Identification and characterization of a deaminoneuraminic acid (Kdn)-specific aldolase from Sphingobacterium species. (29th August 2022)

• Record Type: Journal Article
• Authors: Nakagawa, Takahiro; Iwaki, Yuya; Wu, Di; Hane, Masaya; Sato, Chihiro; Kitajima, Ken
• Is Part Of: Glycobiology. Volume 33:Number 1(2023)
• Page Start: 47
• Page End: 56
• Publication Date: 2022-08-29
• Subjects: deaminoneuraminic acid -- deaminoneuraminate aldolase -- deaminoneuraminate-pyruvate lyase -- sialic acid -- sphingobacterium; Glycoproteins -- Periodicals; Glycolipids -- Periodicals; Glycoconjugates -- Periodicals; 572.567
• DOI: 10.1093/glycob/cwac053
• Languages: English
• ISSNs: 0959-6658

Abstract

Abstract: Sialic acid (Sia) is a group of acidic sugars with a 9-carbon backbone, and classified into 3 species based on the substituent group at C5 position: N -acetylneuraminic acid (Neu5Ac), N -glycolylneuraminic acid (Neu5Gc), and deaminoneuraminic acid (Kdn). In Escherichia coli, the sialate aldolase or N -acetylneuraminate aldolase (NanA) is known to catabolize these Sia species into pyruvate and the corresponding 6-carbon mannose derivatives. However, in bacteria, very little is known about the catabolism of Kdn, compared with Neu5Ac. In this study, we found a novel Kdn-specific aldolase (Kdn-aldolase), which can exclusively degrade Kdn, but not Neu5Ac or Neu5Gc, from Sphingobacterium sp., which was previously isolated from a Kdn-assimilating bacterium. Kdn-aldolase had the optimal pH and temperature at 7.0–8.0 and 50 °C, respectively. It also had the synthetic activity of Kdn from pyruvate and mannose. Site-specific mutagenesis revealed that N50 residue was important for the Kdn-specific reaction. Existence of the Kdn-aldolase suggests that Kdn-specific metabolism may play a specialized role in some bacteria.