Literature summary for 3.2.1.81 extracted from

Henshaw, J.; Horne-Bitschy, A.; van Bueren, A.L.; Money, V.A.; Bolam, D.N.; Czjzek, M.; Ekborg, N.A.; Weiner, R.M.; Hutcheson, S.W.; Davies, G.J.; Boraston, A.B.; Gilbert, H.J.
Family 6 carbohydrate binding modules in beta-agarases display exquisite selectivity for the non-reducing termini of agarose chains (2006), J. Biol. Chem., 281, 17099-17107.

Search for more literature for 3.2.1.81

Crystallization (Commentary)

Crystallization (Comment)	Organism
carbohydrate binding module CBM6-2 of isoform Aga16B in complex with neoagarohexaose. The carbohydrate binding module targets the equatorial O4 and the axial O3 of the anhydro-L-galactose moiety	Saccharophagus degradans

Organism

Organism	UniProt	Comment	Textmining
Saccharophagus degradans	-	isoforms Aga16B and Aga86E	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	carbohydrate binding modules of both isoforms Aga16B and Aga86E bind specifically to the non-reducing end of agarose chains, recognizing only the first repeat of the dissaccharide. The carbohydrate binding module targets the equatorial O4 and the axial O3 of the anhydro-L-galactose moiety	Saccharophagus degradans	?	-	?

Subunits

Subunits	Comment	Organism
More	carbohydrate binding modules of both isoforms Aga16B and Aga86E bind specifically to the non-reducing end of agarose chains, recognizing only the first repeat of the dissaccharide	Saccharophagus degradans

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)