DnaK, purification on a Ni-NTA-agarose column
-
wild-type and mutant enzymes
-
wild-type and mutants N151A, H152A, N153A, D155A. Purified enzymes have a reddish brown colour
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834(DE3) cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expression in Escherichia coli. The amino-terminal portion of the BIO2 gene may play a role in localizing the BIO2 protein to a subcellular compartment
-
hexahistidine tagged protein is expressed in Escherichia coli cells
-
hexahistidine tagged proteins are expressed in Escherichia coli BL21DE3 pLysS cells
-
The delta pdxH::CAT allele of strain TX2767 is transduced into strain ER47 with phage P1vir to give strain AH14 into which plasmids pER30 and pER35 are introduced
-
the primary sequence of the Arabidopsis biotin synthase is similar to biotin synthase from Escherichia coli, Serratia marcescens and Saccharomyces cerevisiae, about 50% sequence identity, and more distantly related to the Bacillus sphaericus enzyme, 33% sequence identity
-
wild-type and mutants
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C188S
-
enzyme is insoluble
C276A
-
normal enzyme activity
C288A
-
normal enzyme activity
C288T
-
normal enzyme activity
C53S
-
no enzyme activity, spectrum shows no peak indicative of the presence of an [Fe-S] cluster
C57S
-
no enzyme activity, spectrum shows no peak indicative of the presence of an [Fe-S] cluster
C60S
-
no enzyme activity, spectrum shows no peak indicative of the presence of an [Fe-S] cluster
D155E
-
mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet
D155N
-
mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet
D155S
-
mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet
N153D
-
mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet
N153Q
-
mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet
R260A
-
contains 1.8 iron atoms per monomer, slightly less active than wild-type
R260C
-
contains 2.0 iron atoms per monomer, slightly more active than wild-type
R260H
-
contains 1.3 iron atoms per monomer, slightly less active than wild-type
R260M
-
contains 1.1 iron atoms per monomer, about 30% of wild-type activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
production of biotin-rich feed and food additives using integration of BIO2 enzyme gene into chromosome under strong promoter for increased production of biotin
Show AA Sequence (7399 entries)
Longer loading times are possible. Please use the Sequence Search for a certain query.