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Difference between revisions of "Carbohydrate Binding Module Family 32"
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A periplasmic CBM32 from Yersinia enterolitica binds polygalaturonic acid components of pectin <cite>Abbott2007</cite>. | A periplasmic CBM32 from Yersinia enterolitica binds polygalaturonic acid components of pectin <cite>Abbott2007</cite>. | ||
| − | The ''Clostridium perfringens'' CBM32s have been well studied and their ligand specificities | + | The ''Clostridium perfringens'' CBM32s have been well studied and many of their ligand specificities described as follows: D-galactose, N-acetyl-D-galactosamine<cite>Boraston2007 Ficko-Blean2012 Ficko-Blean2006</cite>, D-galactose-β-1,4-N-acetyl-D-glucosamine (LacNAc), L-fucose-α-1,2-D-galactose-β-1,4-N-acetyl-D-glucosamine (type II blood group H-trisaccharide) <cite>Ficko-Blean2006</cite> N-acetyl-D-glucosamine, N-acetyl-D-glucosamine-β-1,3-N-acetyl-D-galactosamine, N-acetyl-D-glucosamine-β-1,2-D-mannose, N-acetyl-D-glucosamine-β-1,3-D-mannose (non-biological) <cite>Ficko-Blean2009</cite>, N-acetyl-D-glucosamine-α-1,4-D-galactose<cite>Ficko-Blean2012</cite> |
Some members of the family 32 CBMs have demonstrated a degree of promiscuity in their binding, these include CpCBM32-2 from the NagH enzyme and CpCBM32C from the NagJ enzyme, both produced by ''Clostridium perfringens''<cite>Ficko-Blean2009 Ficko-Blean2006</cite>. | Some members of the family 32 CBMs have demonstrated a degree of promiscuity in their binding, these include CpCBM32-2 from the NagH enzyme and CpCBM32C from the NagJ enzyme, both produced by ''Clostridium perfringens''<cite>Ficko-Blean2009 Ficko-Blean2006</cite>. | ||
Revision as of 07:25, 14 May 2013
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- Author: ^^^Elizabeth Ficko-Blean^^^
- Responsible Curator: ^^^Al Boraston^^^
| CAZy DB link | |
| https://www.cazy.org/CBM32.html |
Ligand specificities
In 1995 the first CBM32 structure and canonical ligand specificity for D-galactose were described from a multi-modular sialidase produced by Micromonospora viridifaciens[1].
A CBM32 from a Cellvibrio mixtus family 16 glycoside hydrolase binds laminarin and pustulan [2]
A CBM32 from a Clostridium thermocellum mannanase has demonstrated binding on the non-reducing end of β-mannans and β-1,4-linked mannooligosaccharides[3]
A periplasmic CBM32 from Yersinia enterolitica binds polygalaturonic acid components of pectin [4].
The Clostridium perfringens CBM32s have been well studied and many of their ligand specificities described as follows: D-galactose, N-acetyl-D-galactosamine[5, 6, 7], D-galactose-β-1,4-N-acetyl-D-glucosamine (LacNAc), L-fucose-α-1,2-D-galactose-β-1,4-N-acetyl-D-glucosamine (type II blood group H-trisaccharide) [7] N-acetyl-D-glucosamine, N-acetyl-D-glucosamine-β-1,3-N-acetyl-D-galactosamine, N-acetyl-D-glucosamine-β-1,2-D-mannose, N-acetyl-D-glucosamine-β-1,3-D-mannose (non-biological) [8], N-acetyl-D-glucosamine-α-1,4-D-galactose[6]
Some members of the family 32 CBMs have demonstrated a degree of promiscuity in their binding, these include CpCBM32-2 from the NagH enzyme and CpCBM32C from the NagJ enzyme, both produced by Clostridium perfringens[7, 8].
Please see these references for an essential introduction to the CAZy classification system: [9, 10]. CBMs, in particular, have been extensively reviewed [11, 12, 13, 14].
Structural Features
Content in this section should include, in paragraph form, a description of:
- Fold: Structural fold (beta trefoil, beta sandwich, etc.)
- Type: Include here Type A, B, or C and properties
- Features of ligand binding: Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.
Functionalities
Content in this section should include, in paragraph form, a description of:
- Functional role of CBM: Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.
- Most Common Associated Modules: 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)
- Novel Applications: Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.
Family Firsts
- First Identified
- Insert archetype here, possibly including very brief synopsis.
- First Structural Characterization
- Insert archetype here, possibly including very brief synopsis.
References
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Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). DOI: 10.1042/BJ20080382
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