Acetylornithine Deacylase Protein, Shigella sonnei

Acetylornithine deacylase protein catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), leading to the formation of succinic acid and LL-2,6-diaminopimelic acid (DAP) , plays a key role in cellular processes. This enzyme activity is integral to the bacterial biosynthesis of lysine and mesodiaminopimelic acid, both of which contribute to the structural integrity of the bacterial cell wall. Acetylornithine Deacylase Protein, Shigella sonnei is the recombinant Acetylornithine Deacylase protein, expressed by E. coli , with tag free. The total length of Acetylornithine Deacylase Protein, Shigella sonnei is 375 a.a., .

Acetylornithine Deacylase is an enzyme that catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), resulting in the formation of succinate and LL-2,6-diaminoheptanedioate (DAP). This reaction is a key step in bacterial lysine biosynthesis and the production of meso-diaminopimelic acid, a critical component of bacterial cell walls. By breaking down SDAP, acetylornithine deacylase plays a crucial role in regulating the biosynthetic pathways responsible for the synthesis of lysine and its derivatives, which are essential for bacterial growth and cell wall integrity. This enzymatic activity contributes to the overall maintenance of bacterial cell structure and function.

Others

E. coli

Tag Free

Q3YZ81 (M1-A375)

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Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.