panD Protein, Corynebacterium jeikeium

The panD protein plays a crucial role in cellular metabolism by catalyzing the pyruvyl-dependent decarboxylation of aspartate, thereby producing β-alanine. This enzyme activity represents a key step in the biosynthesis of pantothenic acid (vitamin B5), since beta-alanine is the precursor for the formation of this important cofactor. panD Protein, Corynebacterium jeikeium is the recombinant panD protein, expressed by E. coli , with tag free. The total length of panD Protein, Corynebacterium jeikeium is 138 a.a., .

The panD protein plays a crucial role in bacterial metabolism as it catalyzes the pyruvoyl-dependent decarboxylation of aspartate, resulting in the production of beta-alanine. This enzymatic activity is a key step in the biosynthesis of pantothenate, an essential precursor for coenzyme A (CoA) biosynthesis. CoA is involved in various fundamental cellular processes, serving as a cofactor for enzymes participating in fatty acid metabolism, the tricarboxylic acid (TCA) cycle, and other pathways. The pyruvoyl-dependent decarboxylation reaction catalyzed by panD represents a critical point in the regulation of pantothenate biosynthesis and, consequently, the cellular capacity for CoA production. Understanding the functions of panD provides insights into the intricate network of metabolic pathways in bacteria and highlights its potential as a target for antimicrobial interventions.

Others

E. coli

Tag Free

Q4JXL3 (M1-A138)

3432856

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

<1 EU/μg, determined by LAL method.