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Literature summary extracted from

  • Dey, S.; Lane, J.M.; Lee, R.E.; Rubin, E.J.; Sacchettini, J.C.
    Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase (2010), Biochemistry, 49, 6746-6760.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.62
-
Mycobacterium tuberculosis
2.6.1.105
-
Bacillus subtilis
6.3.3.3 expression in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.62 to 2.2 A resolution, by molecular replacement, and superimposition of the structures bound either to the S-adenosyl-L-methionine analog sinefungin or to 7-oxo-8-aminopelargonic acid. Comparison to structure of the Bacillus subtilis enzyme, EC 2.5.1.105 Mycobacterium tuberculosis
2.6.1.105 to 2.2 A resolution, by molecular replacement. The overall structure is similar to its Mycobacterium tubrculosis and Escherichia coli counterparts, EC 2.6.1.62. Unlike the counterparts, a large part of the active site, i.e. Lys143-Glu172, is completely disordered in both chains. The substrate stabilizes the loop region of the Bacillus subtilis active site Bacillus subtilis
6.3.3.3 in complexes with the substrate 7,8-diaminopelargonic acid or ADP and the product dethiobiotin, up to 1.85 A resolution. Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.62 0.45
-
S-adenosyl-L-methionine pH 7.5, temperature not specified in the publication Mycobacterium tuberculosis
2.6.1.62 0.7
-
sinefungin pH 7.5, temperature not specified in the publication Mycobacterium tuberculosis
6.3.3.3 0.002
-
7,8-diaminononanoate pH 7.5, temperature not specified in the publication Mycobacterium tuberculosis
6.3.3.3 0.029
-
ATP pH 7.5, temperature not specified in the publication Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.62 Mycobacterium tuberculosis P9WQ80
-
-
2.6.1.62 Mycobacterium tuberculosis CDC 1551 P9WQ80
-
-
2.6.1.105 Bacillus subtilis P53555
-
-
2.6.1.105 Bacillus subtilis 168 P53555
-
-
6.3.3.3 Mycobacterium tuberculosis
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.3.3 ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin enzyme reaction involves three steps: carbamylation of theN7 position of 7,8-diaminononanoate, formation of a carbamate-phosphoric anhydride intermediate, and, closure of the ureido ring to form dethiobiotin and release of the inorganic phosphate Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.62 S-adenosyl-L-methionine + 8-amino-7-oxononanoate
-
Mycobacterium tuberculosis S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
?
2.6.1.62 S-adenosyl-L-methionine + 8-amino-7-oxononanoate
-
Mycobacterium tuberculosis CDC 1551 S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
?
2.6.1.62 S-adenosyl-L-methionine + sinefungin
-
Mycobacterium tuberculosis S-adenosyl-4-methylthio-2-oxobutanoate + ?
-
?
2.6.1.62 S-adenosyl-L-methionine + sinefungin
-
Mycobacterium tuberculosis CDC 1551 S-adenosyl-4-methylthio-2-oxobutanoate + ?
-
?
2.6.1.105 additional information presence of substrate stabilizes the loop region of the active site Bacillus subtilis ?
-
?
2.6.1.105 additional information presence of substrate stabilizes the loop region of the active site Bacillus subtilis 168 ?
-
?
6.3.3.3 ATP + 7,8-diaminononanoate + CO2
-
Mycobacterium tuberculosis ADP + phosphate + dethiobiotin
-
?

Synonyms

EC Number Synonyms Comment Organism
2.6.1.105 bioA
-
Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.62 0.009
-
sinefungin pH 7.5, temperature not specified in the publication Mycobacterium tuberculosis
2.6.1.62 0.012
-
S-adenosyl-L-methionine pH 7.5, temperature not specified in the publication Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.62 S-adenosyl-L-methionine
-
Mycobacterium tuberculosis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.6.1.62 0.013
-
sinefungin pH 7.5, temperature not specified in the publication Mycobacterium tuberculosis
2.6.1.62 0.03
-
S-adenosyl-L-methionine pH 7.5, temperature not specified in the publication Mycobacterium tuberculosis