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
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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
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biotin-deficient
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seborrheic
-
hyperammonemia
- 3-methylcrotonyl-coa
- diagnostics
- analysis
Reaction
Synonyms
amidohydrolase biotinidase, biocytin hydrolyzing amidase, biotinidase, biotinyl-hydrolase, BTD, lipoamidase, lipolysine hydrolase, lipoyl-X-hydrolase
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Natural Substrates Products
Natural Substrates Products on EC 3.5.1.12 - biotinidase
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REACTION DIAGRAM
Met-enkephalin + H2O
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suitable natural substrate for biotinidase
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biotin + L-lysine
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natural substrate, biotinidase is responsible for cleaving biocytin, thereby liberating and recycling biotin
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biocytin + H2O
biotin + L-lysine
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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
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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
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biotin amide + H2O
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171917, 171919, 171921, 171922, 171923, 171925, 171926, 171928, 171929, 171930, 171931, 171932, 171933, 171934, 171935, 171936
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biotin amide + H2O
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very short biotinyl peptides, enzyme is not active when biotin is attached to large native proteins, for example intact holocarboxylases
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biotin amide + H2O
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cleaves D-biotinylamides and esters, recycling of the vitamin
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biotin amide + H2O
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cleaves D-biotinylamides and esters, recycling of the vitamin
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epsilon-N-biotinyl-L-lysine + H2O
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epsilon-N-biotinyl-L-lysine + H2O
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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
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epsilon-N-biotinyl-L-lysine + H2O
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biotinidase is essential for recycling the vitamin biotin and for transferring biotin to proteins
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additional information
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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
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additional information
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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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additional information
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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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