The Enzyme Database

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EC 3.2.1.198     
Accepted name: α-mannan endo-1,2-α-mannanase
Reaction: Hydrolysis of the terminal α-D-mannosyl-(1→3)-α-D-mannose disaccharide from α-D-mannosyl-(1→3)-α-D-mannosyl-(1→2)-α-D-mannosyl-(1→2)-α-D-mannosyl side chains in fungal cell wall α-mannans.
Systematic name: α-mannan 1,2-[α-D-mannosyl-(1→3)-α-D-mannose] hydrolase
Comments: The enzyme, characterized from the gut bacteria Bacteroides thetaiotaomicron and Bacteroides xylanisolvens, can also catalyse the reaction of EC 3.2.1.130, glycoprotein endo-α-1,2-mannosidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hakki, Z., Thompson, A.J., Bellmaine, S., Speciale, G., Davies, G.J. and Williams, S.J. Structural and kinetic dissection of the endo-α-1,2-mannanase activity of bacterial GH99 glycoside hydrolases from Bacteroides spp. Chemistry 21 (2015) 1966–1977. [PMID: 25487964]
2.  Cuskin, F., Lowe, E.C., Temple, M.J., Zhu, Y., Cameron, E.A., Pudlo, N.A., Porter, N.T., Urs, K., Thompson, A.J., Cartmell, A., Rogowski, A., Hamilton, B.S., Chen, R., Tolbert, T.J., Piens, K., Bracke, D., Vervecken, W., Hakki, Z., Speciale, G., Munoz-Munoz, J.L., Day, A., Pena, M.J., McLean, R., Suits, M.D., Boraston, A.B., Atherly, T., Ziemer, C.J., Williams, S.J., Davies, G.J., Abbott, D.W., Martens, E.C. and Gilbert, H.J. Human gut Bacteroidetes can utilize yeast mannan through a selfish mechanism. Nature 517 (2015) 165–169. [PMID: 25567280]
[EC 3.2.1.198 created 2016]
 
 


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