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

BRENDA support

Literature summary for 6.3.4.15 extracted from

  • Ma, Q.; Akhter, Y.; Wilmanns, M.; Ehebauer, M.T.
    Active site conformational changes upon reaction intermediate biotinyl-5-AMP binding in biotin protein ligase from Mycobacterium tuberculosis (2014), Protein Sci., 23, 932-939 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.4.15

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of the apo-form and in complex with reaction intermediate biotinyl-5'-AMP. Binding of the reaction intermediate leads to clear disorder-to-order transitions. A conserved lysine, Lys138, in the active site is essential for biotinylation Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
K138S inactive Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 ATP pH 8.0, 30°C Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis I6YFP0
-
-
Mycobacterium tuberculosis H37Rv I6YFP0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin + apo-[acetyl-CoA carbon-dioxide ligase]
-
 Mycobacterium tuberculosis AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase]
-
 ?
ATP + biotin + apo-[acetyl-CoA carbon-dioxide ligase]
-
 Mycobacterium tuberculosis H37Rv AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase]
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.017
-
 ATP pH 8.0, 30°C Mycobacterium tuberculosis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.085
-
 ATP pH 8.0, 30°C Mycobacterium tuberculosis