3.5.1.12: biotinidase
This is an abbreviated version!
For detailed information about biotinidase, go to the full flat file.
Word Map on EC 3.5.1.12
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3.5.1.12
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newborn
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children
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seizure
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infant
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urine
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holocarboxylase
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inborn
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child
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hearing
-
acidosis
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alopecia
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phenylketonuria
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carboxylases
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biotinylation
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symptomatic
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treatable
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biotin-dependent
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ataxia
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hypotonia
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hypothyroidism
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late-onset
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rash
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galactosemia
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acidurias
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avidin
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homocystinuria
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maple
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acidemia
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medicine
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syrup
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lipoylated
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biotin-responsive
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neurocutaneous
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lethargy
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biotin-binding
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paraparesis
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biotin-deficient
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seborrheic
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hyperammonemia
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3-methylcrotonyl-coa
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diagnostics
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analysis
- 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
Reaction
Synonyms
amidohydrolase biotinidase, biocytin hydrolyzing amidase, biotinidase, biotinyl-hydrolase, BTD, lipoamidase, lipolysine hydrolase, lipoyl-X-hydrolase
ECTree
3.5.1.12 biotinidaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.5.1.12 - biotinidase
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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
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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
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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
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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
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colorimetric synthetic substrate
-
-
?
biotinyl-6-aminoquinoline + H2O
biotin + 6-aminoquinoline
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BAQ, fluorogenic substrate as assay for biotinidase
-
-
?
biotinyl-6-aminoquinoline + H2O
biotin + 6-aminoquinoline
Lacticaseibacillus casei Shirota
-
-
-
-
?
biotinyl-di-iodotyramine + H2O
biotin + di-iodotyramine
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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
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-
?
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
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-
ir
epsilon-N-biotinyl-L-lysine + H2O
biotin + L-lysine
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cannot cleave biocytin that is bound to avidin
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-
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
-
-
?
