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Information on EC 6.3.4.15 - biotin-[biotin carboxyl-carrier protein] ligase and Organism(s) Escherichia coli and UniProt Accession P06709
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6.3.4.15 biotin-[biotin carboxyl-carrier protein] ligaseIUBMB Comments
The enzyme biotinylates a biotin carboxyl-carrier protein that is part of an acetyl-CoA carboxylase complex, enabling its subsequent carboxylation by EC 6.3.4.14, biotin carboxylase. The carboxyl group is eventually transferred to acetyl-CoA by EC 2.1.3.15, acetyl-CoA carboxytransferase. In some organisms the carrier protein is part of EC 6.4.1.2, acetyl-CoA carboxylase.
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Word Map
- 6.3.4.15
-
biotinylation
- streptavidin
-
bioid
-
proximity-dependent
- bap
- avidin
-
avitag
-
streptavidin-coated
-
biotin-dependent
- transcarboxylase
-
proximity-labeling
-
biotinyl-5\'-amp
- drug development
-
unbiotinylated
-
15-amino
-
biotin-streptavidin
- diagnostics
- analysis
- synthesis
- carboxylases
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
biotin ligase, bira protein, biotin-protein ligase, biotin holoenzyme synthetase, bacterial bira biotin ligase, biotin acetyl-coa carboxylase ligase, biotin:apocarboxylase ligase, holocarboxylase synthetase 1, group i biotin protein ligase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acetyl CoA holocarboxylase synthetase
-
-
-
-
Acetyl coenzyme A holocarboxylase synthetase
-
-
-
-
Biotin holoenzyme synthetase
-
-
-
-
biotin protein ligase
Biotin--protein ligase
-
-
-
-
Biotin-[acetyl coenzyme A carboxylase] synthetase
-
-
-
-
Biotin-[acetyl-CoA carboxylase] synthetase
-
-
-
-
Biotin:apocarboxylase ligase
-
-
-
-
BirA
BPL
HCS
Holocarboxylase synthetase
Synthetase, biotin-[acetyl coenzyme A carboxylase]
-
-
-
-
BirA
-
-
BirA
-
bifunctional protein, catalyzes post-translational biotin addition to a biotin-dependent carboxylase and binds sequence-specifically to DNA to repress transcription initiation at the biotin biosynthetic operon
HCS
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine
reaction mechanism, the first step is the reversible formation of a biotinyl-5'-AMP intermediate followed by irreversible transfer of the biotinyl group to the protein
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
biotin:apo-[carboxyl-carrier protein] ligase (AMP-forming)
The enzyme biotinylates a biotin carboxyl-carrier protein that is part of an acetyl-CoA carboxylase complex, enabling its subsequent carboxylation by EC 6.3.4.14, biotin carboxylase. The carboxyl group is eventually transferred to acetyl-CoA by EC 2.1.3.15, acetyl-CoA carboxytransferase. In some organisms the carrier protein is part of EC 6.4.1.2, acetyl-CoA carboxylase.
CAS REGISTRY NUMBER
COMMENTARY
37340-95-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
ATP + biotin + Avi-tagged thioredoxin
?
-
biotin ligase site-specifically biotinylates a lysine side chain within a 15-amino acid acceptor peptide (also known as Avi-tag)
-
-
?
ATP + biotin + C-terminal domain of apo-biotin carboxyl carrier protein
AMP + diphosphate + biotinylated C-terminal domain of acetyl CoA carboxylase
-
Escherichia coli BPL biotinylates both the homologous BCCP domain BCCP87 and the corresponding domain from Mycobacterium tuberculosis
-
-
?
ATP + biotin + CGGGSGGGSGLNDIFEAQKIEWH
AMP + diphosphate + biotinylated CGGGSGGGSGLNDIFEAQKIEWH
-
-
-
-
?
ATP + biotin + fluorescein-labeled peptide 85-11
ADP + diphosphate + biotinyl-fluorescein-labeled peptide 85-11
-
peptide 85-11 has the sequence MAGGLNDIFEAQKIEWHE with the lysine residue being targeted for biotinylation, development of a fluorescence polarization technology-based assay method, overview
-
-
?
ATP + biotin + GLNDIFEAQKIEWH
AMP + diphosphate + biotinylated GLNDIFEAQKIEWH
-
i.e. Schatz' peptide, synthetic biotinable minimal peptide
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine
AMP + diphosphate + [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine
-
ATP in form of MgATP2-
-
-
?
ATP + biotin + [Escherichia coli apo-biotin-carboxyl-carrier-protein mutant M136S]-L-lysine
AMP + diphosphate + [Escherichia coli biotin-carboxyl-carrier-protein mutant M136S]-biotinyl-L-lysine
-
biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. Biotin carboxyl carrier protein becomes an active substrate for carboxylation and carboxyl transfer, after biotinylation of its canonical lysine residue by biotin protein ligase (BPL). BCCP carries a characteristic local sequence surrounding the canonical lysine residue, typically -M-K-M-. Sulfolobus tokodaii is unique in that its biotin carboxyl carrier protein has serine replaced for the methionine C-terminal to the lysine. This biotin carboxyl carrier protein is biotinylated by its own biotin protein ligase, but not by Escherichia coli biotin protein ligase. Likewise, Escherichia coli biotin carboxyl carrier protein is not biotinylated by Sulfolobus tokodaii biotin protein ligase
-
-
?
ATP + biotin + [Escherichia coli apo-biotin-carboxyl-carrier-protein]-L-lysine
AMP + diphosphate + [Escherichia coli biotin-carboxyl-carrier-protein]-biotinyl-L-lysine
-
biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. Biotin carboxyl carrier protein becomes an active substrate for carboxylation and carboxyl transfer, after biotinylation of its canonical lysine residue by biotin protein ligase (BPL). BCCP carries a characteristic local sequence surrounding the canonical lysine residue, typically -M-K-M-. Sulfolobus tokodaii is unique in that its biotin carboxyl carrier protein has serine replaced for the methionine C-terminal to the lysine. This biotin carboxyl carrier protein is biotinylated by its own biotin protein ligase, but not by Escherichia coli biotin protein ligase. Likewise, Escherichia coli biotin carboxyl carrier protein is not biotinylated by Sulfolobus tokodaii biotin protein ligase
-
-
?
ATP + desthiobiotin + CGGGSGGGSGLNDIFEAQKIEWH
AMP + diphosphate + desthiobiotinylated CGGGSGGGSGLNDIFEAQKIEWH
-
-
-
-
?
avitag-tagged maltose-binding protein + biotin + ATP
maltose-binding protein-avitag-biotin + AMP + diphosphate
avitagged BirA + biotin + ATP
BirA-avitag-biotin + AMP + diphosphate
-
recombinant Saccharomyces cerevisiae cells
-
-
?
avitagged BirA + biotin + biotin + ATP
BirA-avitag-biotin + AMP + diphosphate
-
the recombinant avitagged enzyme biotinylates itself at the avitag sequence
-
-
?
biotin + ATP + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
catalyzes the covalent attachment of the biotin prosthetic group to a specific lysine of the biotin carboxyl carrier domain of biotin-dependent carboxylases in a two-step reaction
-
r
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
biotin protein ligase, BPL required to complete acetyl-CoA carboxylase's capability for fatty acid biosynthesis
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
the holo-enzyme is a multienzyme complex, in which biotin is bound to the biotin carboxyl carrier protein, binding structure, overview. All biotin-dependent enzymes utilise the enzyme-bound biotin group for the transfer of CO2 between metabolites
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
conformational changes occur upon biotin binding. Structure-function relationship, modelling, overview
-
-
?
avitag-tagged maltose-binding protein + biotin + ATP
maltose-binding protein-avitag-biotin + AMP + diphosphate
-
recombinant Saccharomyces cerevisiae cells
-
-
?
avitag-tagged maltose-binding protein + biotin + ATP
maltose-binding protein-avitag-biotin + AMP + diphosphate
-
recombinant avitag-tagged maltose-binding protein
-
-
?
additional information
?
-
-
evidence for a direct role of the biotin-[acetyl-CoA-carboxylase] ligase in repression of the biotin operon in Escherichia coli
-
-
?
additional information
?
-
-
also functions to repress the biotin biosynthetic operon and synthesizes its own corepressor, biotinyl-5'-AMP, the catalytic intermediate of the biotinylation reaction, catalyzes key reactions in essential metabolic processes, essential for survival
-
?
additional information
?
-
-
substrate specificities of wild-type enzyme and of mutant R118G, the first biotinylates only a single protein substrate, while the mutant shows a wider substrate spectrum
-
-
?
additional information
?
-
-
the enzyme site-specifically biotinylates proteins via a biotin acceptor peptide tag
-
-
?
additional information
?
-
-
does not use yeast acceptor peptide as a substrate
-
-
?
additional information
?
-
-
mammalian cell surface proteins tagged with a 15-amino acid peptide, i.e. the AP-tag, are specifically biotinylated by Escherichia coli biotin ligase BirA, whereas endogenous proteins are not modified, overview. BirA labels the AP-tag specifically in different cellular compartments: at the cell surface, in the endoplasmic reticulum, in the cytosol, and in the nucleus. BirA labeling may also be used in living animals, for example in a transgenic mouse expressing cytosolic BirA, overview
-
-
?
additional information
?
-
-
Escherichia coli enzyme undergoes self-biotinylation
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
avitag-tagged maltose-binding protein + biotin + ATP
maltose-binding protein-avitag-biotin + AMP + diphosphate
-
recombinant Saccharomyces cerevisiae cells
-
-
?
avitagged BirA + biotin + ATP
BirA-avitag-biotin + AMP + diphosphate
-
recombinant Saccharomyces cerevisiae cells
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
biotin protein ligase, BPL required to complete acetyl-CoA carboxylase's capability for fatty acid biosynthesis
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
the holo-enzyme is a multienzyme complex, in which biotin is bound to the biotin carboxyl carrier protein, binding structure, overview. All biotin-dependent enzymes utilise the enzyme-bound biotin group for the transfer of CO2 between metabolites
-
-
?
additional information
?
-
-
evidence for a direct role of the biotin-[acetyl-CoA-carboxylase] ligase in repression of the biotin operon in Escherichia coli
-
-
?
additional information
?
-
-
also functions to repress the biotin biosynthetic operon and synthesizes its own corepressor, biotinyl-5'-AMP, the catalytic intermediate of the biotinylation reaction, catalyzes key reactions in essential metabolic processes, essential for survival
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no activity with biotin analogues desthiobiotin azide, cis-propargyl biotin, trans-propargyl biotin, iminobiotin, diaminobiotin, nitrobenzoxadiazole gamma-butyric acid, iodouracil valeric acid, thiouracil valeric acid
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
GLNDIFEAQKIEWH
-
i.e. Schatz' peptide, synthetic biotinable minimal peptide, competitively inhibits self-biotinylation
NaCl
-
inhibits the purified enzyme at 0.1 M, but not the immobilized enzyme in crude extract of recombinant yeast cells
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.12
[Escherichia coli apo-biotin-carboxyl-carrier-protein mutant M136S]-L-lysine
-
pH 8.0, 37°C, wild type enzyme
-
0.011
[Escherichia coli apo-biotin-carboxyl-carrier-protein]-L-lysine
-
pH 8.0, 37°C, wild type enzyme
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.58
[Escherichia coli apo-biotin-carboxyl-carrier-protein mutant M136S]-L-lysine
-
pH 8.0, 37°C, wild type enzyme
-
0.165
[Escherichia coli apo-biotin-carboxyl-carrier-protein]-L-lysine
-
pH 8.0, 37°C, wild type enzyme
-
0.8
biotin
-
mutant K321E, wild-type BCCP biotin domain and mutant K283E, E147Kmutant BCCP biotin domain
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.49
[Escherichia coli apo-biotin-carboxyl-carrier-protein mutant M136S]-L-lysine
-
pH 8.0, 37°C, wild type enzyme
-
15
[Escherichia coli apo-biotin-carboxyl-carrier-protein]-L-lysine
-
pH 8.0, 37°C, wild type enzyme
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the immobilized enzyme is slightly less active than the soluble enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36
-
wild type enzyme and mutant enzymes birA311, birA825, birA301, and birA352
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
holo-BPL is protected from proteolysis by biotinyl-5'-AMP, an intermediate of the BPL-catalyzed reaction. Apo-MtBPL is completely digested by trypsin within 20 min of co-ncubation. Substrate selectivity and inability to promote self biotinylation are exquisite features of Mycobacterium tuberculosis BPL
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
EcBPL contains three distinct domains determined through X-ray crystallography. Monomeric and dimeric forms of the enzyme are involved in enzyme regulation, overview. Structure-function relationship, overview. EcBPL contains a DNA binding motif
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
EcBPL domains determination through X-ray crystallography at 2.3 A resolution, and determination of the crystal structure of EcBPL in complex with biotin
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G115S
I11V/P85S/ M157T/K163E/I224T
-
17fold increase in the ability to use desthiobiotin as a substrate
L237P
the mutant shows reduced catalytic activity compared to the wild-type enzyme
Q41R/M157T/I224T/E215D/T225A
-
10fold increase in the ability to use desthiobiotin as a substrate
R118G
additional information
G115S
-
site-directed mutagenesis, the mutant enzyme shows a highly increased rate of biotinyl-5'-AMP intermediate formation, but no release of the intermediate
R118G
-
site-directed mutagenesis, the mutant enzyme shows a wider substrate specificity compared to the wild-type enzyme, the mutant biotinylates bovine serum albumin, chloramphenicol acetyltransferase, immunoglobin heavy and light chains, and RNase A in vitro, it also self-biotinylates in vivo and in vitro, the activity depends on proximity, distance to the substrate can be bridged by a linker like avidin, overview
R118G
mutation of Arg118 to glycine in EcBPL causes altered affinity of BPL for biotin, increased dissociation rates for biotin and biotinyl-5'-AMP, and consequently, promiscuous biotinylation of inappropriate proteins
additional information
-
mammalian cell surface proteins tagged with a 15-amino acid peptide, i.e. the AP-tag, are specifically biotinylated by Escherichia coli biotin ligase BirA, whereas endogenous proteins are not modified, overview. BirA labels the AP-tag specifically in different cellular compartments: at the cell surface, in the endoplasmic reticulum, in the cytosol, and in the nucleus of mammalian cells, including human, mouse, rat and hamster cell lines, and primary neuron culture. BirA labeling may also be used in living animals, for example in a transgenic mouse expressing cytosolic BirA, overview. Benefit of streptavidin labeling over Ab labeling, method development, detailed overview
additional information
mutational analysis, overview. The C-terminal 87 amino acids of biotin carboxyl carrier protein, i.e. BCCP-87, are recognised and biotinylated by BPL as well as full-length BCCP due to the fact that this peptide adopts the tertiary structure that is required for the interaction with BPL
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
mutant enzymes birA707, birA361 and birA91 with strikingly altered thermosensitivity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, immobilized recombinant enzyme, PBS, completely stable for 4 weeks, loss of activity after 5 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography, Ni-NTA resin column chromatography, and Superdex 75 gel filtration
-
recombinant enzyme from Saccharomyces cerevisiae, immobilization of the recombinant enzyme
-
recombinant His-tagged wild-type and mutant enzymes from strain JM109 by nickel affinity chromatography
-
recombinant His6-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coding region of birA biotin-protein ligase gene cloned from genomic DNA by PCR, verfied by sequencing and expressed in mouse erythroleukemic cells
-
construction and expression of the C-terminal 87 amino acids of biotin carboxyl carrier protein, i.e. BCCP-87. cross-species activity of BPLs permitts functional cloning of the cDNA for yeast BPL through genetic complementation with a conditional lethal birA- strain of Escherichia coli
doxycycline-regulated expression of a secreted variant of Escherichia coli biotin ligase BirA with target proteins containing a 13-residue biotin acceptor peptide appended to their extracellular domain, co-expression with three different G-protein coupled receptors, i.e. protease-activated receptors 1 and 2, and the platelet ADP receptor, P2Y12, which become biotinylated, in CHO-K1 Tet-On cells on the cell surface, overview
-
expressed as thioredoxin- and maltose binding protein-fusion proteins in Escherichia coli BL21(DE3) cells
-
expression of BirA from pET-based vector pHBA in Escherichia coli BL21 (lambdaDE3)
-
gene birA, expression of His-tagged wild-type and mutant enzymes in strain JM109, expression of enzyme in strain BM4092 unbiotinylated form
-
gene birA, functional expression of N-terminally and C-terminally multiply tagged enzyme in Saccharomyces cerevisiae, low level expression of the surface-displayed enzyme, expression of avitagged-BirA in Saccharomyces cerevisiae, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
BirA can be useful for specific in vivo labeling of proteins in cell cultures by biotinylation
synthesis
synthesis
-
the enzyme is utilized to synthesize site-specific biotinylated proteins via a biotin acceptor peptide tag
synthesis
-
in vivo biotinylation of bacterial magnetic particles synthesized by Magnetospirillum magneticum AMB-1 by heterologous expression of Escherichia coli biotin ligase. To biotinylate bacterial magnetic particles in vivo, biotin acceptor peptide is fused to a bacterial magnetic particles surface protein, Mms13, and Escherichia coli biotin ligase is simultaneously expressed in the truncated form lacking the DNA-binding domain. The biotinylated biotin acceptor protein-displaying bacterial magnetic particles are then exposed to streptavidin by simple mixing. The streptavidin-binding capacity of bacterial magnetic particles biotinylated in vivo is 35fold greater than that of bacterial magnetic particles biotinylated in vitro
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barker, D.F.; Campbell, A.M.
The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase
J. Mol. Biol.
146
451-467
1981
Escherichia coli
Barker, D.F.; Campbell, A.M.
Genetic and biochemical characterization of the birA gene and its product: evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli
J. Mol. Biol.
146
469-492
1981
Escherichia coli
de Boer, E.; Rodriguez, P.; Bonte, E.; Krijgsveld, J.; Katsantoni, E.; Heck, A.; Grosveld, F.; Strouboulis, J.
Efficient biotinylation and single-step purification of tagged transcription factors in mammalian cells and transgenic mice
Proc. Natl. Acad. Sci. USA
100
7480-7485
2003
Escherichia coli
Chapman-Smith, A.; Mulhern, T.D.; Whelan, F.; Cronan, J.E., Jr.; Wallace, J.C.
The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity
Protein Sci.
10
2608-2617
2001
Escherichia coli
Parthasarathy, R.; Bajaj, J.; Boder, E.T.
An immobilized biotin ligase: surface display of Escherichia coli BirA on Saccharomyces cerevisiae
Biotechnol. Prog.
21
1627-1631
2005
Escherichia coli
Choi-Rhee, E.; Schulman, H.; Cronan, J.E.
Promiscuous protein biotinylation by Escherichia coli biotin protein ligase
Protein Sci.
13
3043-3050
2004
Escherichia coli
Streaker, E.D.; Beckett, D.
The biotin regulatory system: kinetic control of a transcriptional switch
Biochemistry
45
6417-6425
2006
Escherichia coli
Chen, I.; Choi, Y.A.; Ting, A.Y.
Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins
J. Am. Chem. Soc.
129
6619-6625
2007
Saccharomyces cerevisiae, Escherichia coli
Ng, B.; Polyak, S.W.; Bird, D.; Bailey, L.; Wallace, J.C.; Booker, G.W.
Escherichia coli biotin protein ligase: characterization and development of a high-throughput assay
Anal. Biochem.
376
131-136
2008
Escherichia coli
Pendini, N.R.; Bailey, L.M.; Booker, G.W.; Wilce, M.C.; Wallace, J.C.; Polyak, S.W.
Microbial biotin protein ligases aid in understanding holocarboxylase synthetase deficiency
Biochim. Biophys. Acta
1784
973-982
2008
Escherichia coli (P06709), Homo sapiens, Pyrococcus horikoshii, Pyrococcus horikoshii OT-3, Saccharomyces cerevisiae
Slavoff, S.A.; Chen, I.; Choi, Y.; Ting, A.Y.
Expanding the substrate tolerance of biotin ligase through exploration of enzymes from diverse species
J. Am. Chem. Soc.
130
1160-1162
2008
Bacillus subtilis, Leuconostoc mesenteroides, Saccharomyces cerevisiae, Escherichia coli, Giardia intestinalis, Homo sapiens, Methanocaldococcus jannaschii, Cutibacterium acnes, Pyrococcus horikoshii, Trypanosoma cruzi
Howarth, M.; Ting, A.Y.
Imaging proteins in live mammalian cells with biotin ligase and monovalent streptavidin
Nat. Protoc.
3
534-545
2008
Escherichia coli
Mize, G.J.; Harris, J.E.; Takayama, T.K.; Kulman, J.D.
Regulated expression of active biotinylated G-protein coupled receptors in mammalian cells
Protein Expr. Purif.
57
280-289
2008
Escherichia coli
Maeda, Y.; Yoshino, T.; Matsunaga, T.
In vivo biotinylation of bacterial magnetic particles by a truncated form of Escherichia coli biotin ligase and biotin acceptor peptide
Appl. Environ. Microbiol.
76
5785-5790
2010
Escherichia coli
Purushothaman, S.; Annamalai, K.; Tyagi, A.; Surolia, A.
Diversity in functional organization of class I and class II biotin protein ligase
PLoS ONE
6
e16850
2011
Escherichia coli, Mycobacterium tuberculosis (P96884)
Li, Y.Q.; Sueda, S.; Kondo, H.; Kawarabayasi, Y.
A unique biotin carboxyl carrier protein in archaeon Sulfolobus tokodaii
FEBS Lett.
580
1536-1540
2006
Escherichia coli, Sulfurisphaera tokodaii (F9VNG7), Sulfurisphaera tokodaii 7 (F9VNG7)
Li, Y.; Sousa, R.
Expression and purification of E. coli BirA biotin ligase for in vitro biotinylation
Protein Expr. Purif.
82
162-167
2012
Escherichia coli, Escherichia coli AVB101
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