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Literature summary for 6.3.4.15 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
Search for more literature for 6.3.4.15

Protein Variants

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

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Mycobacterium tuberculosis P96884
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-

Substrates and Products (Substrate)

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

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