acnB Protein, E. coli

The acnB protein coordinates short-chain fatty acid catabolism through the TCA pathway and 2-methylcitric acid cycle I, demonstrating catalytic versatility. It is involved in the reversible isomerization of citric acid to isocitrate and the hydration of 2-methyl-cis-aconitic acid. acnB Protein, E. coli is the recombinant Virus-derived acnB protein, expressed by E. coli , with tag free. The total length of acnB Protein, E. coli is 865 a.a., with molecular weight of ~95 kDa.

The acnB Protein plays a multifaceted role in the catabolism of short-chain fatty acids (SCFA) through both the tricarboxylic acid (TCA) pathway, specifically the acetyl degradation route, and the 2-methylcitrate cycle I, associated with propionate degradation. This enzyme exhibits catalytic versatility, facilitating the reversible isomerization of citrate to isocitrate via cis-aconitate, as well as the hydration of 2-methyl-cis-aconitate to generate (2R,3S)-2-methylisocitrate. Beyond its metabolic functions, the apo form of AcnB serves as a RNA-binding regulatory protein, particularly during oxidative stress. In this state, the inactive AcnB apo-enzyme lacking iron-sulfur clusters binds the acnB mRNA 3' untranslated regions, stabilizing acnB mRNA and augmenting AcnB synthesis. This intricate regulatory mechanism establishes a post-transcriptional positive autoregulatory switch. Additionally, AcnB influences the stability of the sodA transcript, revealing its broader impact on cellular processes beyond its primary metabolic functions.

Virus

E. coli

Tag Free

P36683 (M1-V865)

Approximately 95 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.