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Difference between revisions of "Carbohydrate Binding Module Family 74"
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== Functionalities == | == Functionalities == | ||
''Content in this section should include, in paragraph form, a description of:'' | ''Content in this section should include, in paragraph form, a description of:'' | ||
− | * '''Functional role of CBM:''' | + | * '''Functional role of CBM:''' Aside from starch binding, additional roles of CBM74 in raw starch degradation remain unclear. The deletion of the CBM74 domain of MaAmyA resulted in smaller, but not fewer, pores on starch granules as shown by Scanning Electron Microscopy <cite> Valk2016 </cite>. This suggests that CBM74 may contribute to local polysaccharide chain disruption or may keep the enzyme in close proximity to the areas that have already been hydrolyzed. |
* '''Most Common Associated Modules:''' | * '''Most Common Associated Modules:''' | ||
:1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above.So far, two CBM74-containing proteins have been characterized. | :1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above.So far, two CBM74-containing proteins have been characterized. |
Revision as of 11:17, 23 October 2020
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- 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 | |
https://www.cazy.org/CBM74.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
Functionalities
Content in this section should include, in paragraph form, a description of:
- Functional role of CBM: Aside from starch binding, additional roles of CBM74 in raw starch degradation remain unclear. The deletion of the CBM74 domain of MaAmyA resulted in smaller, but not fewer, pores on starch granules as shown by Scanning Electron Microscopy [1]. This suggests that CBM74 may contribute to local polysaccharide chain disruption or may keep the enzyme in close proximity to the areas that have already been hydrolyzed.
- Most Common Associated Modules:
- 1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above.So far, two CBM74-containing proteins have been characterized.
- In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii is has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.
- 2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes an adjacent CBM25 or CBM26 domain.
- 3. FNIII or Bacterial Ig-like2
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 |
- Candussio A, Schmid G, and Böck A. (1990). Biochemical and genetic analysis of a maltopentaose-producing amylase from an alkaliphilic gram-positive bacterium. Eur J Biochem. 1990;191(1):177-85. DOI:10.1111/j.1432-1033.1990.tb19108.x |
- Candussio A, Schmid G, and Böck A. (1991). Comparative study of the structure/function relationship of wild-type and structurally modified maltopentaose-producing amylase. Eur J Biochem. 1991;199(3):637-41. DOI:10.1111/j.1432-1033.1991.tb16164.x |