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Literature summary extracted from

  • Purushothaman, S.; Annamalai, K.; Tyagi, A.; Surolia, A.
    Diversity in functional organization of class I and class II biotin protein ligase (2011), PLoS ONE, 6, e16850.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.15 R118G mutant shows enhanced self and promiscuous biotinylation Escherichia coli
6.3.4.15 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

EC Number Inhibitors Comment Organism Structure
6.3.4.15 GLNDIFEAQKIEWH i.e. Schatz' peptide, synthetic biotinable minimal peptide, competitively inhibits self-biotinylation Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.15 Escherichia coli
-
-
-
6.3.4.15 Mycobacterium tuberculosis P96884
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.15 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
-
 ?
6.3.4.15 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
-
 ?
6.3.4.15 ATP + biotin + GLNDIFEAQKIEWH i.e. Schatz' peptide, synthetic biotinable minimal peptide Escherichia coli AMP + diphosphate + biotinylated GLNDIFEAQKIEWH
-
 ?
6.3.4.15 additional information enzyme is not able to biotinylate Schatz' minimal peptide GLNDIFEAQKIEWH Mycobacterium tuberculosis ?
-
 ?
6.3.4.15 additional information Escherichia coli enzyme undergoes self-biotinylation Escherichia coli ?
-
 ?

General Information

EC Number General Information Comment Organism
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 Escherichia coli
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 Mycobacterium tuberculosis