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Difference between revisions of "Carbohydrate Binding Module Family 74"
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| − | * [[Author]]: ^^^ | + | * [[Author]]: ^^^Amanda Photenhauer^^^ |
| − | * [[Responsible Curator]]: ^^^ | + | * [[Responsible Curator]]: ^^^Nicole Koropatkin^^^ |
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<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --> | <!-- The data in the table below should be updated by the Author/Curator according to current information on the family --> | ||
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| − | {| {{Prettytable}} | + | {| {{Prettytable}} |
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| + | |{{Hl2}} colspan="2" align="center" |'''Carbohydrate Binding Module Family 74''' | ||
| + | |- | ||
| + | |'''Carbohydrate Specificity''' | ||
| + | |Starch | ||
| + | |||
| + | |- | ||
| + | |||
| + | |'''Associated GH Families''' | ||
| + | |GH13_28<br>GH13_19<br>GH13_32<br>none | ||
|- | |- | ||
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
|- | |- | ||
| − | | colspan="2" |{{CAZyDBlink}} | + | | colspan="2" |{{CAZyDBlink}}GH27.html |
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== Ligand specificities == | == Ligand specificities == | ||
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| − | + | The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type <cite> Valk2016 </cite> | |
== Structural Features == | == Structural Features == | ||
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== Family Firsts == | == Family Firsts == | ||
;First Identified | ;First Identified | ||
| − | : | + | :CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>. |
;First Structural Characterization | ;First Structural Characterization | ||
| − | : | + | :No structure has yet been determined for any CBM74 family member. |
== References == | == References == | ||
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#Shoseyov2006 pmid=16760304 | #Shoseyov2006 pmid=16760304 | ||
#Guillen2010 pmid=19908036 | #Guillen2010 pmid=19908036 | ||
| + | #Valk2016 pmid=27101946 | ||
</biblio> | </biblio> | ||
[[Category:Carbohydrate Binding Module Families|CBM074]] | [[Category:Carbohydrate Binding Module Families|CBM074]] | ||
Revision as of 20:26, 15 August 2019
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: ^^^Amanda Photenhauer^^^
- Responsible Curator: ^^^Nicole Koropatkin^^^
| Carbohydrate Binding Module Family 74 | |
| Carbohydrate Specificity | Starch |
| Associated GH Families | GH13_28 GH13_19 GH13_32 none |
| CAZy DB link | |
| http://www.cazy.org/GH27.html | |
Ligand specificities
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type [1]
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
- CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from Microbacterium aurum[1].
- First Structural Characterization
- No structure has yet been determined for any CBM74 family member.
References
- Valk V, Lammerts van Bueren A, van der Kaaij RM, and Dijkhuizen L. (2016). Carbohydrate-binding module 74 is a novel starch-binding domain associated with large and multidomain α-amylase enzymes. FEBS J. 2016;283(12):2354-68. DOI:10.1111/febs.13745 |
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |
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Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. The Biochemist, vol. 30, no. 4., pp. 26-32. Download PDF version.
- Boraston AB, Bolam DN, Gilbert HJ, and Davies GJ. (2004). Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J. 2004;382(Pt 3):769-81. DOI:10.1042/BJ20040892 |
- Hashimoto H (2006). Recent structural studies of carbohydrate-binding modules. Cell Mol Life Sci. 2006;63(24):2954-67. DOI:10.1007/s00018-006-6195-3 |
- Shoseyov O, Shani Z, and Levy I. (2006). Carbohydrate binding modules: biochemical properties and novel applications. Microbiol Mol Biol Rev. 2006;70(2):283-95. DOI:10.1128/MMBR.00028-05 |
- Guillén D, Sánchez S, and Rodríguez-Sanoja R. (2010). Carbohydrate-binding domains: multiplicity of biological roles. Appl Microbiol Biotechnol. 2010;85(5):1241-9. DOI:10.1007/s00253-009-2331-y |