NPL cleaves Neu5Ac,Neu5Gc to ManNAc,ManNGc and pyruvate

Stable Identifier
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Once in the cytosol, sialic acids are either reutilized or degraded. N-acetylneuraminate lyase (NPL) is a cytosolic, tetrameric enzyme that can cleave the major sialic acids N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc) to form N-acetylmannosamine (ManNAc) and N-glycolylmannosamine (ManNGc) respectively (Wu et al. 2005). Although humans cannot form Neu5Gc due to a non-functional CMAHP enzyme, Neu5Gc can be ingested by dietary means and must therefore be degraded to avoid accumulation of this immunoreactive sialic acid (Bergfeld et al. 2012).

Literature References
PubMed ID Title Journal Year
22692205 Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating the intracellular fate of the non-human sialic acid N-glycolylneuraminic acid

Pearce, OM, Pham, T, Diaz, SL, Varki, A, Bergfeld, AK

J. Biol. Chem. 2012
16147865 A novel splice variant of human gene NPL, mainly expressed in human liver, kidney and peripheral blood leukocyte

Xu, J, Gu, S, Zou, X, Xie, Y, Mao, Y, Ji, C, Zheng, H, Jin, Z, Wu, M

DNA Seq. 2005
Catalyst Activity

N-acetylneuraminate lyase activity of NPL tetramer [cytosol]

Orthologous Events
Cite Us!