Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.3.4.15 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
Search for more literature for 6.3.4.15

Application

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information thermodynamics Mycobacterium tuberculosis
0.000424
-
 d-biotin pH 8.0, 37°C Mycobacterium tuberculosis
0.0052
-
 apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] pH 8.0, 37°C Mycobacterium tuberculosis
0.0211
-
 ATP pH 8.0, 37°C Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29500
-
 monomeric enzyme, gel filtration Mycobacterium tuberculosis
56000
-
 dimeric enzyme, gel filtration Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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)]
-
 ?
biotin + ATP Mycobacterium tuberculosis first half-reaction of BPL biotinyl-5'-AMP + diphosphate
-
 ?
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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] overall reaction Mycobacterium tuberculosis AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
 ?
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)]
-
 ?
biotin + ATP first half-reaction of BPL Mycobacterium tuberculosis biotinyl-5'-AMP + diphosphate
-
 ?
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
-
 ?
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
-
 ?
D-biotin + ATP first half-reaction of BPL Mycobacterium tuberculosis biotinyl-5'-AMP + diphosphate
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 29500, SDS-PAGE and dynamic light scattering Mycobacterium tuberculosis
monomer 1 * 29500, SDS-PAGE and dynamic light scattering Mycobacterium tuberculosis
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

Synonyms Comment Organism
biotin protein ligase
-
 Mycobacterium tuberculosis
BirA
-
 Mycobacterium tuberculosis
BPL
-
 Mycobacterium tuberculosis
group I biotin protein ligase
-
 Mycobacterium tuberculosis
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]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Mycobacterium tuberculosis
biotin dependent on, association of biotin and BPL is stabilized by 52 interactions, overview Mycobacterium tuberculosis
additional information no activity with GTP Mycobacterium tuberculosis