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Information on EC 3.5.1.12 - biotinidase and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.12 biotinidase
IUBMB Comments
Also acts on biotin esters.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
biotinidase, lipoamidase, biotinyl-hydrolase, biocytin hydrolyzing amidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidohydrolase biotinidase
-
-
-
-
biocytin hydrolyzing amidase
-
-
biotinidase
-
-
biotinyl-hydrolase
-
-
lipoyl-X-hydrolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
biotin amide + H2O = biotin + NH3
show the reaction diagram
also acts on biotin esters
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of amide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
biotin-amide amidohydrolase
Also acts on biotin esters.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-15-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(N-D,L-lipoyl-p-aminobenzoic acid) + H2O
?
show the reaction diagram
-
-
-
-
?
biocytin + ?
biotin + L-lysine
show the reaction diagram
-
-
-
-
?
biocytin + H2O
biotin + L-lysine
show the reaction diagram
biotin amide + H2O
?
show the reaction diagram
biotin amide + H2O
biotin + NH3
show the reaction diagram
-
good substrate, Cys-245 is likely the active site cysteine, formation of a thioester intermediate between biotin and cysteine
-
-
?
biotinyl-4-amino benzoic acid + H2O
biotin + 4-aminobenzoic acid
show the reaction diagram
-
-
-
?
biotinyl-4-aminobenzoic acid + H2O
biotin + 4-aminobenzoic acid
show the reaction diagram
biotinyl-6-aminoquinoline + H2O
biotin + 6-aminoquinoline
show the reaction diagram
biotinyl-di-iodotyramine + H2O
biotin + di-iodotyramine
show the reaction diagram
biotinyl-monoiodotyramine + H2O
biotin + monoiodotyramine
show the reaction diagram
-
radioactive assay for early diagnosis of biotinidase defiency in serum
-
-
?
biotinyl-p-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
-
?
dynorphin A (1-6) + H2O
?
show the reaction diagram
-
-
-
-
?
dynorphin A (1-7) + H2O
?
show the reaction diagram
-
-
-
-
?
epsilon-N-(D,L-lipoyl)-L-lysine + H2O
?
show the reaction diagram
-
-
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
show the reaction diagram
-
-
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
biotin + L-lysine
show the reaction diagram
Leu-enkephalin + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-enkephalin amide + H2O
?
show the reaction diagram
-
-
-
-
?
Met-enkephalin + H2O
?
show the reaction diagram
Met-enkephalin amide + H2O
?
show the reaction diagram
-
-
-
-
?
N-(+)biotinyl-4-aminobenzoic acid + H2O
4-aminobenzoic acid + biotin
show the reaction diagram
-
-
-
-
?
N-biotinyl-3-amino benzoate + H2O
biotin + 3-aminobenzoate
show the reaction diagram
-
-
-
?
N-biotinyl-3-aminobenzoic acid + H2O
biotin + 3-aminobenzoic acid
show the reaction diagram
-
-
-
-
?
N-DL-dethiobiotinyl-p-aminobenzoic acid + H2O
dethiobiotin + 4-aminobenzoic acid
show the reaction diagram
-
-
-
-
?
p-(N-biotinylamino)benzoic acid + H2O
biotin + p-aminobenzoic acid
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
biocytin + H2O
biotin + L-lysine
show the reaction diagram
biotin amide + H2O
?
show the reaction diagram
epsilon-N-(D,L-lipoyl)-L-lysine + H2O
?
show the reaction diagram
-
-
-
-
?
epsilon-N-biotinyl-L-lysine + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-enkephalin + H2O
?
show the reaction diagram
-
-
-
-
?
Met-enkephalin + H2O
?
show the reaction diagram
-
suitable natural substrate for biotinidase
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
amastatin
-
peptidase inhibitor
bestatin
-
peptidase inhibitor
biotin
biotinyl 2-amido-pyridine
-
40% inhibition at 1 mM
biotinyl 4-(amidomethyl)phenyl boronic acid
-
53% inhibition at 1 mM
biotinyl allylamide
-
37% inhibition at 1 mM
biotinyl anilide
-
55% inhibition at 1 mM
biotinyl benzylamide
-
47% inhibition at 1 mM
biotinyl N-methylanilide
-
26% inhibition at 1 mM
biotinyl-methyl 4-(amidomethyl)benzoate
-
competitive inhibitor, 80% inhibition at 1 mM
guanidine hydrochloride
-
0.5 M
iodoacetamide
-
-
monoiodoacetate
-
-
p-hydroxymercuribenzoate
phenylmethylsulfonyl fluoride
puromycin
-
peptidase inhibitor
Urea
-
0.5 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
biotinyl-4-aminobenzoic acid
0.022
Biotinyl-6-aminoquinoline
-
human plasma
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 - 0.0078
epsilon-N-biotinyl-L-lysine
0.119
Leu-enkephalin amide
-
-
0.0905 - 0.1002
m-(N-biotinylamino)benzoic acid
0.303
Met-enkephalin
-
-
0.099
Met-enkephalin amide
-
-
0.0685 - 0.0714
N-DL-desthiobiotinyl-p-aminobenzoic acid
0.009 - 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
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 0.485
biotin
0.27
biotinyl 2-amido-pyridine
-
-
0.09
biotinyl allylamide
-
-
0.26
biotinyl anilide
-
-
0.06
biotinyl-methyl 4-(amidomethyl)benzoate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6
5 - 8
-
p-(N-biotinylamino)benzoic acid as substrate
6 - 6.8
6 - 7.5
-
with synthetic substrates
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
analysis of gene expression in breast cancer plasma, diverse tissue samples, profiling, overview
Manually annotated by BRENDA team
-
splice variant 1a is present only in testis
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
splice variants 1a and 1b localize to mitochondria and/or endoplasmic reticulum
Manually annotated by BRENDA team
additional information
-
biotinidase is directed to the secretory pathway and perhaps mitochondria
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
BTD is responsible for recycling the vitamin biotin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BTD_HUMAN
543
0
61133
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
115000
56770
-
estimated from amino acid sequence
60000
-
gel filtration, treated with N-glycanase
66000 - 76000
68000
70000 - 80000
-
glycosylated enzyme
71000
-
gel filtration, treated with neuraminidase
76000
76500
-
gel filtration, SDS-PAGE, normal serum biotinidase has 9 isoforms
78000
-
gel filtration
80000
-
SDS-PAGE
85000
-
-
92000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A171T/D444H
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
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
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
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
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
-
-
171922
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 70
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, activity decreases upon storage
-
-70°C stable
-
4°C, 0.1 M phosphate buffer pH 6.0, 1 mM 2-mercaptoethanol, 1 mM EDTA, 1 month without loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
76000 Da and 110000 Da proteins copurified
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA from a liver library encoding biotinidase cloned and sequenced
-
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 biotinidase deficiency greek patient genes, real-time PCR
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Cr(VI) causes downregulation at the transcriptional level by modification of histone acetylation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Ebrahim, H.; Dakshinamurti, K.
A fluorometric assay for biotinidase
Anal. Biochem.
154
282-286
1986
Homo sapiens, no activity in Lactobacillus arabinosus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Hayakawa, K.; Oizumi, J.
Determination of biotinidase activity by liquid chromatography with fluorometric detection
J. Chromatogr.
383
148-152
1986
Homo sapiens
Manually annotated by BRENDA team
Wolf, B.; Hymes, J.; Heard, G.S.
Biotinidase
Methods Enzymol.
184
103-111
1990
Enterococcus faecalis, Homo sapiens, Lacticaseibacillus casei, Rattus rattus, Sus scrofa
Manually annotated by BRENDA team
Garganta, C.L.; Wolf, B.
Lipoamidase activity in human serum is due to biotinidase
Clin. Chim. Acta
189
313-326
1990
Homo sapiens
Manually annotated by BRENDA team
Oizumi, J.; Hayakawa, K.
Biotinidase in the porcine cerebrum
Arch. Biochem. Biophys.
278
381-385
1990
Cavia porcellus, Homo sapiens, Oryctolagus cuniculus, Rattus rattus, Sus scrofa
Manually annotated by BRENDA team
Hart, P.S.; Hymes, J.; Wolf, B.
Isoforms of human serum biotinidase
Clin. Chim. Acta
197
257-264
1991
Homo sapiens
Manually annotated by BRENDA team
Oizumi, J.; Hayakawa, K.
Enkephalin hydrolysis by human serum biotinidase
Biochim. Biophys. Acta
1074
433-438
1991
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Oizumi, J.; Hayakawa, K.
Biocytin-specific 110-kDa biotinidase from human serum
Clin. Chim. Acta
215
63-71
1993
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Hymes, J.; Fleischhauer, K.; Wolf, B.
Biotinidase in serum and tissues
Methods Enzymol.
279
422-435
1997
Homo sapiens, Rattus rattus, Sus scrofa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Brenner, C.
Catalysis in the nitrilase superfamily
Curr. Opin. Struct. Biol.
12
775-782
2002
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Hayakawa, K.; Nagamine, T.
Effect of fucoidan on the biotinidase kinetics in human hepatocellular carcinoma
Anticancer Res.
29
1211-1217
2009
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team