EC Number | Application | Comment | Organism |
---|---|---|---|
6.3.4.15 | drug development | the enzyme is a potential target for anti-mycobacterial drugs | Mycobacterium tuberculosis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.4.15 | additional information | - |
additional information | thermodynamics | Mycobacterium tuberculosis | |
6.3.4.15 | 0.000424 | - |
d-biotin | pH 8.0, 37°C | Mycobacterium tuberculosis | |
6.3.4.15 | 0.0052 | - |
apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] | pH 8.0, 37°C | Mycobacterium tuberculosis | |
6.3.4.15 | 0.0211 | - |
ATP | pH 8.0, 37°C | Mycobacterium tuberculosis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.3.4.15 | Mg2+ | - |
Mycobacterium tuberculosis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
6.3.4.15 | 29500 | - |
monomeric enzyme, gel filtration | Mycobacterium tuberculosis |
6.3.4.15 | 56000 | - |
dimeric enzyme, gel filtration | Mycobacterium tuberculosis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.11.23 | ATP + RNA polymerase II carboxy terminal domain | Saccharomyces cerevisiae | the phosphorylated RNAPII CTD, interacts with BRCA1 for induction of DEF1-dependent cleavage and accumulation of a RNAPII fragment containing the P-CTD, overview | ADP + phosphorylated RNA polymerase II carboxy terminal domain | - |
? | |
2.7.11.23 | additional information | Saccharomyces cerevisiae | CTK1 kinase is required for BRCA1-induced lethality in yeast, overview | ? | - |
? | |
6.3.4.15 | ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] | Mycobacterium tuberculosis | overall reaction, BPL catalyses transfer of biotin to an epsilon-amino group of a specific lysine residue, which is usually the 35th amino acid from C-terminal of apoBCCP and converts it to active holoBCCP which promotes fatty acid initiation and elongation | AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)] | - |
? | |
6.3.4.15 | biotin + ATP | Mycobacterium tuberculosis | first half-reaction of BPL | biotinyl-5'-AMP + diphosphate | - |
? | |
6.3.4.15 | biotinyl-5'-AMP + apocarboxylase | Mycobacterium tuberculosis | second half-reaction of BPL, the apocarboxylase is the biotin-carboxyl-carrier protein, which is carboxylated after biotin binding by the biotin carboxylase, BCCP, EC 6.3.4.14 | holocarboxylase + AMP | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.11.23 | Saccharomyces cerevisiae | - |
- |
- |
6.3.4.15 | Mycobacterium tuberculosis | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.11.23 | ATP + RNA polymerase II carboxy terminal domain | the phosphorylated RNAPII CTD, interacts with BRCA1 for induction of DEF1-dependent cleavage and accumulation of a RNAPII fragment containing the P-CTD, overview | Saccharomyces cerevisiae | ADP + phosphorylated RNA polymerase II carboxy terminal domain | - |
? | |
2.7.11.23 | ATP + RNA polymerase II carboxy terminal domain | i.e. RNAPII CTD | Saccharomyces cerevisiae | ADP + phosphorylated RNA polymerase II carboxy terminal domain | - |
? | |
2.7.11.23 | additional information | CTK1 kinase is required for BRCA1-induced lethality in yeast, overview | Saccharomyces cerevisiae | ? | - |
? | |
6.3.4.15 | ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] | overall reaction | Mycobacterium tuberculosis | AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)] | - |
? | |
6.3.4.15 | ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] | overall reaction, BPL catalyses transfer of biotin to an epsilon-amino group of a specific lysine residue, which is usually the 35th amino acid from C-terminal of apoBCCP and converts it to active holoBCCP which promotes fatty acid initiation and elongation | Mycobacterium tuberculosis | AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)] | - |
? | |
6.3.4.15 | biotin + ATP | first half-reaction of BPL | Mycobacterium tuberculosis | biotinyl-5'-AMP + diphosphate | - |
? | |
6.3.4.15 | biotinyl-5'-AMP + apocarboxylase | second half-reaction of BPL, the apocarboxylase is the biotin-carboxyl-carrier protein, which is carboxylated after biotin binding by the biotin carboxylase, BCCP, EC 6.3.4.14 | Mycobacterium tuberculosis | holocarboxylase + AMP | - |
? | |
6.3.4.15 | biotinyl-5'-AMP + apocarboxylase | second half-reaction of BPL, the apocarboxylase is the biotin-carboxyl-carrier protein, which is carboxylated after biotin binding by the biotin carboxylase, EC 6.3.4.14 | Mycobacterium tuberculosis | holocarboxylase + AMP | - |
? | |
6.3.4.15 | D-biotin + ATP | first half-reaction of BPL | Mycobacterium tuberculosis | biotinyl-5'-AMP + diphosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.3.4.15 | dimer | 2 * 29500, SDS-PAGE and dynamic light scattering | Mycobacterium tuberculosis |
6.3.4.15 | monomer | 1 * 29500, SDS-PAGE and dynamic light scattering | Mycobacterium tuberculosis |
6.3.4.15 | More | BPL forms a weak dimer with bio-5'-AMP synthesized from ATP and biotin, on catalysis BPL forms monomeric and a weakly formed physiological dimer, both of which are holoenzymes | Mycobacterium tuberculosis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.11.23 | CTDK-I | - |
Saccharomyces cerevisiae |
2.7.11.23 | CTDK-I kinase | - |
Saccharomyces cerevisiae |
6.3.4.15 | biotin protein ligase | - |
Mycobacterium tuberculosis |
6.3.4.15 | BirA | - |
Mycobacterium tuberculosis |
6.3.4.15 | BPL | - |
Mycobacterium tuberculosis |
6.3.4.15 | group I biotin protein ligase | - |
Mycobacterium tuberculosis |
6.3.4.15 | More | the BPL of Mycobacterium tuberculosis belongs to the group I enzymes, monofunctional enzymes lacking the N-terminal HTH domain | Mycobacterium tuberculosis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.3.4.15 | 37 | - |
assay at | Mycobacterium tuberculosis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
6.3.4.15 | 8 | - |
assay at | Mycobacterium tuberculosis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.7.11.23 | ATP | - |
Saccharomyces cerevisiae | |
6.3.4.15 | ATP | dependent on | Mycobacterium tuberculosis | |
6.3.4.15 | biotin | dependent on, association of biotin and BPL is stabilized by 52 interactions, overview | Mycobacterium tuberculosis | |
6.3.4.15 | additional information | no activity with GTP | Mycobacterium tuberculosis |