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Information on EC 3.5.1.12 - biotinidase
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3.5.1.12 biotinidaseIUBMB Comments
Also acts on biotin esters.
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Word Map
- 3.5.1.12
- newborn
- children
- seizure
- infant
- urine
- holocarboxylase
-
inborn
- child
-
hearing
- acidosis
- alopecia
- phenylketonuria
- carboxylases
-
biotinylation
-
symptomatic
-
treatable
-
biotin-dependent
- ataxia
- hypotonia
- hypothyroidism
-
late-onset
- rash
- galactosemia
- acidurias
- avidin
- homocystinuria
-
maple
- acidemia
- medicine
- syrup
-
lipoylated
-
biotin-responsive
-
neurocutaneous
- lethargy
-
biotin-binding
- paraparesis
-
biotin-deficient
-
seborrheic
-
hyperammonemia
- 3-methylcrotonyl-coa
- diagnostics
- analysis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
biotinidase, lipoamidase, biotinyl-hydrolase, biocytin hydrolyzing amidase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amidohydrolase biotinidase
-
-
-
-
biotinidase
BTD
lipoamidase
lipolysine hydrolase
-
not yet given an EC number, seems to be identical with biotinidase
lipoyl-X-hydrolase
-
-
-
-
lipoamidase
-
not yet given an EC number, seems to be identical with biotinidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
biotin amide + H2O = biotin + NH3
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of amide bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
biotin-amide amidohydrolase
Also acts on biotin esters.
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CAS REGISTRY NUMBER
COMMENTARY
9025-15-4
-
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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
1'-N-methoxycarbonyl-biocytin + H2O
1-N-methoxycarbonyl-biotin + L-lysine
-
-
-
-
?
biotin amide + H2O
biotin + NH3
-
good substrate, Cys-245 is likely the active site cysteine, formation of a thioester intermediate between biotin and cysteine
-
-
?
biotinyl-monoiodotyramine + H2O
biotin + monoiodotyramine
-
radioactive assay for early diagnosis of biotinidase defiency in serum
-
-
?
N,N-(dipicolyl)biotinamido-Boc-lysine + H2O
N,N-(dipicolyl)biotinamine + Boc-L-lysine
-
-
-
-
?
N-(+)biotinyl-4-aminobenzoic acid + H2O
4-aminobenzoic acid + biotin
-
-
-
-
?
N-(1'-N-methoxycarbonyl-biotinyl)p-aminobenzoic acid + H2O
1-N-methoxycarbonyl-biotin + 4-aminobenzoic acid
-
-
-
-
?
N-DL-dethiobiotinyl-p-aminobenzoic acid + H2O
dethiobiotin + 4-aminobenzoic acid
-
-
-
-
?
2-(N-biotinyl)-amino-5-nitro-benzoic acid + H2O
biotin + 2-amino-5-nitrobenzoic acid
-
-
-
-
?
2-(N-biotinyl)-amino-5-nitro-benzoic acid + H2O
biotin + 2-amino-5-nitrobenzoic acid
-
-
-
-
?
3-(N-biotinyl)-amino-6-nitrobenzoic acid + H2O
biotin + 3-amino-6-nitrobenzoic acid
-
-
-
-
?
3-(N-biotinyl)-amino-6-nitrobenzoic acid + H2O
biotin + 3-amino-6-nitrobenzoic acid
-
-
-
-
?
biocytin + H2O
biotin + L-lysine
-
natural substrate, biotinidase is responsible for cleaving biocytin, thereby liberating and recycling biotin
-
-
?
biocytin + H2O
biotin + L-lysine
-
biotinylation of histones by biotinidase depends on the hydrolytic cleavage of biocytin (biotinyl-epsilon-lysine), coupled to the transfer of biotinyl residue to free amino groups in histones. K4, K9 and K18 in histone H3 are good targets for biotinylation, K14 and K23 are relatively poor targets
-
-
?
biocytin + H2O
biotin + L-lysine
-
i.e. biotin-epsilon-lysine. The enzyme is involved in modification of histones by covalent attachment of the vitamin biotin. A reaction mechanism is proposed by which cleavage of biocytin by biotinidase leads to the formation of a biotinyl-thioester intermediate (cysteine-bound biotin) at or near the active site of biotinidase. In the next step, the biotinyl moiety is transferred from the thioester to the epsilon-amino group of lysine in histones. Biotinidase may catalyze both biotinylation and debiotinylation of histones
-
-
?
biocytin + H2O
biotin + L-lysine
-
i.e. biotin-epsilon-lysine. Because polylysine is readily biotinylated by biotinidase in the presence of biocytin, whereas polyarginine is not biotinylated, the enzyme likely transfers biotin to the epsilon-amino group of lysyl residues
-
-
?
biocytin + H2O
biotin + L-lysine
-
the enzyme belongs to the nitrilase superfamily
-
-
?
biotin amide + H2O
?
-
-
171917, 171919, 171921, 171922, 171923, 171925, 171926, 171928, 171929, 171930, 171931, 171932, 171933, 171934, 171935, 171936
-
-
?
biotin amide + H2O
?
-
very short biotinyl peptides, enzyme is not active when biotin is attached to large native proteins, for example intact holocarboxylases
-
-
?
biotin amide + H2O
?
-
cleaves D-biotinylamides and esters, recycling of the vitamin
-
-
?
biotin amide + H2O
?
-
cleaves D-biotinylamides and esters, recycling of the vitamin
-
-
?
biotinyl-4-aminobenzoic acid + H2O
biotin + 4-aminobenzoic acid
-
-
-
-
?
biotinyl-4-aminobenzoic acid + H2O
biotin + 4-aminobenzoic acid
-
colorimetric synthetic substrate
-
-
?
biotinyl-6-aminoquinoline + H2O
biotin + 6-aminoquinoline
-
BAQ, fluorogenic substrate as assay for biotinidase
-
-
?
biotinyl-6-aminoquinoline + H2O
biotin + 6-aminoquinoline
Lacticaseibacillus casei Shirota
-
-
-
-
?
biotinyl-di-iodotyramine + H2O
biotin + di-iodotyramine
-
radioactive assay for early diagnosis of biotinidase defiency in serum
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
-
-
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
-
-
171917, 171919, 171920, 171921, 171922, 171923, 171924, 171925, 171926, 171927, 171928, 171929, 171930, 171931, 171932, 171933, 171934, 171935, 171936
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
-
-
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
-
-
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
biotin + L-lysine
-
-
-
-
ir
epsilon-N-biotinyl-L-lysine + H2O
biotin + L-lysine
-
-
-
-
ir
epsilon-N-biotinyl-L-lysine + H2O
biotin + L-lysine
-
-
171917, 171919, 171920, 171921, 171922, 171923, 171925, 171926, 171927, 171928, 171929, 171930, 171931, 171932, 171933, 171934, 171935, 171936
-
-
ir
epsilon-N-biotinyl-L-lysine + H2O
biotin + L-lysine
-
cannot cleave biocytin that is bound to avidin
-
-
ir
epsilon-N-biotinyl-L-lysine + H2O
biotin + L-lysine
-
-
-
-
ir
epsilon-N-biotinyl-L-lysine + H2O
biotin + L-lysine
-
-
-
-
ir
epsilon-N-biotinyl-L-lysine + H2O
biotin + L-lysine
-
-
-
-
ir
epsilon-N-biotinyl-L-lysine + H2O
biotin + L-lysine
-
biocytin, soluble bound biotin
-
-
ir
Met-enkephalin + H2O
?
-
suitable natural substrate for biotinidase
-
-
?
N-biotinyl-3-aminobenzoic acid + H2O
biotin + 3-aminobenzoic acid
-
-
-
-
?
N-biotinyl-3-aminobenzoic acid + H2O
biotin + 3-aminobenzoic acid
-
-
-
-
?
N-biotinyl-beta-alanine + H2O
biotin + beta-alanine
-
-
-
-
?
N-biotinyl-beta-alanine + H2O
biotin + beta-alanine
-
-
-
-
?
N-biotinyl-beta-alanine + H2O
biotin + beta-alanine
-
-
-
-
?
p-(N-biotinylamino)benzoic acid + H2O
biotin + p-aminobenzoic acid
-
-
-
-
ir
p-(N-biotinylamino)benzoic acid + H2O
biotin + p-aminobenzoic acid
-
-
-
-
ir
p-(N-biotinylamino)benzoic acid + H2O
biotin + p-aminobenzoic acid
-
PAB, artificial substrate
-
-
ir
p-(N-biotinylamino)benzoic acid + H2O
biotin + p-aminobenzoic acid
-
-
-
-
ir
p-(N-biotinylamino)benzoic acid + H2O
biotin + p-aminobenzoic acid
-
-
-
-
?
p-(N-biotinylamino)benzoic acid + H2O
biotin + p-aminobenzoic acid
-
-
-
-
ir
additional information
?
-
-
no hydrolysis of acetamide or p-nitroacetanilide
-
-
?
additional information
?
-
-
biotinidase is essential for recycling the vitamin biotin and for transferring biotin to proteins
-
-
?
additional information
?
-
-
enzymatic activity including biotinidase is not solely responsible for the biotin release from biotinylated IgGs. It is speculated that heat-stable, low-molecular-weight chemical factors present in plasma also catalyze hydrolysis of the amide bond to the carboxyl group of biotin
-
-
?
additional information
?
-
-
lysine residues K9 and K13 in N-terminus of human histones H2A and H2AX are targets for biotinylation. K125, K127 and K129 in the C-terminus of histone H2A are targets for biotinylation
-
-
?
additional information
?
-
biotinidase, an amidohydrolase, catalyzes the cleavage of biotin from biocytin or biotinylated peptides formed from proteolytic degradation of the holocarboxylases and other biotinylated proteins
-
-
?
additional information
?
-
-
biotinidase, an amidohydrolase, catalyzes the cleavage of biotin from biocytin or biotinylated peptides formed from proteolytic degradation of the holocarboxylases and other biotinylated proteins
-
-
?
additional information
?
-
-
biotinylamidopropyl-N,N-(dipicolyl)amine and N,N-(dipicolyl)biotinamine are resistant to biotinidase activity
-
-
?
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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
Met-enkephalin + H2O
?
-
suitable natural substrate for biotinidase
-
-
?
biocytin + H2O
biotin + L-lysine
-
natural substrate, biotinidase is responsible for cleaving biocytin, thereby liberating and recycling biotin
-
-
?
biocytin + H2O
biotin + L-lysine
-
biotinylation of histones by biotinidase depends on the hydrolytic cleavage of biocytin (biotinyl-epsilon-lysine), coupled to the transfer of biotinyl residue to free amino groups in histones. K4, K9 and K18 in histone H3 are good targets for biotinylation, K14 and K23 are relatively poor targets
-
-
?
biocytin + H2O
biotin + L-lysine
-
i.e. biotin-epsilon-lysine. The enzyme is involved in modification of histones by covalent attachment of the vitamin biotin. A reaction mechanism is proposed by which cleavage of biocytin by biotinidase leads to the formation of a biotinyl-thioester intermediate (cysteine-bound biotin) at or near the active site of biotinidase. In the next step, the biotinyl moiety is transferred from the thioester to the epsilon-amino group of lysine in histones. Biotinidase may catalyze both biotinylation and debiotinylation of histones
-
-
?
biotin amide + H2O
?
-
-
171917, 171919, 171921, 171922, 171923, 171925, 171926, 171928, 171929, 171930, 171931, 171932, 171933, 171934, 171935, 171936
-
-
?
biotin amide + H2O
?
-
very short biotinyl peptides, enzyme is not active when biotin is attached to large native proteins, for example intact holocarboxylases
-
-
?
biotin amide + H2O
?
-
cleaves D-biotinylamides and esters, recycling of the vitamin
-
-
?
biotin amide + H2O
?
-
cleaves D-biotinylamides and esters, recycling of the vitamin
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
-
-
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
-
-
171917, 171919, 171920, 171921, 171922, 171923, 171924, 171925, 171926, 171927, 171928, 171929, 171930, 171931, 171932, 171933, 171934, 171935, 171936
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
-
-
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
-
-
-
-
?
additional information
?
-
-
biotinidase is essential for recycling the vitamin biotin and for transferring biotin to proteins
-
-
?
additional information
?
-
-
enzymatic activity including biotinidase is not solely responsible for the biotin release from biotinylated IgGs. It is speculated that heat-stable, low-molecular-weight chemical factors present in plasma also catalyze hydrolysis of the amide bond to the carboxyl group of biotin
-
-
?
additional information
?
-
biotinidase, an amidohydrolase, catalyzes the cleavage of biotin from biocytin or biotinylated peptides formed from proteolytic degradation of the holocarboxylases and other biotinylated proteins
-
-
?
additional information
?
-
-
biotinidase, an amidohydrolase, catalyzes the cleavage of biotin from biocytin or biotinylated peptides formed from proteolytic degradation of the holocarboxylases and other biotinylated proteins
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
biotinyl-methyl 4-(amidomethyl)benzoate
-
competitive inhibitor, 80% inhibition at 1 mM
biotin
-
competitive inhibition at acidic pH, no inhibition at ph 7.4 with p-(N-biotinylamino)benzoic acid as substrate
biotin
-
competitive inhibition at acidic pH, no inhibition at ph 7.4 with p-(N-biotinylamino)benzoic acid as substrate
biotin
-
product inhibition, decreased by fucoidan in hepatocellular carcinoma, but increased in liver cirrhosis
biotin
-
competitive inhibition at acidic pH, no inhibition at ph 7.4 with p-(N-biotinylamino)benzoic acid as substrate
biotin
-
competitive inhibition at acidic pH, no inhibition at ph 7.4 with p-(N-biotinylamino)benzoic acid as substrate
p-hydroxymercuribenzoate
-
inhibits biotinidase hydrolase activity and biotinyl-transferase activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
enzyme kinetics in liver from hepatoma patients with additional hepatitis B or hepatitis C infection, or from patients with chronic active hepatitis or cirrhosis
-
0.00383
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from supernatant fraction
0.00556
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from membrane fraction
0.0167
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from membrane and supernatant fraction
0.75
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from upper labial skin, male rat
1.18
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from upper labial skin, female rat
1.71
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from bone marrow, male rat
1.82
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from lower labial skin, female rat
1.87
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from diaphragm, female rat
1.87
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from diaphragm, male rat
2.43
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from cerebrum, male rat
2.67
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from small intestine, female rat
2.97
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from cerebrum, female rat
3.36
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from stomach, male rat
3.69
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from lung, female rat
3.7 - 5
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from large intestine, female rat
3.87
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from pancreatic head, female rat
3.88
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from stomach (corpus), male rat
3.9
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from uterus, female rat
4.15
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from bone marrow, female rat
4.17
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from cerebellum, female rat
4.17
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from cerebellum, male rat
4.27
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from large intestine, male rat
4.39
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from cerebrum, male rat
4.39
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from pancreatic tail, female rat
4.63
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from cerebrum, female rat
4.77
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from lower labial skin, male rat
4.77
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from tigh muscle, male rat
5.41
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from spleen, female rat
5.45
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from ovary, female rat
5.81
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from small intestine (jejunum), male rat
6.17
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from testis, male rat
6.25
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from tigh muscle, female rat
6.76
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from liver, female rat
7.75
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from small intestine (duodenum), male rat
7.97
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from kidney, female rat
8.58
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from spleen, male rat
10.1
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from esophagus, female rat
10.1
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from esophagus, male rat
11
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from abdominal skin, female rat
11.6
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from stomach (pylori), female rat
11.6
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from stomach, male rat
11.9
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from abdominal skin, male rat
11.9
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from kidney, male rat
12.1
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from small intestine (ileum), male rat
19.2
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from pancreatic head, male rat
21.7
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from pancreatic tail, male rat
24.1
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from heart, female rat
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
a quantitative analytical method is developed for the determination of biotinidase activity in dried blood spot samples
additional information
-
a quantitative analytical method is developed for the determination of biotinidase activity in dried blood spot samples
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6
6 - 6.8
9.5
-
liver enzyme has 2 pH optima at pH 6.0 and pH 9.5 with lipoyl-p-aminobenzoic acid as substrate
6
-
enzyme from plasma, liver enzyme has 2 pH optima at pH 6.0 and pH 9.5 with lipoyl-p-aminobenzoic acid as substrate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Lactobacillus arabinosus
-
655310, 656803, 667185, 667540, 668553, 668880, 669965, 669967, 670277, 670282, 687001, 688567, 689004
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
analysis of gene expression in breast cancer plasma, diverse tissue samples, profiling, overview
brenda
enzyme expression analysis in 129 papillary thyroid cancers, 34 benign thyroid tissues and 43 FNA samples. The overall biotinidase expression is decreased in papillary thyroid cancers compared to benign nodules
brenda
-
serum, plasma, leukocytes
171919, 171920, 171921, 171922, 171923, 171924, 171925, 171927, 171928, 171929, 171930, 171931, 171933, 171935
brenda
-
increased plasma biotinidase activity in rats with paracetamol-induced acute liver injury. The increase may serve as an indicator of paracetamol-induced acute liver injury in the rat
brenda
BTD is synthesized by the liver and secreted into the circulation
brenda
-
from hepatoma patients with additional hepatitis B or hepatitis C infection, or from patients with chronic active hepatitis or cirrhosis
brenda
BTD is synthesized by the liver and secreted into the circulation
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
splice variants 1a and 1b localize to mitochondria and/or endoplasmic reticulum
brenda
additional information
-
biotinidase is directed to the secretory pathway and perhaps mitochondria
-
brenda
-
splice variants 1a and 1b localize to mitochondria and/or endoplasmic reticulum
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
BTD is responsible for recycling the vitamin biotin
malfunction
-
biotinidase deficiency is an autosomal recessive disorder of biotin metabolism that causes incomplete recycling of free biotin. The resulting depletion of intracellular biotin leads to impaired activities of biotin-dependent carboxylases. The ensuing clinical phenotype includes progressive neurologic deterioration with epileptic seizures, muscular hypotonia as well as skin eczema
malfunction
-
biotinidase deficiency, an autosomal recessively inherited disorder, is characterized by neurologic and cutaneous symptoms and can be detected by newborn screening
malfunction
BTD mutation leads to hepatic glycogen storage diseases, overview
malfunction
biotinidase deficiency (BTD) is an inherited disorder with severe clinical manifestations if not treated early
malfunction
biotinidase deficiency is an autosomal recessive disorder of biotin metabolism leading to varying degrees of neurologic and cutaneous symptoms when untreated, phenotypes, overview
malfunction
biotinidase deficiency is caused by enzyme mutations, correlation of phenotype and genotype, overview
malfunction
loss of overall biotinidase expression is associated with poor disease free survival in case of thyroid cancer, effect of subcellular compartmentalization of nuclear and cytoplasmic biotinidase on patient survival, correlation of biotinidase expression with clinico-pathological parameters of thyroid cancer patients, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BTD_BOVIN
525
0
58353
Swiss-Prot
Secretory Pathway (Reliability: 1)
BTD_HUMAN
543
0
61133
Swiss-Prot
Mitochondrion (Reliability: 4)
BTD_MOUSE
520
0
58154
Swiss-Prot
Secretory Pathway (Reliability: 2)
BTD_RAT
521
0
58021
Swiss-Prot
Secretory Pathway (Reliability: 1)
BTD_TAKRU
504
0
55552
Swiss-Prot
Secretory Pathway (Reliability: 1)
Q0P471_DANRE
520
1
57477
TrEMBL
Secretory Pathway (Reliability: 1)
A0A061ILN6_CRIGR
580
0
64437
TrEMBL
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
115000
66000 - 76000
68000
76000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A171T/D444H
C160Y
impaired biotinidase activity (activity in cells: 14%, activity in medium: 0.3%) and undetectable amount of protein in intra and extracellular space. Variant identified among Brazilian individuals showing low activity of biotinidase in serum
C186Y/D444H
naturally occuring mutation involved in biotinidase deficiency
C458fs/H323R
naturally occuring mutation involved in biotinidase deficiency, no phenotype
D228G/D444H
naturally occuring mutation involved in biotinidase deficiency, no phenotype
D444H
D444H/Q456H
naturally occuring mutation involved in biotinidase deficiency
D444H/T532M
naturally occuring mutation involved in biotinidase deficiency
G34D/G114V
-
naturally occuring mutation in a Spanish patient with enzyme deficiency
L40P
impaired biotinidase activity (activity in cells: 33%, activity in medium: 7%) and undetectable amount of protein in intra and extracellular space. Variant identified among Brazilian individuals showing low activity of biotinidase in serum
L446P
impaired biotinidase activity (activity in cells: 0%, activity in medium: 2%) and undetectable amount of protein in intra and extracellular space. Variant identified among Brazilian individuals showing low activity of biotinidase in serum
L71P
-
naturally occuring mutation, with additional frameshift mutation in this mutant, in an Indian patient with enzyme deficiency
M86R/Q456H
naturally occuring mutation involved in biotinidase deficiency, no phenotype
N300H/D444H
naturally occuring mutation involved in biotinidase deficiency, no phenotype
P187S
-
naturally occuring mutation in an Austrian patient with enzyme deficiency
Q456H
R157H/D444H
naturally occuring mutation involved in biotinidase deficiency
R209H
naturally occuring mutation involved in biotinidase deficiency, no phenotype
R209H/Q456H
naturally occuring mutation involved in biotinidase deficiency, no phenotype
R538C
T152R/D444H
naturally occuring mutation involved in biotinidase deficiency, no phenotype
T234I
naturally occuring mutation involved in biotinidase deficiency, no phenotype
T234I/D444H
naturally occuring mutation involved in biotinidase deficiency, no phenotype
Y425Ter
-
naturally occuring mutation, with additional frameshift mutation in this mutant, in several Austrian patients with enzyme deficiency
additional information
A171T/D444H
-
naturally occuring mutation involved in BTD deficiency in Hungarian patients
D444H
-
naturally occuring mutation involved in BTD deficiency in Hungarian patients
D444H
naturally occuring mutation of BTD in patients with hepatic glycogen storage disease, GSD-Ia, the mutant shows normal enzyme activity compared to wild-type
D444H
naturally occuring homozygous mutation involved in biotinidase deficiency
D444H
naturally occuring mutation involved in biotinidase deficiency, the mutant enzyme shows 50% reduced activity compaerd to the wild-type enzyme, with phenotype
D444H
expression of the variant results in detectable protein and slightly reduced activity in cells (activity in cells: 46%; activity in medium: 115%)
Q456H
-
naturally occuring mutation involved in BTD deficiency in Hungarian patients
R538C
-
naturally occuring mutation involved in BTD deficiency in Hungarian patients
R538C
-
naturally occuring mutation, with additional frameshift mutation in this mutant, in a Spanish patient with enzyme deficiency
additional information
-
naturally occuring missense mutations resulting in profound biotinidase deficiency
additional information
-
c.98_104del7 insTCC is a naturally occuring truncation mutation involved in BTD deficiency
additional information
-
identification of several frameshift mutations, overview
additional information
correlation of biotinidase expression with clinico-pathological parameters of thyroid cancer patients, overview
additional information
-
correlation of biotinidase expression with clinico-pathological parameters of thyroid cancer patients, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 70
60 - 70
-
15 min 60°C 60% activity lost, 70°C activity completely lost
60 - 70
-
stable up to 60°C, stable 30 min at 60°C, at 70°C activity decreases after 10 min to 20-50% of the initial value
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
15°C enzyme solution with toluene, for a week or more without appreciable loss of activity
-
4°C, 0.1 M phosphate buffer pH 6.0, 1 mM 2-mercaptoethanol, 1 mM EDTA, 1 month without loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, genotyping in patients from Austria, India, Morocco, and Spain with enzyme deficiency
-
enzyme expression and immunohistochemic analysis in 169 different samples of thyroid cancer, overview
genotyping of biotinidase deficiency algerian patient genes, PCR, mutation analysis reveals three mutations, c.del631C and c.1557T>G within exon 4 and c.324-325insTA in exon 3
genotyping of biotinidase deficiency american patient genes, quantitative real-time reverse-transcription PCR, most mutations in exon 4, overview
genotyping of Hungarian population, the most common biotinidase variant alleles are higher in the Hungarian population than in other Caucasian populations
-
PCR amplification mutational hotspot in biotinidase gene identified, causes biotinidase deficiency, located on chromosome 3p25
-
the variants Leu40Pro, Cys160Tyr, Asp222Asn, Asp444His, Leu446Pro, Asn489Ser and the wild type gene are expressed in HEK 293 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Cr(VI) causes downregulation at the transcriptional level by modification of histone acetylation
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
identification of the site of carboxylation of the biotinyl prosthetic group of several biotin enzymes
diagnostics
medicine
diagnostics
BTD is a biomarker for the hepatic glycogen storage disease, overview
diagnostics
BTD is a potential serological biomarker for the detection of breast cancer to use with plasma
diagnostics
loss of overall biotinidase expression is a marker for papillary thyroid cancer aggressiveness acting as a predictor of disease progression and prognosis
medicine
-
plasma biotinidase activity assay for diagnosis and screen newborn infants for biotinidase deficiency, treatment of inborn metabolism errors with large doses of biotin
medicine
-
naturally occuring missense mutations result in biotinidase deficiency, an autosomal recessively inherited disorder in which affected individuals have multiple carboxylase deficiency due to secondary deficiency of free biotin
medicine
-
thirteen novel mutations in children with biotinidase deficiency. Biotinidase deficiency is a defect in the recycling of the vitamin biotin. Biotin supplementation can markedly improve the neurological and cutaneous symptoms of affected children and prevents symptoms in children identified by newborn screening or treated since birth
medicine
-
serum biotinidase is a sensitive and specific biochemical marker of hepatic dysfunction
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thoma, R.W.; Peterson, W.H.
The enzymatic degradation of soluble bound biotin
J. Biol. Chem.
210
569-579
1954
Gallus sp., no activity in Lactobacillus arabinosus, Sus scrofa
brenda
Knappe, J.; Bruemer, W.; Biederbick, K.
Reinigung und Eigenschaften der Biotinidase aus Schweinenieren und Lactobacillus casei
Biochem. Z.
338
599-613
1963
Enterococcus faecalis, Homo sapiens, Lacticaseibacillus casei, no activity in Achromobacter sp., no activity in Lactobacillus arabinosus, Rattus rattus, Sus scrofa
-
brenda
Moss, J.; Lane, M.D.
The biotin-dependent enzymes
Adv. Enzymol. Relat. Areas Mol. Biol.
35
321-442
1971
Enterococcus faecalis, Lacticaseibacillus casei, Sus scrofa
brenda
Wastell, H.; Dale, G.; Bartlett, K.
A sensitive fluorimetric rate assay for biotinidase using a new derivative of biotin, biotynyl-6-aminoquinoline
Anal. Biochem.
140
69-73
1984
Homo sapiens, Sus scrofa
brenda
Craft, D.V.; Goss, N.H.; Chandramouli, N.; Wood, H.G.
Purification of biotinidase from human plasma and its activity on biotinyl peptides
Biochemistry
24
2471-2476
1985
Enterococcus faecalis, Homo sapiens
brenda
Ebrahim, H.; Dakshinamurti, K.
A fluorometric assay for biotinidase
Anal. Biochem.
154
282-286
1986
Homo sapiens, no activity in Lactobacillus arabinosus
brenda
Chauhan, J.; Dakshinamurti, K.
Purification and characterization of human serum biotinidase
J. Biol. Chem.
261
4268-4275
1986
Enterococcus faecalis, Homo sapiens, Rattus rattus, Sus scrofa
brenda
Hayakawa, K.; Oizumi, J.
Determination of biotinidase activity by liquid chromatography with fluorometric detection
J. Chromatogr.
383
148-152
1986
Homo sapiens
brenda
Wolf, B.; Hymes, J.; Heard, G.S.
Biotinidase
Methods Enzymol.
184
103-111
1990
Enterococcus faecalis, Homo sapiens, Lacticaseibacillus casei, Rattus rattus, Sus scrofa
brenda
Garganta, C.L.; Wolf, B.
Lipoamidase activity in human serum is due to biotinidase
Clin. Chim. Acta
189
313-326
1990
Homo sapiens
brenda
Oizumi, J.; Hayakawa, K.
Biotinidase in the porcine cerebrum
Arch. Biochem. Biophys.
278
381-385
1990
Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Rattus rattus, Sus scrofa
brenda
Hart, P.S.; Hymes, J.; Wolf, B.
Isoforms of human serum biotinidase
Clin. Chim. Acta
197
257-264
1991
Homo sapiens
brenda
Oizumi, J.; Hayakawa, K.
Enkephalin hydrolysis by human serum biotinidase
Biochim. Biophys. Acta
1074
433-438
1991
Homo sapiens, Sus scrofa
brenda
Oizumi, J.; Hayakawa, K.
Biocytin-specific 110-kDa biotinidase from human serum
Clin. Chim. Acta
215
63-71
1993
Homo sapiens
brenda
Evangelatos, S.A.; Kakabakos, S.E.; Evangelatos, G.P.; Ithakissios, D.S.
Determination of serum biotinidase activity with biotinyl derivatives of iodotyramines as substrates
J. Pharm. Sci.
82
1228-1231
1993
Homo sapiens
brenda
Nilsson, L.; Kagedal, B.
Co-purification of human serum lipoamidase and biotinidase:evidence that the two enzyme activities are due to the same enzyme protein
Biochem. J.
291
545-551
1993
Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Rattus rattus
brenda
Cole, H.; Reynolds, T.R.; Lockyer, J.M.; Buck, G.A.; Denson, T.; Spence, E.J.; Hymes, J.; Wolf, B.
Human serum biotinidase cDNA cloning, sequence and characterization
J. Biol. Chem.
269
6566-6570
1994
Homo sapiens
brenda
Nilsson, L.; Kagedal, B.
Lipoamidase and biotinidase activities in the rat: Tissue distribution and intracellular localization
Eur. J. Clin. Chem. Clin. Biochem.
32
501-509
1994
Cavia porcellus, Homo sapiens, Rattus rattus
brenda
Pomponio,R.J.; Reynolds, T.R.; Cole, H.; Buck, G.A.; Wolf, B.
Mutational hotspot in the human biotinidase gene causes profound biotinidase deficiency
Nature Genet.
11
96-98
1995
Homo sapiens
brenda
Hymes, J.; Fleischhauer, K.; Wolf, B.
Biotinidase in serum and tissues
Methods Enzymol.
279
422-435
1997
Homo sapiens, Rattus rattus, Sus scrofa
brenda
Livaniou, E.; Kakabakos, S.E.; Evangelatos, S.A.; Evangelatos, G.P.; Ithakissios, D.
Determination of serum biotinidase activity with radioiodinated biotinylamide analogs
Methods Enzymol.
279
442-451
1997
Homo sapiens
brenda
Brenner, C.
Catalysis in the nitrilase superfamily
Curr. Opin. Struct. Biol.
12
775-782
2002
Homo sapiens
brenda
Swango, K.L.; Hymes, J.; Brown, P.; Wolf, B.
Amino acid homologies between human biotinidase and bacterial aliphatic amidases: putative identification of the active site of biotinidase
Mol. Genet. Metab.
69
111-115
2000
Homo sapiens
brenda
Bogusiewicz, A.; Mock, N.I.; Mock, D.M.
Release of biotin from biotinylated proteins occurs enzymatically and nonenzymatically in human plasma
Anal. Biochem.
331
260-266
2004
Homo sapiens
brenda
Hymes, J.; Fleischauer, K.; Wolf, B.
Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency
Biochem. Mol. Med.
56
76-83
1995
Homo sapiens
brenda
James, S.; Maresca, K.P.; Allis, D.G.; Valliant, J.F.; Eckelman, W.; Babich, J.W.; Zubieta, J.
Extension of the single amino acid chelate concept (SAAC) to bifunctional biotin analogues for complexation of the M(CO)3(+1) Core (M = Tc and Re): syntheses, characterization, biotinidase stability, and avidin binding
Bioconjug. Chem.
17
579-589
2006
Mus musculus
brenda
Abraham, P.
Increased plasma biotinidase activity in rats with paracetamol-induced acute liver injury
Clin. Chim. Acta
349
61-65
2004
Rattus norvegicus
brenda
Kobza, K.; Camporeale, G.; Rueckert, B.; Kueh, A.; Griffin, J.B.; Sarath, G.; Zempleni, J.
K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase
FEBS J.
272
4249-4259
2005
Homo sapiens
brenda
Wolf, B.; Jensen, K.P.; Barshop, B.; Blitzer, M.; Carlson, M.; Goudie, D.R.; Gokcay, G.H.; Demirkol, M.; Baykal, T.; Demir, F.; Quary, S.; Shih, L.Y.; Pedro, H.F.; Chen, T.H.; Slonim, A.E.
Biotinidase deficiency: novel mutations and their biochemical and clinical correlates
Hum. Mutat.
25
413
2005
Homo sapiens
brenda
Hayakawa, K.; Guo, L.; Terentyeva, E.A.; Li, X.K.; Kimura, H.; Hirano, M.; Yoshikawa, K.; Nagamine, T.; Katsumata, N.; Ogata, T.; Tanaka, T.
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and Lactobacillus casei (Shirota)
J. Chromatogr. B
844
240-250
2006
Lacticaseibacillus casei, Mus musculus, Rattus norvegicus, Lacticaseibacillus casei Shirota
brenda
Kothapalli, N.; Camporeale, G.; Kueh, A.; Chew, Y.C.; Oomme, A.M.; Griffin, J.B.; Zempleni, J.
Biological functions of biotinylated histones
J. Nutr. Biochem.
16
446-448
2005
Homo sapiens
brenda
Chew, Y.C.; Camporeale, G.; Kothapalli, N.; Sarath, G.; Zempleni, J.
Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase
J. Nutr. Biochem.
17
225-233
2006
Homo sapiens
brenda
Stanley, C.M.; Hymes, J.; Wolf, B.
Identification of alternatively spliced human biotinidase mRNAs and putative localization of endogenous biotinidase
Mol. Genet. Metab.
81
300-312
2004
Homo sapiens
brenda
Wolf, B.; Jensen, K.
Evolutionary conservation of biotinidase: implications for the enzymes structure and subcellular localization
Mol. Genet. Metab.
86
44-50
2005
Homo sapiens
brenda
Korkmazer, N.; Vurucu, S.; Demirkaya, E.; Unay, B.; Kul, M.; Akin, R.; Gokcay, E.
Serum and liver tissue biotinidase enzyme activity in rats which were administrated to valproic acid
Brain Dev.
28
515-520
2006
Rattus norvegicus
brenda
Faith, M.; Eapen, C.E.; Wilfred, G.; Ramachandran, J.; Jacob, M.
Serum biotinidase is a sensitive and specific biochemical marker of hepatic dysfunction: A preliminary report
Hepatol. Res.
37
13-17
2007
Homo sapiens
brenda
Kobza, K.A.; Chaiseeda, K.; Sarath, G.; Takacs, J.M.; Zempleni, J.
Biotinyl-methyl 4-(amidomethyl)benzoate is a competitive inhibitor of human biotinidase
J. Nutr. Biochem.
19
826-832
2008
Homo sapiens
brenda
Milankovics, I.; Kamory, E.; Csokay, B.; Fodor, F.; Somogyi, C.; Schuler, A.
Mutations causing biotinidase deficiency in children ascertained by newborn screening in Western Hungary
Mol. Genet. Metab.
90
345-348
2007
Homo sapiens
brenda
Pindolia, K.; Jensen, K.; Wolf, B.
Three dimensional structure of human biotinidase: computer modeling and functional correlations
Mol. Genet. Metab.
92
13-22
2007
Homo sapiens (P43251), Homo sapiens
brenda
Vlachos, G.D.; Schulpis, K.H.; Papakonstantinou, E.; Papadakis, M.; Elefsiniotis, I.; Papassotiriou, I.; Antsaklis, A.
Maternal chronic hepatitis B virus does not affect neonatal biotinidase activity
Acta Paediatr.
97
362-365
2008
Homo sapiens
brenda
Arslan, M.; Vurucu, S.; Balamtekin, N.; Unay, B.; Akin, R.; Kurt, I.; Ozcan, O.
The effects of biotin supplementation on serum and liver tissue biotinidase enzyme activity and alopecia in rats which were administrated to valproic acid
Brain Dev.
31
405-410
2009
Rattus norvegicus
brenda
Yilmaz, Y.; Tasdemir, H.A.; Paksu, M.S.
The influence of valproic acid treatment on hair and serum zinc levels and serum biotinidase activity
Eur. J. Paediatr. Neurol.
13
439-443
2009
Homo sapiens
brenda
Perez-Monjaras, A.; Cervantes-Roldan, R.; Meneses-Morales, I.; Gravel, R.A.; Reyes-Carmona, S.; Solorzano-Vargas, S.; Gonzalez-Noriega, A.; Leon-Del-Rio, A.
Impaired biotinidase activity disrupts holocarboxylase synthetase expression in late onset multiple carboxylase deficiency
J. Biol. Chem.
283
34150-34158
2008
Homo sapiens
brenda
Hayakawa, K.; Nagamine, T.
Effect of fucoidan on the biotinidase kinetics in human hepatocellular carcinoma
Anticancer Res.
29
1211-1217
2009
Homo sapiens
brenda
Kang, U.B.; Ahn, Y.; Lee, J.W.; Kim, Y.H.; Kim, J.; Yu, M.H.; Noh, D.Y.; Lee, C.
Differential profiling of breast cancer plasma proteome by isotope-coded affinity tagging method reveals biotinidase as a breast cancer biomarker
BMC Cancer
10
114
2010
Homo sapiens (P43251), Homo sapiens
brenda
Angaroni, C.J.; Giner-Ayala, A.N.; Hill, L.P.; Guelbert, N.B.; Paschini-Capra, A.E.; de Kremer, R.D.
Evaluation of the biotinidase activity in hepatic glycogen storage disease patients. Undescribed genetic finding associated with atypical enzymatic behavior: an outlook
J. Inherit. Metab. Dis.
33 Suppl 2
S289-S294
2010
Homo sapiens (P43251), Homo sapiens
brenda
Milankovics, I.; Nemeth, K.; Somogyi, C.; Schuler, A.; Fekete, G.
High frequencies of biotinidase (BTD) gene mutations in the Hungarian population
J. Inherit. Metab. Dis.
33 Suppl 3
S289-S292
2010
Homo sapiens
brenda
Iqbal, F.; Item, C.B.; Vilaseca, M.A.; Jalan, A.; Muehl, A.; Couce, M.L.; Duat, A.; Delgado, M.P.; Bosch, J.; Puche, A.; Campistol, J.; Pineda, M.; Bodamer, O.A.
The identification of novel mutations in the biotinidase gene using denaturing high pressure liquid chromatography (dHPLC)
Mol. Genet. Metab.
100
42-45
2010
Homo sapiens
brenda
Xia, B.; Yang, L.Q.; Huang, H.Y.; Pang, L.; Hu, G.H.; Liu, Q.C.; Yuan, J.H.; Liu, J.J.; Xia, Y.B.; Zhuang, Z.X.
Chromium(VI) causes down regulation of biotinidase in human bronchial epithelial cells by modifications of histone acetylation
Toxicol. Lett.
205
140-145
2011
Homo sapiens
brenda
Thodi, G.; Schulpis, K.H.; Molou, E.; Georgiou, V.; Loukas, Y.L.; Dotsikas, Y.; Papadopoulos, K.; Biti, S.
High incidence of partial biotinidase deficiency cases in newborns of Greek origin
Gene
524
361-362
2013
Homo sapiens (P43251), Homo sapiens
brenda
Tiar, A.; Mekki, A.; Nagara, M.; Rhouma, F.B.; Messaoud, O.; Halim, N.B.; Kefi, R.; Hamlaoui, M.T.; Lebied, A.; Abdelhak, S.
Biotinidase deficiency: novel mutations in Algerian patients
Gene
536
193-196
2014
Homo sapiens (P43251), Homo sapiens
brenda
Li, H.; Spencer, L.; Nahhas, F.; Miller, J.; Fribley, A.; Feldman, G.; Conway, R.; Wolf, B.
Novel mutations causing biotinidase deficiency in individuals identified by newborn screening in Michigan including an unique intronic mutation that alters mRNA expression of the biotinidase gene
Mol. Genet. Metab.
112
242-246
2014
Homo sapiens (P43251), Homo sapiens
brenda
So, A.K.; Kaur, J.; Kak, I.; Assi, J.; MacMillan, C.; Ralhan, R.; Walfish, P.G.
Biotinidase is a novel marker for papillary thyroid cancer aggressiveness
PLoS ONE
7
e40956
2012
Homo sapiens (P43251), Homo sapiens
brenda
Szabo, E.; Szatmari, I.; Szonyi, L.; Takats, Z.
Quantitative analytical method for the determination of biotinidase activity in dried blood spot samples
Anal. Chem.
87
10573-10578
2015
Homo sapiens (P43251), Homo sapiens
brenda
Borsatto, T.; Sperb-Ludwig, F.; Blom, H.J.; Schwartz, I.V.D.
Effect of BTD gene variants on in vitro biotinidase activity
Mol. Genet. Metab.
127
361-367
2019
Homo sapiens (P43251), Homo sapiens
brenda
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