Literature summary for 2.6.1.105 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P53555	-	-
Bacillus subtilis 168	P53555	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	presence of substrate stabilizes the loop region of the active site	Bacillus subtilis	?	-	?
additional information	presence of substrate stabilizes the loop region of the active site	Bacillus subtilis 168	?	-	?

Synonyms

Synonyms	Comment	Organism
bioA	-	Bacillus subtilis

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Release 2023.1 (January 2023)