EC Number   |
General Information |
Reference |
|---|
    6.3.4.15 | malfunction |
biotin deficiency, e.g. occuring in patients with BTD deficiency, in severely malnourished children in developing countries, and in individuals consuming large amounts of raw egg white which contains the protein avidin, has adverse effects on cellular and humoral immune functions, and it can lead to candida dermatitis and presented with absent delayed-hypersensitivity skin-tests responses, IgA deficiency, and subnormal percentages of T-lymphocytes in peripheral blood, overview |
702499 |
| 6.3.4.15 | malfunction |
deficiency in human HCS results in decreased activity of the acyl-CoA carboxylase and affects various metabolic processes |
703738 |
| 6.3.4.15 | malfunction |
holocarboxylase synthetase, HCS, deficiency is an inborn error of biotin metabolism, leading to a multiple carboxylases deficiency. A Japanese male neonate with HCS deficiency received maternal administration of biotin from 33 weeks gestation, acylcarnitine profiles compared to control, phenotype, overview |
702952 |
| 6.3.4.15 | metabolism |
holo-BPL is protected from proteolysis by biotinyl-5'-AMP, an intermediate of the BPL-catalyzed reaction. Apo-MtBPL is completely digested by trypsin within 20 min of co-ncubation. Substrate selectivity and inability to promote self biotinylation are exquisite features of Mycobacterium tuberculosis BPL |
716697 |
| 6.3.4.15 | metabolism |
holocarboxylase synthetase governs the cellular fate of the essential micronutrient biotin, i.e. vitamin H or B7 |
701936 |
| 6.3.4.15 | metabolism |
the enzyme is involved in the biotin metabolism, detailed overview |
702499 |
| 6.3.4.15 | physiological function |
BirA is an effective regulator of biotin operon transcription. Deletion of the DNA binding domain of BirA results in loss of virtually all of its ligation activity |
-, 745788 |
| 6.3.4.15 | physiological function |
BirA regulates transcription at three genomic sites: bioWAFDBI, yuiG and yhfUTS. The N-terminal DNA binding domain can be deleted from Bacillus subtilis BirA without adverse effects on its ligase function |
-, 746268 |
| 6.3.4.15 | physiological function |
expression of biotin operon genes bioW, bioA, bioF, bioD, bioB, and bioI in Corynebacterium glutamicum. The recombinant strain is able to produce lysine in a medium lacking biotin, and the lysine yield on glucose is similar to what is obtained when using a medium containing biotin. Specific growth rate decreases by of 20% when the strain is cultivated without biotin. Neither pyruvate carboxylase pycA nor biotin ligase birA overexpression, whether alone or in combination, has an effect on specific growth rate |
-, 744795 |
| 6.3.4.15 | physiological function |
Francisella novicida encodes two biotin protein ligases. BirA and BplA are both functional biotin protein ligases. BirA has a ligase domain as well as an N-terminal DNA-binding regulatory domain. BirA, but not BplA, regulates transcription of the biotin synthetic operon, regulating and thereby likely preventing wasteful synthesis of biotin. Isoform BplA lacks the N-terminal DNA binding motif and is more efficient in ligase reaction than BirA. Expression of BplA (but not birA) increases significantly during infection of macrophages. BplA (but not BirA) is required for bacterial replication within macrophages as well as in mice |
745676 |
