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Literature summary extracted from

  • Bennett, C.B.; Westmoreland, T.J.; Verrier, C.S.; Blanchette, C.A.; Sabin, T.L.; Phatnani, H.P.; Mishina, Y.V.; Huper, G.; Selim, A.L.; Madison, E.R.; Bailey, D.D.; Falae, A.I.; Galli, A.; Olson, J.A.; Greenleaf, A.L.; Marks, J.R.
    Yeast screens identify the RNA polymerase II CTD and SPT5 as relevant targets of BRCA1 interaction (2008), PLoS ONE, 3, e1448.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
6.3.4.15 drug development the enzyme is a potential target for anti-mycobacterial drugs Mycobacterium tuberculosis

KM Value [mM]

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.15 Mg2+
-
 Mycobacterium tuberculosis

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.23 Saccharomyces cerevisiae
-
-
-
6.3.4.15 Mycobacterium tuberculosis
-
-
-

Substrates and Products (Substrate)

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
-
 ?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.4.15 37
-
 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.4.15 8
-
 assay at Mycobacterium tuberculosis

Cofactor

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