P12 Features and structure of a sialic acid aldolase from Aliivibrio salmonicida

P12 Features and structure of a sialic acid aldolase from Aliivibrio salmonicida

Man Kumari Gurung, Bjørn Altermark, Inger Lin Uttakleiv Ræder, Ronny Helland and Arne Oskar Smalås

N-acetylneuraminic acid aldolase (NanA) is a class I aldolase that catalyzes the reversible cleavage of N-acetylneuraminic acid (Neu5Ac) into N-acetyl-D-mannosamine (ManNAc) and
pyruvate. The enzyme is found in both eukaryotes and prokaryotes. Its biological role is to cleave Neu5Ac however; the in vitro condensation of ManNAc and ManNAc-analogues with
pyruvate to produce Neu5Ac variants has been studied extensively as well. Neu5Ac belongs to the family of 9-carbon α-keto acidic sugars called sialic acids. The many application areas for sialic acids i. e. their uses as glyconutrients, antiviral- and potential anticancer agents and in diagnostic research have increased the global demand for these sugars. Thus it is vital to develop more cost-efficient methods for production. Enzymatic methods are maybe the easiest and most efficient way of production due to the enzymes isomeric specificity. However, to date, all of the characterized aldolases are from mesophilic sources. Cold-adapted enzymes are known to have higher catalytic efficiency compared to their mesophilic counterparts. In
order to identify an efficient aldolase we have cloned, expressed, purified and characterized NanA from the psychrophilic gram-negative fish pathogen Aliivibrio salmonicida. In addition
the crystal structure is solved to a resolution of 1.65 Å.

Poster and presentation not available