Protein Variants | Comment | Organism |
---|---|---|
R118G | mutant shows enhanced self and promiscuous biotinylation | Escherichia coli |
R69A | the binding constant for biotin is nearly the same as that observed for the wild type protein. Mutant does not undergo self-botinylation | Mycobacterium tuberculosis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
GLNDIFEAQKIEWH | i.e. Schatz' peptide, synthetic biotinable minimal peptide, competitively inhibits self-biotinylation | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Mycobacterium tuberculosis | P96884 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + biotin + C-terminal domain of apo-biotin carboxyl carrier protein | Escherichia coli BPL biotinylates both the homologous BCCP domain BCCP87 and the corresponding domain from Mycobacterium tuberculosis | Escherichia coli | AMP + diphosphate + biotinylated C-terminal domain of acetyl CoA carboxylase | - |
? | |
ATP + biotin + C-terminal domain of apo-biotin carboxyl carrier protein | Mycobacterium tuberculosis BPL specifically biotinylates the homologous BCCP domain BCCP87, but not the Escherichia coli domain BCCP87 | Mycobacterium tuberculosis | AMP + diphosphate + biotinylated C-terminal domain of apo-biotin carboxyl carrier protein | - |
? | |
ATP + biotin + GLNDIFEAQKIEWH | i.e. Schatz' peptide, synthetic biotinable minimal peptide | Escherichia coli | AMP + diphosphate + biotinylated GLNDIFEAQKIEWH | - |
? | |
additional information | enzyme is not able to biotinylate Schatz' minimal peptide GLNDIFEAQKIEWH | Mycobacterium tuberculosis | ? | - |
? | |
additional information | Escherichia coli enzyme undergoes self-biotinylation | Escherichia coli | ? | - |
? |
General Information | Comment | Organism |
---|---|---|
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 | Escherichia coli |
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 | Mycobacterium tuberculosis |