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(N-D,L-lipoyl-p-aminobenzoic acid) + H2O
?
1'-N-methoxycarbonyl-biocytin + H2O
1-N-methoxycarbonyl-biotin + L-lysine
-
-
-
-
?
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
biocytin + ?
biotin + L-lysine
-
-
-
-
?
biocytin + H2O
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
-
-
?
biotin methyl ester + H2O
?
biotinyl-4-amino benzoic acid + H2O
biotin + 4-aminobenzoic acid
-
-
-
?
biotinyl-4-aminobenzoic acid + H2O
biotin + 4-aminobenzoic acid
biotinyl-6-aminoquinoline + H2O
biotin + 6-aminoquinoline
biotinyl-di-iodotyramine + H2O
biotin + di-iodotyramine
biotinyl-L-aspartate + H2O
biotin + L-aspartate
biotinyl-monoiodotyramine + H2O
biotin + monoiodotyramine
-
radioactive assay for early diagnosis of biotinidase defiency in serum
-
-
?
biotinyl-p-aminobenzoate + H2O
?
-
-
-
-
?
dynorphin A (1-6) + H2O
?
-
-
-
-
?
dynorphin A (1-7) + H2O
?
-
-
-
-
?
epsilon-N-(D,L-lipoyl)-L-lysine + H2O
?
epsilon-N-biotinyl-L-lysine + H2O
?
epsilon-N-biotinyl-L-lysine + H2O
biotin + L-lysine
Leu-enkephalin + H2O
?
-
-
-
-
?
Leu-enkephalin amide + H2O
?
-
-
-
-
?
lipoyl-4-aminobenzoic acid + H2O
?
-
-
-
-
?
lipoyllysine + H2O
?
-
-
-
-
?
Met-enkephalin amide + H2O
?
-
-
-
-
?
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-biotinyl-3-amino benzoate + H2O
biotin + 3-aminobenzoate
-
-
-
?
N-biotinyl-3-aminobenzoic acid + H2O
biotin + 3-aminobenzoic acid
N-biotinyl-beta-alanine + H2O
biotin + beta-alanine
N-biotinyl-p-aminobenzoate + ?
p-aminobenzoate + biotin
-
-
-
-
?
N-DL-dethiobiotinyl-p-aminobenzoic acid + H2O
dethiobiotin + 4-aminobenzoic acid
-
-
-
-
?
p-(N-biotinylamino)benzoic acid + H2O
biotin + p-aminobenzoic acid
additional information
?
-
(N-D,L-lipoyl-p-aminobenzoic acid) + H2O
?
-
-
-
-
?
(N-D,L-lipoyl-p-aminobenzoic acid) + H2O
?
-
-
-
-
?
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
-
-
-
-
?
biocytin + H2O
biotin + L-lysine
-
-
-
?
biocytin + H2O
biotin + L-lysine
-
natural substrate
-
-
?
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
-
-
?
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
?
-
-
-
-
?
biotin amide + H2O
?
-
-
-
-
?
biotin amide + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
biotin amide + H2O
?
-
-
-
-
?
biotin amide + H2O
?
-
-
-
-
?
biotin amide + H2O
?
-
-
-
-
?
biotin amide + H2O
?
-
cleaves D-biotinylamides and esters, recycling of the vitamin
-
-
?
biotin amide + H2O
?
-
soluble bound biotin
-
-
?
biotin methyl ester + H2O
?
-
-
-
-
?
biotin methyl ester + H2O
?
-
-
-
-
?
biotin methyl ester + H2O
?
-
-
-
-
?
biotin methyl ester + H2O
?
-
-
-
-
?
biotinyl-4-aminobenzoic acid + H2O
biotin + 4-aminobenzoic acid
-
-
-
-
?
biotinyl-4-aminobenzoic acid + H2O
biotin + 4-aminobenzoic acid
-
colorimetric synthetic substrate
-
-
?
biotinyl-4-aminobenzoic acid + H2O
biotin + 4-aminobenzoic acid
-
-
-
-
?
biotinyl-6-aminoquinoline + H2O
biotin + 6-aminoquinoline
-
-
-
-
?
biotinyl-6-aminoquinoline + H2O
biotin + 6-aminoquinoline
-
BAQ, fluorogenic substrate as assay for biotinidase
-
-
?
biotinyl-6-aminoquinoline + H2O
biotin + 6-aminoquinoline
-
-
-
-
?
biotinyl-6-aminoquinoline + H2O
biotin + 6-aminoquinoline
-
-
-
-
?
biotinyl-6-aminoquinoline + H2O
biotin + 6-aminoquinoline
-
-
-
-
?
biotinyl-6-aminoquinoline + H2O
biotin + 6-aminoquinoline
-
-
-
-
?
biotinyl-di-iodotyramine + H2O
biotin + di-iodotyramine
-
-
-
-
?
biotinyl-di-iodotyramine + H2O
biotin + di-iodotyramine
-
radioactive assay for early diagnosis of biotinidase defiency in serum
-
-
?
biotinyl-L-aspartate + H2O
biotin + L-aspartate
-
-
-
-
?
biotinyl-L-aspartate + H2O
biotin + L-aspartate
-
-
-
-
?
biotinyl-L-aspartate + H2O
biotin + L-aspartate
-
-
-
-
?
biotinyl-L-aspartate + H2O
biotin + L-aspartate
-
-
-
-
?
epsilon-N-(D,L-lipoyl)-L-lysine + H2O
?
-
-
-
-
?
epsilon-N-(D,L-lipoyl)-L-lysine + H2O
?
-
-
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
-
-
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
-
biocytin, soluble bound biotin
-
-
?
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
-
-
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
-
-
-
-
ir
epsilon-N-biotinyl-L-lysine + H2O
biotin + L-lysine
-
biocytin, soluble bound biotin
-
-
ir
Met-enkephalin + H2O
?
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
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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5
1'-N-methoxycarbonyl-biocytin
-
-
0.01 - 0.055
biotinyl-4-aminobenzoic acid
0.00383 - 24.1
Biotinyl-6-aminoquinoline
0.0259 - 0.027
biotinyl-di-iodotyramine
0.0158
biotinyl-monoiodotyramine
-
-
0.167
dynorphin A (1-6)
-
-
0.132
dynorphin A (1-7)
-
-
0.00048 - 0.016
epsilon-N-biotinyl-L-lysine
0.119
Leu-enkephalin amide
-
-
0.69 - 1.3
lipoyl-4-aminobenzoic acid +
-
0.0905 - 0.1002
m-(N-biotinylamino)benzoic acid
0.099
Met-enkephalin amide
-
-
0.85
N-(1'-N-methoxycarbonyl-biotinyl)p-aminobenzoic acid
-
-
0.0685 - 0.0714
N-DL-desthiobiotinyl-p-aminobenzoic acid
0.0042 - 0.05
p-(N-biotinylamino)benzoic acid
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
-
0.01
biotinyl-4-aminobenzoic acid
-
-
0.01
biotinyl-4-aminobenzoic acid
-
human plasma
0.01
biotinyl-4-aminobenzoic acid
-
porcine liver, human serum
0.01
biotinyl-4-aminobenzoic acid
-
porcine liver, human serum
0.055
biotinyl-4-aminobenzoic acid
-
porcine serum
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
0.022
Biotinyl-6-aminoquinoline
-
human plasma
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
5.49
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from heart, male 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
7.91
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from lung, male rat
7.97
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from kidney, female rat
8.23
Biotinyl-6-aminoquinoline
-
pH 7.0, 37°C, enzyme from liver, male 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
0.0259
biotinyl-di-iodotyramine
-
-
0.027
biotinyl-di-iodotyramine
-
-
0.00048
epsilon-N-biotinyl-L-lysine
-
110000 Da biotinidase
0.002
epsilon-N-biotinyl-L-lysine
-
human serum
0.005
epsilon-N-biotinyl-L-lysine
-
-
0.005
epsilon-N-biotinyl-L-lysine
-
human serum
0.0051
epsilon-N-biotinyl-L-lysine
-
-
0.0051
epsilon-N-biotinyl-L-lysine
-
76000 Da biotinidase
0.0062
epsilon-N-biotinyl-L-lysine
-
-
0.0062
epsilon-N-biotinyl-L-lysine
-
human plasma
0.00625
epsilon-N-biotinyl-L-lysine
-
-
0.0065
epsilon-N-biotinyl-L-lysine
-
-
0.0065
epsilon-N-biotinyl-L-lysine
-
human plasma
0.0077
epsilon-N-biotinyl-L-lysine
-
-
0.0077
epsilon-N-biotinyl-L-lysine
-
pH 5.5
0.0078
epsilon-N-biotinyl-L-lysine
-
-
0.0078
epsilon-N-biotinyl-L-lysine
-
pH 7
0.008
epsilon-N-biotinyl-L-lysine
-
-
0.008
epsilon-N-biotinyl-L-lysine
-
serum
0.01
epsilon-N-biotinyl-L-lysine
-
porcine liver
0.016
epsilon-N-biotinyl-L-lysine
-
-
0.016
epsilon-N-biotinyl-L-lysine
-
kidney
0.69
lipoyl-4-aminobenzoic acid +
-
pH 9.5
-
1.3
lipoyl-4-aminobenzoic acid +
-
pH 6.0
-
0.0905
m-(N-biotinylamino)benzoic acid
-
pH 5.5
0.1002
m-(N-biotinylamino)benzoic acid
-
-
0.0685
N-DL-desthiobiotinyl-p-aminobenzoic acid
-
pH 7
0.0714
N-DL-desthiobiotinyl-p-aminobenzoic acid
-
pH 5.5
0.0042
p-(N-biotinylamino)benzoic acid
-
-
0.009
p-(N-biotinylamino)benzoic acid
-
110000 Da biotinidase
0.015
p-(N-biotinylamino)benzoic acid
-
crude liver extract
0.02
p-(N-biotinylamino)benzoic acid
-
-
0.03
p-(N-biotinylamino)benzoic acid
-
-
0.03
p-(N-biotinylamino)benzoic acid
-
76000 Da biotinidase
0.0306
p-(N-biotinylamino)benzoic acid
-
-
0.0306
p-(N-biotinylamino)benzoic acid
-
pH 5.5, D-biotin as inhibitor
0.0319
p-(N-biotinylamino)benzoic acid
-
-
0.0319
p-(N-biotinylamino)benzoic acid
-
pH 5.5
0.0333
p-(N-biotinylamino)benzoic acid
-
-
0.0333
p-(N-biotinylamino)benzoic acid
-
pH 7
0.0341
p-(N-biotinylamino)benzoic acid
-
-
0.0341
p-(N-biotinylamino)benzoic acid
-
pH 7, D-biocytin as inhibitor
0.05
p-(N-biotinylamino)benzoic acid
-
-
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A82D
-
4% activity compared to the wild type enzyme
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
C418S/D444H
-
24% activity compared to the wild type enzyme
C458fs/H323R
naturally occuring mutation involved in biotinidase deficiency, no phenotype
D222N
variant shows normal activity
D228G/D444H
naturally occuring mutation involved in biotinidase deficiency, no phenotype
D444H/Q456H
naturally occuring mutation involved in biotinidase deficiency
D444H/T532M
naturally occuring mutation involved in biotinidase deficiency
E112K/Q456H
-
1% activity compared to the wild type enzyme
E112K/R538C
-
1% activity compared to the wild type enzyme
E218Q/L278V
-
1% activity compared to the wild type enzyme
E46X/D444H
-
20% activity compared to the wild type enzyme
G34D/G114V
-
naturally occuring mutation in a Spanish patient with enzyme deficiency
L215F/D444H
-
17% activity compared to the wild type enzyme
L278V/D444H
-
14-20% activity compared to the wild type enzyme
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
N195S/D444H
-
21% activity compared to the wild type enzyme
N300H/D444H
naturally occuring mutation involved in biotinidase deficiency, no phenotype
N489S
activity in medium is 43% compared to wild-type activity
P187S
-
naturally occuring mutation in an Austrian patient with enzyme deficiency
Q456H/D444H
-
19-29% activity compared to the wild type enzyme
Q456H/R538C
-
2% activity compared to the wild type enzyme
R157C/D444H
-
18-23% activity compared to the wild type enzyme
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/D444H
-
16-25% activity compared to the wild type enzyme
S311R
-
naturally occuring mutation in a Spanish patient with enzyme deficiency
T152P/D444H
-
20% activity compared to the wild type enzyme
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
V199M/R211C
-
8% activity compared to the wild type enzyme
V62M
-
1% activity compared to the wild type enzyme
Y425Ter
-
naturally occuring mutation, with additional frameshift mutation in this mutant, in several Austrian patients with enzyme deficiency
A171T/D444H
-
15-27% activity compared to the wild type enzyme
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
-
2% activity compared to the wild type enzyme
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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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
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1963
Enterococcus faecalis, Homo sapiens, Lacticaseibacillus casei, no activity in Achromobacter sp., no activity in Lactobacillus arabinosus, Rattus rattus, Sus scrofa
-
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Moss, J.; Lane, M.D.
The biotin-dependent enzymes
Adv. Enzymol. Relat. Areas Mol. Biol.
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1971
Enterococcus faecalis, Lacticaseibacillus casei, Sus scrofa
brenda
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A sensitive fluorimetric rate assay for biotinidase using a new derivative of biotin, biotynyl-6-aminoquinoline
Anal. Biochem.
140
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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
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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
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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