Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(4S)-4-(hept-6-yn-1-yl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one + 9-(4-azidobutyl)-9H-purin-6-amine
(4S)-4-(5-[1-[4-(6-amino-9H-purin-9-yl)butyl]-1H-1,2,3-triazol-4-yl]pentyl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
i.e. reaction of acetylene derivative of biotin and an azide-functionalized adenine
-
-
?
(4S)-4-(hept-6-yn-1-yl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one + N-(3-azidopropyl)-7-nitro-2,1,3-benzoxadiazol-4-amine
(4S)-4-[5-(1-[3-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]propyl]-1H-1,2,3-triazol-4-yl)pentyl]tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
i.e. reaction of acetylene derivative of biotin and an azide-functionalied analogue of the fluorophore nitrobenzofurazan
-
-
?
ATP + biotin + AccB-86
AMP + diphosphate + biotinylated AccB-86
ATP + biotin + apo-[acetyl CoA carboxylase]
AMP + diphosphate + acetyl CoA carboxylase
no coupling is observed in ATP and biotin binding to the BPL
-
-
?
ATP + biotin + apo-[acetyl-CoA carbon-dioxide ligase]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase]
ATP + biotin + apo-[acetyl-CoA carboxylase 1]
AMP + diphosphate + acetyl-CoA carboxylase 1
-
cytoplasmic acetyl-CoA carboxylase isozyme
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
ATP + biotin + apo-[biotin carboxyl carrier protein]
AMP + diphosphate + biotin carboxyl carrier protein
-
i.e. BCCP, substrate is the recombinantly expressed His-tagged biotinoyl domain, BCCP87, of Escherichia coli BCCP, binding pattern, overview
-
-
?
ATP + biotin + apo-[biotin carboxyl carrier protein]
AMP + diphosphate + biotinylated biotin carboxyl carrier protein
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + propionyl-CoA carboxylase
-
-
-
-
?
ATP + biotin + apocarboxylase
AMP + diphosphate + holocarboxylase
-
-
-
-
?
ATP + biotin + Avi-tagged thioredoxin
?
ATP + biotin + BLAP
AMP + diphosphate + biotinylated BLAP
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 + C-terminal domain of apo-biotin carboxyl carrier protein
AMP + diphosphate + biotinylated C-terminal domain of apo-biotin carboxyl carrier protein
Mycobacterium tuberculosis BPL specifically biotinylates the homologous BCCP domain BCCP87, but not the Escherichia coli domain BCCP87
-
-
?
ATP + biotin + carboxyl carrier protein
?
-
the biotinylated product, holo biotin carboxyl carrier protein, forms a stable complex with the enzyme, which barely dissociates at room temperature
-
-
?
ATP + biotin + CGGGSGGGSGLNDIFEAQKIEWH
AMP + diphosphate + biotinylated CGGGSGGGSGLNDIFEAQKIEWH
-
-
-
-
?
ATP + biotin + chimeric protein of glutathione S-transferase and green fluorescence protein with biotin carboxyl carrier proteinDelta100
?
-
-
-
-
?
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 + PyC-77
AMP + diphosphate + biotinylated PyC-77
ATP + biotin + yeast acceptor peptide
?
-
-
-
-
?
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 + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein mutant S136M]-biotinyllysine
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
ATP + cis-propargyl biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + cis-propargyl bioti-containing [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + cis-propargyl biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + cis-propargyl biotin-containing [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + desthiobiotin + CGGGSGGGSGLNDIFEAQKIEWH
AMP + diphosphate + desthiobiotinylated CGGGSGGGSGLNDIFEAQKIEWH
-
-
-
-
?
ATP + desthiobiotin azide + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + desthiobiotin azide-containing [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
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
biotinyl-5'-AMP + diphosphate
-
first half-reaction of BPL
-
-
?
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
biotinyl-5'-AMP + apocarboxylase
holocarboxylase + AMP
D-biotin + ATP
biotinyl-5'-AMP + diphosphate
-
first half-reaction of BPL
-
-
?
additional information
?
-
ATP + biotin + AccB-86
AMP + diphosphate + biotinylated AccB-86
AccB, i.e. acetyl-CoA carboxylase biotin carboxyl carrier protein biotin attachment domain
-
-
?
ATP + biotin + AccB-86
AMP + diphosphate + biotinylated AccB-86
AccB, i.e. acetyl-CoA carboxylase biotin carboxyl carrier protein biotin attachment domain
-
-
?
ATP + biotin + apo-[acetyl-CoA carbon-dioxide ligase]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA carbon-dioxide ligase]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
-
mitochondrial acetyl-CoA carboxylase isozyme
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
-
i.e. ACC2, substrate is the recombinantly expressed His-tagged biotinoyl domain, ACC75, of ACC2, comprising residues 891-965. hHCS recognizes the MKM motif, NMR binding study, binding pattern, overview
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
-
i.e. ACC2, substrate is the recombinantly expressed His-tagged biotinoyl domain, ACC75, of ACC2. The apo-biotinoyl domain is biotinylated at Lys929 to form the holoprotein
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
-
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
biotin binding structure with importance of arginine 40 in the glycine-rich motif in the specificity of the biotinylation reaction. The Arg40 residue from the conserved GXGRXG motif interacts with the carboxyl group of biotin and stabilizes the alpha- and beta-phosphates of the nucleotide, overview. Presence of biotin is not required for ATP binding to the wild-type enzyme in the absence of Mg2+, the binding of biotin and ATP occurs via a random but cooperative process
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
-
-
-
-
?
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)]
-
BPL is an essential enzyme responsible for the activation of biotin-dependent enzymes through the covalent attachment of biotin
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
determination of the biotin domains of acetyl-CoA carboxylase, ACC
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
determination of the biotin domains of the pyruvate carboxylase, PC, of the organism, substrate is peptide fragment CaPC115 as GST-tagged recombinant protein, overview
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
BPL is an essential enzyme responsible for the activation of biotin-dependent enzymes through the covalent attachment of biotin
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
determination of the biotin domains of acetyl-CoA carboxylase, ACC
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
determination of the biotin domains of the pyruvate carboxylase, PC, of the organism, substrate is peptide fragment CaPC115 as GST-tagged recombinant protein, overview
-
-
?
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)]
-
-
-
-
?
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
-
-
?
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)]
-
incorporation of biotin into apo-carboxyl carrier protein, a subunit of acetyl-CoA carboxylase from E. coli
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
activation by biotinylation, HCS is the enzyme responsible for specifically attaching biotin onto the mammalian biotin domains. Biotinylation is catalysed through a two-step reaction where biotin is first activated to biotinyl-5'-AMP in an ATP-dependent manner, the biotin is then transferred onto the epsilon-amino group of a specific target lysine residue. 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)]
-
activation by biotinylation. The biotinylated lysine itself is located in a hairpin turn between beta-strands 4 and 5 in the centre of the polypeptide, present in a Met-Lys-Met motif that is essentially invariant in all biotin domains. HCS may well contain proofreading activity to select appropriate substrates
-
-
?
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)]
-
biotinylation site determination, overview
-
-
?
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)]
-
biotinylation site determination, overview
-
-
?
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)]
-
overall reaction
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
overall reaction, BPL catalyses transfer of biotin to an epsilon-amino group of a specific lysine residue, which is usually the 35th amino acid from C-terminal of apoBCCP and converts it to active holoBCCP which promotes fatty acid initiation and elongation
-
-
?
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)]
-
biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
structure-function relationship, modelling, overview
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase
-
-
?
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)]
-
structure-function relationship, modelling, overview
-
-
?
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)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
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)]
-
-
-
-
?
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-[biotin carboxyl carrier protein]
AMP + diphosphate + biotinylated biotin carboxyl carrier protein
-
-
-
?
ATP + biotin + apo-[biotin carboxyl carrier protein]
AMP + diphosphate + biotinylated biotin carboxyl carrier protein
-
-
-
?
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 + 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 + BLAP
AMP + diphosphate + biotinylated BLAP
BLAP, i.e. biotin/lipoyl attachment protein
-
-
?
ATP + biotin + BLAP
AMP + diphosphate + biotinylated BLAP
BLAP, i.e. biotin/lipoyl attachment protein
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + PyC-77
AMP + diphosphate + biotinylated PyC-77
Pyc-77, i.e. pyruvate carboxylase biotin attachment domain
-
-
?
ATP + biotin + PyC-77
AMP + diphosphate + biotinylated PyC-77
Pyc-77, i.e. pyruvate carboxylase biotin attachment domain
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein mutant S136M]-biotinyllysine
biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. BCCP 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 + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein mutant S136M]-biotinyllysine
the enzyme from Sulfolobus tokodaii cannot use wild-type biotin carboxyl carrier protein from Escherichia coli as a substrate
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein mutant S136M]-biotinyllysine
the enzyme from Sulfolobus tokodaii cannot use wild-type biotin carboxyl carrier protein from Escherichia coli as a substrate
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein mutant S136M]-biotinyllysine
biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. BCCP 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 + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. BCCP 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 + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
the enzyme from Sulfolobus tokodaii cannot use wild-type biotin carboxyl carrier protein from Escherichia coli as a substrate
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
the enzyme from Sulfolobus tokodaii cannot use wild-type biotin carboxyl carrier protein from Escherichia coli as a substrate
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. BCCP 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
-
-
?
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
-
-
?
biotinyl-5'-AMP + apocarboxylase
holocarboxylase + AMP
-
second half-reaction of BPL, the apocarboxylase is the biotin-carboxyl-carrier protein, which is carboxylated after biotin binding by the biotin carboxylase, BCCP, EC 6.3.4.14
-
-
?
biotinyl-5'-AMP + apocarboxylase
holocarboxylase + AMP
-
second half-reaction of BPL, the apocarboxylase is the biotin-carboxyl-carrier protein, which is carboxylated after biotin binding by the biotin carboxylase, EC 6.3.4.14
-
-
?
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
-
-
?
additional information
?
-
-
no activity with protein p67
-
-
?
additional information
?
-
-
acetyl-CoA carboxylase-1 and -2 perform the essential role of converting acetyl CoA to malonyl CoA, the first committed step in fatty acid synthesis, required for membrane biogenesis. The enzyme exists either as catalytic homodimers or associated with more highly active filamentous fibres. Development of an assay method using apo-pyruvate carboxylase partially purified from the livers of biotin-deficient rats for detection of biotin in fibroblast samples from healthy persons and patients with multiple carboxylase deficiency
-
-
?
additional information
?
-
-
protein-protein interaction between BPL and biotin-dependent enzymes is highly conserved. substrate recognition by BPLs occurs through conserved structural cues that govern the specificity of biotinylation, molecular modelling, overview. The region between Leu166 and Arg290 of BPL is required for catalysis. Development of an assay method using apo-pyruvate carboxylase partially purified from the livers of biotin-deficient rats for detection of biotin in samples from healthy persons and patients with multiple carboxylase deficiency
-
-
?
additional information
?
-
-
although mammals have multiple biotin-dependent enzymes there is only a single gene encoding holocarboxylase synthetase, HCS, responsible for all cellular biotinylation. The enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
-
-
?
additional information
?
-
-
holocarboxylase synthetase catalyzes the attachment of biotin to the epsilon-amino group of a specific lysine residue in apocarboxylases, biotinylation of biotin-dependent carboxylases requires ATP and proceeds in the following two steps
-
-
?
additional information
?
-
-
the enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
-
-
?
additional information
?
-
-
the 4'-hydroxyazobenzene-2-carboxylic acid dye assay can be used to quantify biotin
-
-
?
additional information
?
-
-
the N-terminal domain of hHCS recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain
-
-
?
additional information
?
-
biotin-dependent acetyl-CoA carboxylases/transcarboxylases are a class of enzymes that, in addition to fatty-acid biosynthesis, are important for gluconeogenesis as well as propionate catabolism
-
-
?
additional information
?
-
-
biotin-dependent acetyl-CoA carboxylases/transcarboxylases are a class of enzymes that, in addition to fatty-acid biosynthesis, are important for gluconeogenesis as well as propionate catabolism
-
-
?
additional information
?
-
enzyme is not able to biotinylate Schatz' minimal peptide GLNDIFEAQKIEWH
-
-
?
additional information
?
-
-
structural features influencing the reaction mechanism, overview
-
-
?
additional information
?
-
-
structural features influencing the reaction mechanism, overview
-
-
?
additional information
?
-
-
biotin protein ligase from Staphylococcus aureus catalyses the biotinylation of acetyl-CoA carboxylase and pyruvate carboxylase
-
-
?
additional information
?
-
-
biotin protein ligase is a bifunctional protein, possessing both biotin ligase and transcription repressor activities
-
-
?
additional information
?
-
-
biotin protein ligase is a bifunctional protein, possessing both biotin ligase and transcription repressor activities
-
-
?
additional information
?
-
-
SH2 domain-based tyrosine kinase assay using biotin ligase modified with a terbium(III) complex. An SH2 domain from lymphocyte-specific tyrosine kinase is genetically fused to a truncated biotin carboxyl carrier protein, and the resulting fusion protein is labeled through biotinylation with biotin protein ligase carrying multiple copies of a luminescent Tb3+ complex. The labeled SH2 fusion proteins are employed to detect a phosphorylated peptide immobilized on the surface of the microtiter plate, where the phosphorylated peptide is produced by phosphorylation to the substrate peptide by Src tyrosine kinase. The assay allows for a reliable determination of the activity of Src kinase lower than 10 ng/mL
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + biotin + apo-[acetyl-CoA carboxylase 1]
AMP + diphosphate + acetyl-CoA carboxylase 1
-
cytoplasmic acetyl-CoA carboxylase isozyme
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
-
mitochondrial acetyl-CoA carboxylase isozyme
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
ATP + biotin + apocarboxylase
AMP + diphosphate + holocarboxylase
-
-
-
-
?
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
-
-
?
biotin + ATP
biotinyl-5'-AMP + diphosphate
-
first half-reaction of BPL
-
-
?
biotinyl-5'-AMP + apocarboxylase
holocarboxylase + AMP
-
second half-reaction of BPL, the apocarboxylase is the biotin-carboxyl-carrier protein, which is carboxylated after biotin binding by the biotin carboxylase, BCCP, EC 6.3.4.14
-
-
?
additional information
?
-
ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
-
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
-
-
-
-
?
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)]
-
BPL is an essential enzyme responsible for the activation of biotin-dependent enzymes through the covalent attachment of biotin
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
BPL is an essential enzyme responsible for the activation of biotin-dependent enzymes through the covalent attachment of biotin
-
-
?
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)]
-
-
-
-
?
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)]
-
activation by biotinylation, HCS is the enzyme responsible for specifically attaching biotin onto the mammalian biotin domains. Biotinylation is catalysed through a two-step reaction where biotin is first activated to biotinyl-5'-AMP in an ATP-dependent manner, the biotin is then transferred onto the epsilon-amino group of a specific target lysine residue. 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)]
-
-
-
-
?
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)]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
overall reaction, BPL catalyses transfer of biotin to an epsilon-amino group of a specific lysine residue, which is usually the 35th amino acid from C-terminal of apoBCCP and converts it to active holoBCCP which promotes fatty acid initiation and elongation
-
-
?
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)]
-
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)]
-
-
-
-
?
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)]
-
-
-
-
?
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
?
-
-
acetyl-CoA carboxylase-1 and -2 perform the essential role of converting acetyl CoA to malonyl CoA, the first committed step in fatty acid synthesis, required for membrane biogenesis. The enzyme exists either as catalytic homodimers or associated with more highly active filamentous fibres. Development of an assay method using apo-pyruvate carboxylase partially purified from the livers of biotin-deficient rats for detection of biotin in fibroblast samples from healthy persons and patients with multiple carboxylase deficiency
-
-
?
additional information
?
-
-
although mammals have multiple biotin-dependent enzymes there is only a single gene encoding holocarboxylase synthetase, HCS, responsible for all cellular biotinylation. The enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
-
-
?
additional information
?
-
-
holocarboxylase synthetase catalyzes the attachment of biotin to the epsilon-amino group of a specific lysine residue in apocarboxylases, biotinylation of biotin-dependent carboxylases requires ATP and proceeds in the following two steps
-
-
?
additional information
?
-
-
the enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
-
-
?
additional information
?
-
biotin-dependent acetyl-CoA carboxylases/transcarboxylases are a class of enzymes that, in addition to fatty-acid biosynthesis, are important for gluconeogenesis as well as propionate catabolism
-
-
?
additional information
?
-
-
biotin-dependent acetyl-CoA carboxylases/transcarboxylases are a class of enzymes that, in addition to fatty-acid biosynthesis, are important for gluconeogenesis as well as propionate catabolism
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2'R,6'S)-9-[6'-([[N-(D-biotinoyl)sulfamoyl]oxy]methyl)morpholin-2'-yl]adenine
nucleoside-based inhibitor, KD value 0.324 nM
(3aS,4S,6aR)-4-(5-[1-[3-(naphthalen-2-yloxy)propyl]-1H-1,2,3-triazol-4-yl]pentyl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
-
(3aS,4S,6aR)-4-(5-[1-[4-(naphthalen-1-yloxy)butyl]-1H-1,2,3-triazol-4-yl]pentyl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
-
(3aS,4S,6aR)-4-(5-[1-[4-(naphthalen-2-yloxy)butyl]-1H-1,2,3-triazol-4-yl]pentyl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
-
(3aS,4S,6aR)-4-[-[1-[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl]triazol-4-yl]pentyl]-1,3,3a,4,6,6ahexahydrothieno[3,4-d]imidazol-2-one
-
competitive inhibitor
(3aS,4S,6aR)-4-[4-[1-[[(3aR,4R,6R,6aR)-4-(6-aminopurin-9-yl)-2,2-dimethyl-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3]dioxol-6-yl]methyl]triazol-4-yl]butyl]-1,3,3a,4,6,6a-hexa hydrothieno[3,4-d]imidazol-2-one
-
-
(3aS,4S,6aR)-4-[5-[1-(4-phenoxybutyl)-1H-1,2,3-triazol-4-yl]pentyl]tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
-
(3aS,4S,6aR)-4-[5-[1-[[(3aR,4R,6R,6aR)-4-(6-aminopurin-9-yl)-2,2-dimethyl-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3]dioxol-6-yl]methyl]triazol-4-yl]pentyl]-1,3,3a,4,6,6a-hexa hydrothieno[3,4-d]imidazol-2-one
-
-
(3aS,4S,6aR)-4-[5-[3-[[(3aR,4R,6R,6aR)-4-(6-aminopurin-9-yl)-2,2-dimethyl-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3]dioxol-6-yl]methyl]triazol-4-yl]pentyl]-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-2-one
-
-
(3aS,4S,6aR)-4-[6-[1-[[(3aR,4R,6R,6aR)-4-(6-aminopurin-9-yl)-2,2-dimethyl-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3]dioxol-6-yl]methyl]triazol-4-yl]hexyl]-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-2-one
-
-
2'-amino-5'-[N-(D-biotinoyl)sulfamoyl]amino-3',5'-dideoxyadenosine
nucleoside-based inhibitor, KD value 0.627 nM
2-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)ethyl 2,2-dimethylpropanoate
-
-
3-(2-oxo-1,3-benzoxazol-3(2H)-yl)-N-phenylpropanamide
-
inhibitor identified by molecular docking, glide score -7.49, glide energy -40.64 kcal/mol
5-chloro-3-[4-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)butyl]-1,3-benzoxazol-2(3H)-one
-
not inhibitory to human enzyme at 0.08 mM
5-methyl-3-[3-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)propyl]-1,3-benzoxazol-2(3H)-one
-
-
5-methyl-3-[4-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)butyl]-1,3-benzoxazol-2(3H)-one
9-[2'-azido-5'-O-[N-(D-biotinoyl)sulfamoyl]-2'-deoxy-beta-D-arabinofuranosyl]adenine
nucleoside-based inhibitor, KD value 0.027 nM. Strongest binding inhibitor in series
biotin acetylene
-
i.e. (3aS,4S,6aR)-4-hept-6-ynyl-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-2-one
biotinyl-5'-AMP
-
selective inhibitor
diphosphate
-
endproduct inhibition
GLNDIFEAQKIEWH
-
i.e. Schatz' peptide, synthetic biotinable minimal peptide, competitively inhibits self-biotinylation
glycerol
-
inhibits the recombinant enzyme at 10%
MgAMP
-
endproduct inhibition, mechanism of inhibition, overview
N-(2-methylphenyl)-2-(2-oxo-1,3-benzoxazol-3(2H)-yl)acetamide
-
inhibitor identified by molecular docking, glide score -7.34, glide energy -37.68 kcal/mol
NaCl
-
inhibits the purified enzyme at 0.1 M, but not the immobilized enzyme in crude extract of recombinant yeast cells
5-methyl-3-[4-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)butyl]-1,3-benzoxazol-2(3H)-one
-
competitive inhibitor versus biotin
5-methyl-3-[4-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)butyl]-1,3-benzoxazol-2(3H)-one
-
not inhibitory to human enzyme at 0.08 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
R40G
site-directed mutagenesis, the structure of the mutant enzyme in both the ligand-free and biotin-bound forms reveals that the mutated loop has collapsed, thus hindering ATP binding. The mutant is catalytically active but shows poor substrate specificity. The affinity for biotin is reduced 3.5fold by the R40G mutation, but binding of ATP to mutant R40G is very weak in the absence or in the presence of biotin. Comparison to the equivalent mutant of Escherichia coli BirA, overview
DELTA1-81
elimination of N-terminal domain plus part of the central domain, loss of ligase activity
DELTA2-63
elimination of N-terminal domain, mutant shows normal ligase activity
DELTA2-65
elimination of N-terminal domain, mutant shows normal ligase activity
DELTA1-81
-
elimination of N-terminal domain plus part of the central domain, loss of ligase activity
-
DELTA2-63
-
elimination of N-terminal domain, mutant shows normal ligase activity
-
DELTA2-65
-
elimination of N-terminal domain, mutant shows normal ligase activity
-
I11V/P85S/ M157T/K163E/I224T
-
17fold increase in the ability to use desthiobiotin as a substrate
I272X
-
site-directed mutagenesis
K122E
-
site-directed mutagenesis
K277E
-
site-directed mutagenesis
K283E
-
site-directed mutagenesis
K321E
-
site-directed mutagenesis
L237P
the mutant shows reduced catalytic activity compared to the wild-type enzyme
M157T
-
2-3fold increase in kcat value for desthiobiotin as a substrate
Q41R/M157T/I224T/E215D/T225A
-
10fold increase in the ability to use desthiobiotin as a substrate
R182E
-
site-directed mutagenesis
R212E
-
site-directed mutagenesis
R213E
-
site-directed mutagenesis
R317E
-
site-directed mutagenesis
D571N
-
naturally occuring mutation, important in positioning K579 in the AMP binding site
D615Y
-
naturally occuring mutation in the loop between alpha3 and beta6 that cover AMP, may coordinate oxygens of the AMP phosphate
D634Y
-
naturally occuring mutation of a solvent exposed residue, distal to active site on alpha4 and alpha5, respectively
D715G
-
naturally occuring mutation on beta9, may be involved in capping and stabilising the catalytic domain structure
G518E
-
naturally occuring mutation close to the active site and part of the ligand-binding loop, the mutation may not allow as much flexibility of this loop. As part of the hydrophobic pocket, making this polar residue would perturb biotin binding
G581S
-
naturally occuring mutation of a residue involved in hydrophobic interactions with biotin in the binding pocket
G582R
-
naturally occuring mutation of a residue involved in hydrophobic interactions with biotin in the binding pocket
L470S
-
naturally occuring mutation in an unstructured loop distal to the ligand-binding site
R508W/N511K
-
naturally occuring mutation of a residue critical in loop covering the ligand-binding site. R508 co-ordinates to the backbone carbonyl N712 to form a salt bridge, removing this would result in a more flexible loop, analogous to EcBPL R118 and R121 that co-ordinate oxygens within the AMP phosphate group
T462I
-
naturally occuring mutation in an unstructured loop distal to the ligand-binding site
V547G
-
naturally occuring mutation of a buried hydrophobic residue in alpha2 that reside near the AMP-binding beta5 strand
V550M
-
naturally occuring mutation of a buried hydrophobic residue in alpha2 that reside near the AMP-binding beta5 strand
Y456C
-
naturally occuring mutation in an unstructured loop distal to the ligand-binding site
R69A
the binding constant for biotin is nearly the same as that observed for the wild type protein. Mutant does not undergo self-botinylation
R48A/K111A
-
site-directed mutagenesis, comparison of the nucleotide binding mode in the double mutant to that in the wild-type enzyme, the active site loop Gly45-Trp53 is disordered in the mutant. Interface charge distribution in the double mutant complex, overview
R48K
-
site-directed mutagenesis, comparison of the nucleotide binding mode in the mutant to that in the wild-type enzyme, the active site loop Gly45-Trp53 is disordered in the mutant
R48A/K111A
-
site-directed mutagenesis, comparison of the nucleotide binding mode in the double mutant to that in the wild-type enzyme, the active site loop Gly45-Trp53 is disordered in the mutant. Interface charge distribution in the double mutant complex, overview
-
R48K
-
site-directed mutagenesis, comparison of the nucleotide binding mode in the mutant to that in the wild-type enzyme, the active site loop Gly45-Trp53 is disordered in the mutant
-
DELTA1-81
elimination of N-terminal domain plus part of the central domain, complete loss of ligase activity
DELTA2-65
elimination of N-terminal domain, complete loss of ligase activity
DELTA2-74
elimination of N-terminal domain plus part of the central domain, complete loss of ligase activity
F123G
-
the mutation has minimal effect upon the Km value for MgATP and biotin. In contrast, the kcat for biotin and MgATP are significantly compromised to about 10% that of wild type enzyme
F123R
-
the mutation has minimal effect upon the Km value for MgATP and biotin. In contrast, the kcat for biotin and MgATP are significantly compromised to about 10% that of wild type enzyme
R125A
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R125N
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R125A
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
R125N
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
F123G
-
the mutation has minimal effect upon the Km value for MgATP and biotin. In contrast, the kcat for biotin and MgATP are significantly compromised to about 10% that of wild type enzyme
-
F123R
-
the mutation has minimal effect upon the Km value for MgATP and biotin. In contrast, the kcat for biotin and MgATP are significantly compromised to about 10% that of wild type enzyme
-
DELTA1-81
-
elimination of N-terminal domain plus part of the central domain, complete loss of ligase activity
-
DELTA2-65
-
elimination of N-terminal domain, complete loss of ligase activity
-
DELTA2-74
-
elimination of N-terminal domain plus part of the central domain, complete loss of ligase activity
-
G115S
-
site-directed mutagenesis
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
R118G
-
mutant shows enhanced self and promiscuous biotinylation
A43G
catalytic efficiency is 2fold lower than catalytic efficiency of wild-type enzyme
A43G
-
catalytic efficiency is 2fold lower than catalytic efficiency of wild-type enzyme
-
additional information
-
disruption of BPL affects important metabolic pathways such as fatty acid biosynthesis and gluconeogenesis
additional information
-
disruption of BPL affects important metabolic pathways such as fatty acid biosynthesis and gluconeogenesis
-
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
additional information
-
HCS mutants with deletions up to Ala235 or Thr266 still show catalytic activity and can complement an enzyme-deficient Escherichia coli birA- strain. Enzyme deficiency can cause symptoms like ketoacidosis, feeding difficulties, hypotonia, seizures, developmental delay and dermal abnormalities such as rashes, dryness of the skin and alopecia, multiple carboxylase deficiency is caused by a lack of activity of the biotin-dependent enzymes, phenotypes, overview. Molecular modelling of mutations causing HCS deficiency, detailed overview
additional information
-
construction of biotinylated magnetic nanoparticles, with or without introduced strepatavidin, by displaying biotin acceptor peptide or biotin carboxyl carrier protein, BCCP, on the surface of bacterial magnetic particles for analysis of in vitro biotinylation, method development and evaluation, overview
additional information
-
construction of biotinylated magnetic nanoparticles, with or without introduced strepatavidin, by displaying biotin acceptor peptide or biotin carboxyl carrier protein, BCCP, on the surface of bacterial magnetic particles for analysis of in vitro biotinylation, method development and evaluation, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Dupuis, L.; Leon-del Rio, A.; Leclerc, D.; Campeau, E.; Sweetman, L.; Saudubray, J.M.; Herman, G.; Gibson, K.M.; Gravel, R.A.
Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency
Hum. Mol. Genet.
5
1011-1016
1996
Homo sapiens
brenda
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
brenda
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
brenda
Mishina, M.; Roggenkamp, R.; Schweizer, E.
Yeast mutants defective in acetyl-coenzyme A carboxylase and biotin:apocarboxylase ligase
Eur. J. Biochem.
111
79-87
1980
Saccharomyces cerevisiae, Rattus norvegicus
brenda
Landman, A.D.; Desjardins, P.R.; Dakshinamurti, K.
A simple assay for acetyl-CoA holocarboxylase synthetase
Can. J. Biochem.
54
813-815
1976
Rattus norvegicus
brenda
Landman, A.D.; Dakshinamurti, K.
Enzymatic diagnosis of holocarboxylase synthetase deficiency using apo-carboxyl carrier protein as a substrate
Clin. Chim. Acta
251
41-52
1996
Homo sapiens
brenda
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
brenda
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
brenda
Bagautdinov, B.; Kuroishi, C.; Sugahara, M.; Kunishima, N.
Purification, crystallization and preliminary crystallographic analysis of the biotin-protein ligase from Pyrococcus horikoshii OT3
Acta Crystallogr. Sect. F
61
193-195
2005
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
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
brenda
Bagautdinov, B.; Kuroishi, C.; Sugahara, M.; Kunishima, N.
Crystal structures of biotin protein ligase from Pyrococcus horikoshii OT3 and its complexes: structural basis of biotin activation
J. Mol. Biol.
353
322-333
2005
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
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
brenda
Bagautdinov, B.; Matsuura, Y.; Bagautdinova, S.; Kunishima, N.
Crystallization and preliminary X-ray crystallographic studies of the biotin carboxyl carrier protein and biotin protein ligase complex from Pyrococcus horikoshii OT3
Acta Crystallogr. Sect. F
63
334-337
2007
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Sueda, S.; Li, Y.Q.; Kondo, H.; Kawarabayasi, Y.
Substrate specificity of archaeon Sulfolobus tokodaii biotin protein ligase
Biochem. Biophys. Res. Commun.
344
155-159
2006
Sulfurisphaera tokodaii (F9VNG7), Sulfurisphaera tokodaii 7 (F9VNG7)
brenda
Streaker, E.D.; Beckett, D.
The biotin regulatory system: kinetic control of a transcriptional switch
Biochemistry
45
6417-6425
2006
Escherichia coli
brenda
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
brenda
Gralla, M.; Camporeale, G.; Zempleni, J.
Holocarboxylase synthetase regulates expression of biotin transporters by chromatin remodeling events at the SMVT locus
J. Nutr. Biochem.
19
400-408
2008
Homo sapiens
brenda
Bennett, C.B.; Westmoreland, T.J.; Verrier, C.S.; Blanchette, C.A.; Sabin, T.L.; Phatnani, H.P.; Mishina, Y.V.; Huper, G.; Selim, A.L.; Madison, E.R.; Bailey, D.D.; Falae, A.I.; Galli, A.; Olson, J.A.; Greenleaf, A.L.; Marks, J.R.
Yeast screens identify the RNA polymerase II CTD and SPT5 as relevant targets of BRCA1 interaction
PLoS ONE
3
e1448
2008
Mycobacterium tuberculosis
brenda
Gupta, V.; Gupta, R.K.; Khare, G.; Surolia, A.; Salunke, D.M.; Tyagi, A.K.
Crystallization and preliminary X-ray diffraction analysis of biotin acetyl-CoA carboxylase ligase (BirA) from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
64
524-527
2008
Mycobacterium tuberculosis (P96884), Mycobacterium tuberculosis
brenda
Pendini, N.R.; Polyak, S.W.; Booker, G.W.; Wallace, J.C.; Wilce, M.C.
Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus
Acta Crystallogr. Sect. F
F64
520-523
2008
Staphylococcus aureus
brenda
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
brenda
Maeda, Y.; Yoshino, T.; Takahashi, M.; Ginya, H.; Asahina, J.; Tajima, H.; Matsunaga, T.
Noncovalent immobilization of streptavidin on in vitro- and in vivo-biotinylated bacterial magnetic particles
Appl. Environ. Microbiol.
74
5139-5145
2008
Magnetospirillum magneticum, Magnetospirillum magneticum AMB-1
brenda
Pendini, N.R.; Bailey, L.M.; Booker, G.W.; Wilce, M.C.; Wallace, J.C.; Polyak, S.W.
Biotin protein ligase from Candida albicans: expression, purification and development of a novel assay
Arch. Biochem. Biophys.
479
163-169
2008
Candida albicans, Candida albicans CBF562
brenda
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
Saccharomyces cerevisiae, Homo sapiens, Pyrococcus horikoshii, Escherichia coli (P06709), Pyrococcus horikoshii OT-3
brenda
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
brenda
Bagautdinov, B.; Matsuura, Y.; Bagautdinova, S.; Kunishima, N.
Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrate
J. Biol. Chem.
283
14739-14750
2008
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
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
brenda
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
brenda
Verhaegen, M.; Christopoulos, T.
Recombinant Gaussia luciferase: Overexpression, purification, and analytical application of a bioluminescent reporter for DNA hybridization
Anal. Chem.
74
4378-4385
2002
Escherichia coli K-12 (P06709)
brenda
Bailey, L.M.; Wallace, J.C.; Polyak, S.W.
Holocarboxylase synthetase: correlation of protein localisation with biological function
Arch. Biochem. Biophys.
496
45-52
2010
Homo sapiens
brenda
Lee, C.K.; Cheong, C.; Jeon, Y.H.
Substrate recognition characteristics of human holocarboxylase synthetase for biotin ligation
Biochem. Biophys. Res. Commun.
391
455-460
2010
Homo sapiens
brenda
Zempleni, J.; Wijeratne, S.S.; Hassan, Y.I.
Biotin
Biofactors
35
36-46
2009
Homo sapiens
brenda
Yokoi, K.; Ito, T.; Maeda, Y.; Nakajima, Y.; Kurono, Y.; Sugiyama, N.; Togari, H.
A case of holocarboxylase synthetase deficiency with insufficient response to prenatal biotin therapy
Brain Dev.
31
775-778
2009
Homo sapiens
brenda
Lee, C.K.; Cheong, C.; Jeon, Y.H.
The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein
FEBS Lett.
584
675-680
2010
Homo sapiens
brenda
Tron, C.M.; McNae, I.W.; Nutley, M.; Clarke, D.J.; Cooper, A.; Walkinshaw, M.D.; Baxter, R.L.; Campopiano, D.J.
Structural and functional studies of the biotin protein ligase from Aquifex aeolicus reveal a critical role for a conserved residue in target specificity
J. Mol. Biol.
387
129-146
2009
Aquifex aeolicus (O66837), Aquifex aeolicus
brenda
Wijeratne, S.S.; Camporeale, G.; Zempleni, J.
K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts
J. Nutr. Biochem.
21
310-316
2010
Homo sapiens
brenda
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
brenda
Daniels, K.; Beckett, D.
Biochemical properties and biological function of a monofunctional microbial biotin protein ligase
Biochemistry
49
5358-5365
2010
Pyrococcus horikoshii (O57883)
brenda
Delli-Bovi, T.; Spalding, M.; Prigge, S.
Overexpression of biotin synthase and biotin ligase is required for efficient generation of sulfur-35 labeled biotin in E. coli
BMC Biotechnol.
10
73
2010
Plasmodium falciparum (C6S3D7), Plasmodium falciparum
brenda
Gupta, V.; Gupta, R.; Khare, G.; Salunke, D.; Surolia, A.; Tyagi, A.
Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration
PLoS ONE
5
e9222
2010
Mycobacterium tuberculosis (P96884), Mycobacterium tuberculosis
brenda
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)
brenda
Sueda, S.; Tanaka, H.; Yamagishi, M.
A biotin-based protein tagging system
Anal. Biochem.
393
189-195
2009
Sulfurisphaera tokodaii
brenda
Sueda, S.; Shinboku, Y.; Kusaba, T.
An SH2 domain-based tyrosine kinase assay using biotin ligase modified with a terbium(III) complex
Anal. Sci.
29
491-497
2013
Sulfurisphaera tokodaii
brenda
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)
brenda
Peters-Wendisch, P.; Stansen, K.C.; Goetker, S.; Wendisch, V.F.
Biotin protein ligase from Corynebacterium glutamicum: role for growth and L: -lysine production
Appl. Microbiol. Biotechnol.
93
2493-2502
2012
Corynebacterium glutamicum (Q8NSG6), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q8NSG6)
brenda
Soares da Costa, T.P.; Tieu, W.; Yap, M.Y.; Pendini, N.R.; Polyak, S.W.; Sejer Pedersen, D.; Morona, R.; Turnidge, J.D.; Wallace, J.C.; Wilce, M.C.; Booker, G.W.; Abell, A.D.
Selective inhibition of biotin protein ligase from Staphylococcus aureus
J. Biol. Chem.
287
17823-17832
2012
Staphylococcus aureus, Staphylococcus aureus ECT-2
brenda
Soares da Costa, T.P.; Yap, M.Y.; Perugini, M.A.; Wallace, J.C.; Abell, A.D.; Wilce, M.C.; Polyak, S.W.; Booker, G.W.
Dual roles of F123 in protein homodimerization and inhibitor binding to biotin protein ligase from Staphylococcus aureus
Mol. Microbiol.
91
110-120
2014
Staphylococcus aureus, Staphylococcus aureus ECT-R2
brenda
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
brenda
Pendini, N.R.; Yap, M.Y.; Traore, D.A.; Polyak, S.W.; Cowieson, N.P.; Abell, A.; Booker, G.W.; Wallace, J.C.; Wilce, J.A.; Wilce, M.C.
Structural characterization of Staphylococcus aureus biotin protein ligase and interaction partners: an antibiotic target
Protein Sci.
22
762-773
2013
Staphylococcus aureus, Staphylococcus aureus ECT-R2
brenda
Chen, X.; Chou, H.H.; Wurtele, E.S.
Holocarboxylase synthetase 1 physically interacts with histone H3 in Arabidopsis
Scientifica
2013
983501
2013
Arabidopsis thaliana
brenda
Miyao, H.; Ikeda, Y.; Shiraishi, A.; Kawakami, Y.; Sueda, S.
Immobilization of immunoglobulin-G-binding domain of Protein A on a gold surface modified with biotin ligase
Anal. Biochem.
484
113-121
2015
Sulfurisphaera tokodaii (F9VNG7), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (F9VNG7)
brenda
Tieu, W.; Jarrad, A.M.; Paparella, A.S.; Keeling, K.A.; Soares da Costa, T.P.; Wallace, J.C.; Booker, G.W.; Polyak, S.W.; Abell, A.D.
Heterocyclic acyl-phosphate bioisostere-based inhibitors of Staphylococcus aureus biotin protein ligase
Bioorg. Med. Chem. Lett.
24
4689-4693
2014
Staphylococcus aureus
brenda
Lu, W.; Levy, M.; Kincaid, R.; Ellington, A.
Directed evolution of the substrate specificity of biotin ligase
Biotechnol. Bioeng.
111
1071-1081
2014
Escherichia coli
brenda
Wang, Z.; Moslehi-Jenabian, S.; Solem, C.; Jensen, P.
Increased expression of pyruvate carboxylase and biotin protein ligase increases lysine production in a biotin prototrophic Corynebacterium glutamicum strain
Eng. Life Sci.
15
73-82
2015
Bacillus subtilis, Bacillus subtilis 168
-
brenda
Sam, J.; Sharmila, J.
Molecular docking of benzoxazolone and its derivatives against Staphylococcus aureus biotin protein ligase
Int. J. Pharm. Sci. Rev. Res.
32
72-76
2015
Staphylococcus aureus
-
brenda
Bockman, M.R.; Kalinda, A.S.; Petrelli, R.; De la Mora-Rey, T.; Tiwari, D.; Liu, F.; Dawadi, S.; Nandakumar, M.; Rhee, K.Y.; Schnappinger, D.; Finzel, B.C.; Aldrich, C.C.
Targeting Mycobacterium tuberculosis biotin protein ligase (MtBPL) with nucleoside-based bisubstrate adenylation inhibitors
J. Med. Chem.
58
7349-7369
2015
Mycobacterium tuberculosis (I6YFP0), Mycobacterium tuberculosis H37Rv (I6YFP0)
brenda
Feng, Y.; Chin, C.; Chakravartty, V.; Gao, R.; Crispell, E.; Weiss, D.; Cronan, J.
The atypical occurrence of two biotin protein ligases in Francisella novicida is due to distinct roles in virulence and biotin metabolism
mBio
6
e00591
2015
Francisella tularensis subsp. novicida
brenda
Bond, T.E.H.; Sorenson, A.E.; Schaeffer, P.M.
A green fluorescent protein-based assay for high-throughput ligand-binding studies of a mycobacterial biotin protein ligase
Microbiol. Res.
205
35-39
2017
Mycobacterium tuberculosis (P96884), Mycobacterium tuberculosis CDC 1551 (P96884)
brenda
Henke, S.K.; Cronan, J.E.
The Staphylococcus aureus group II biotin protein ligase BirA is an effective regulator of biotin operon transcription and requires the DNA binding domain for full enzymatic activity
Mol. Microbiol.
102
417-429
2016
Staphylococcus aureus (A0A0H3KCT0), Staphylococcus aureus Newman (A0A0H3KCT0)
brenda
Henke, S.; Cronan, J.
Successful conversion of the Bacillus subtilis BirA group II biotin protein ligase into a group I ligase
PLoS ONE
9
e96757
2014
Bacillus subtilis (P0CI75), Bacillus subtilis 168 (P0CI75)
brenda
Ma, Q.; Akhter, Y.; Wilmanns, M.; Ehebauer, M.T.
Active site conformational changes upon reaction intermediate biotinyl-5-AMP binding in biotin protein ligase from Mycobacterium tuberculosis
Protein Sci.
23
932-939
2014
Mycobacterium tuberculosis (I6YFP0), Mycobacterium tuberculosis H37Rv (I6YFP0)
brenda
Paparella, A.; Feng, J.; Blanco-Rodriguez, B.; Feng, Z.; Phetsang, W.; Blaskovich, M.; Cooper, M.; Booker, G.; Polyak, S.; Abell, A.
A template guided approach to generating cell permeable inhibitors of Staphylococcus aureus biotin protein ligase
Tetrahedron
74
1175-1183
2017
Staphylococcus aureus
-
brenda