Information on EC 3.5.1.12 - biotinidase

Word Map on EC 3.5.1.12
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.5.1.12
-
RECOMMENDED NAME
GeneOntology No.
biotinidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
biotin amide + H2O = biotin + NH3
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of amide bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biotin metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
biotin-amide amidohydrolase
Also acts on biotin esters.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-15-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
guinea pig
-
-
Manually annotated by BRENDA team
chicken
-
-
Manually annotated by BRENDA team
Shirota strain
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Achromobacter sp.
-
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus arabinosus
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
BTD is responsible for recycling the vitamin biotin
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
1'-N-methoxycarbonyl-biocytin + H2O
1-N-methoxycarbonyl-biotin + L-lysine
show the reaction diagram
-
-
-
-
?
2-(N-biotinyl)-amino-5-nitro-benzoic acid + H2O
biotin + 2-amino-5-nitrobenzoic acid
show the reaction diagram
3-(N-biotinyl)-amino-6-nitrobenzoic acid + H2O
biotin + 3-amino-6-nitrobenzoic acid
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
-
-
?
biotin methyl ester + H2O
?
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-L-aspartate + H2O
biotin + L-aspartate
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,N-(dipicolyl)biotinamido-Boc-lysine + H2O
N,N-(dipicolyl)biotinamine + Boc-L-lysine
show the reaction diagram
-
-
-
-
?
N-(+)biotinyl-4-aminobenzoic acid + H2O
4-aminobenzoic acid + biotin
show the reaction diagram
N-(1'-N-methoxycarbonyl-biotinyl)p-aminobenzoic acid + H2O
1-N-methoxycarbonyl-biotin + 4-aminobenzoic acid
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-biotinyl-beta-alanine + H2O
biotin + beta-alanine
show the reaction diagram
N-biotinyl-p-aminobenzoate + ?
p-aminobenzoate + biotin
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 SUBSTRATES
NATURAL PRODUCTS
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
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
activator might be need to give full release of biotin, erratic effect
Zn2+
-
activator might be need to give full release of biotin, erratic effect
INHIBITORS
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
CuCl2
diisopropylfluorophosphate
guanidine hydrochloride
-
0.5 M
iodoacetamide
lipoic acid
-
competitive
monoiodoacetate
p-hydroxymercuribenzoate
PCMB
-
noncompetitive
phenylmethylsulfonyl fluoride
puromycin
-
peptidase inhibitor
Urea
-
0.5 M
Valproic acid
-
200-600 mg/kg
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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-p-aminobenzoic acid
1.3
lipoyllysine
-
-
0.0905 - 0.1002
m-(N-biotinylamino)benzoic acid
0.303
Met-enkephalin
-
-
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
-
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
0.2 - 0.3
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6
5 - 8
-
p-(N-biotinylamino)benzoic acid as substrate
5.5
-
lipoyllysine as substrate
6 - 6.8
6 - 7.5
-
with synthetic substrates
6.8 - 7
-
-
9.5
-
liver enzyme has 2 pH optima at pH 6.0 and pH 9.5 with lipoyl-p-aminobenzoic acid as substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7.5
-
-
5 - 8.5
-
-
5.3 - 9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
; abdominal
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56770
-
estimated from amino acid sequence
60000
-
gel filtration, treated with N-glycanase
66000 - 76000
70000 - 80000
-
glycosylated enzyme
70000
-
gel permeation, nondenaturating
71000
-
gel filtration, treated with neuraminidase
76500
-
gel filtration, SDS-PAGE, normal serum biotinidase has 9 isoforms
78000
-
gel filtration
80000
-
SDS-PAGE
85000
-
-
92000
-
gel filtration
110000
115000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
-
-
171922
6 - 9.5
-
-
171933
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 70
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
-
no loss of enzyme occurs in 10% at 0C, at 50% all activity lost
urea
-
50% activity in 3 M solution
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, activity decreases upon storage
-
-20C, mercaptoethanol, a few months without loss of activity
-
-20C, phosphate buffer pH 7.5, a few months
-
-70C stable
-
15C enzyme solution with toluene, for a week or more without appreciable loss of activity
-
4C, 0.1 M phosphate buffer pH 6.0, 1 mM 2-mercaptoethanol, 1 mM EDTA, 1 month without loss of activity
-
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Cr(VI) causes downregulation at the transcriptional level by modification of histone acetylation
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A171T/D444H
A82D
-
4% activity compared to the wild type enzyme
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
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
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
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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
identification of the site of carboxylation of the biotinyl prosthetic group of several biotin enzymes
diagnostics
medicine