Structural highlights
Function
[SIAS_HUMAN] Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of the C-terminal antifreeze-like (AFL) domain of human sialic acid synthase was determined by NMR spectroscopy. The structure comprises one alpha- and two single-turn 3(10)-helices and two beta-strands, and is similar to those of the type III antifreeze proteins. Evolutionary trace analyses of the type III antifreeze protein family suggested that the class-specific residues in the human and bacterial AFL domains are important for their substrate binding, while the class-specific residues of the fish antifreeze proteins are gathered on the ice-binding surface.
Solution structure of the antifreeze-like domain of human sialic acid synthase.,Hamada T, Ito Y, Abe T, Hayashi F, Guntert P, Inoue M, Kigawa T, Terada T, Shirouzu M, Yoshida M, Tanaka A, Sugano S, Yokoyama S, Hirota H Protein Sci. 2006 May;15(5):1010-6. Epub 2006 Apr 5. PMID:16597820[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hamada T, Ito Y, Abe T, Hayashi F, Guntert P, Inoue M, Kigawa T, Terada T, Shirouzu M, Yoshida M, Tanaka A, Sugano S, Yokoyama S, Hirota H. Solution structure of the antifreeze-like domain of human sialic acid synthase. Protein Sci. 2006 May;15(5):1010-6. Epub 2006 Apr 5. PMID:16597820 doi:10.1110/ps.051700406
