Difference between revisions of "Part:BBa K5185002"
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<partinfo>BBa_K5185002 short</partinfo> | <partinfo>BBa_K5185002 short</partinfo> | ||
| − | Carbohydrate-Binding Module 5 (CBM5) is a protein domain found in carbohydrate-active enzymes, particularly those involved in the degradation of crystalline chitin. CBM5 enhances the ability of related enzymes to bind to their polysaccharide substrates such as chitosan, improving catalytic efficiency. By fusing CBM5 to functional proteins, chitosan-containing materials can be effective targets for modification or degradation. | + | Carbohydrate-Binding Module 5 (CBM5) in particular is a protein binding domain found in carbohydrate-active enzymes, particularly those involved in the degradation of crystalline chitin. CBM5 enhances the ability of related enzymes to bind to their polysaccharide substrates such as chitosan, improving catalytic efficiency. |
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| + | Carbohydrate-binding modules (CBMs) are modules with specificity toward different types of carbohydrates when assisting in carbohydrate degradation. Other than CBM5, this part collection includes other CBMs such as CBM2, CBM3, VbCBMxx, and human integrin domains such as α1 and α2. | ||
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| + | This is part of a part collection aimed to provide first aid wound dressings with enhanced antimicrobial functions and a wider and more complex application, where we characterize bacterial cellulose modification methods and constructs using CBMs as a binding domain, linking HNPs such as HNP1 and HNP4 to carbohydrates such as cellulose and chitosan. By fusing CBM5 to functional proteins, chitosan-containing materials can be effective targets for modification or degradation. The part collection includes: Cellulose binding matrices CBM2 (<partinfo>BBa_K4011001 </partinfo>) which binds to trehalose, CBM3 (<partinfo>BBa_K4011000</partinfo>) which binds to fibrin, CBM5 (<partinfo>BBa_K5185002</partinfo>) which binds to chitosan, and VbCBMxx (<partinfo>BBa_K5185008</partinfo>) which binds to sodium alginate. Human integrins α1 domain (<partinfo>BBa_K5185003 </partinfo>) and α2 domain (<partinfo>BBa_K5185004</partinfo>), linking functional proteins to collagen. This part collection can help to achieve modification of cellulose membranes using different modification/functionalization proteins. | ||
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| + | Because chitosan already possesses stand-alone antimicrobial properties, it could be made into a wound dressing with enhanced antimicrobial strength to combat especially severe instances of infection. | ||
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===Usage and Biology=== | ===Usage and Biology=== | ||
| − | + | In nature, CBM5 is expressed as a domain within chitinases and other glycosidic hydrolases that degrade chitin, a structural polysaccharide found in fungal cell walls and arthropod exoskeletons. The binding of CBM5 to chitin increases catalytic efficiency by creating a better fit between the enzyme and substrate surfaces. The structure of CBM5 is documented in the Protein Data Bank (accession: 1ED7). | |
| + | CBM5 is applied in biotechnological processes such as biocontrol of fungal pathogens, processing of chitinous waste, and production of chitooligosaccharides with biomedical significance. | ||
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<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
Revision as of 19:16, 1 October 2024
Carbohydrate -binding modules 5（CBM5）
Carbohydrate-Binding Module 5 (CBM5) in particular is a protein binding domain found in carbohydrate-active enzymes, particularly those involved in the degradation of crystalline chitin. CBM5 enhances the ability of related enzymes to bind to their polysaccharide substrates such as chitosan, improving catalytic efficiency.
Carbohydrate-binding modules (CBMs) are modules with specificity toward different types of carbohydrates when assisting in carbohydrate degradation. Other than CBM5, this part collection includes other CBMs such as CBM2, CBM3, VbCBMxx, and human integrin domains such as α1 and α2.
This is part of a part collection aimed to provide first aid wound dressings with enhanced antimicrobial functions and a wider and more complex application, where we characterize bacterial cellulose modification methods and constructs using CBMs as a binding domain, linking HNPs such as HNP1 and HNP4 to carbohydrates such as cellulose and chitosan. By fusing CBM5 to functional proteins, chitosan-containing materials can be effective targets for modification or degradation. The part collection includes: Cellulose binding matrices CBM2 (BBa_K4011001) which binds to trehalose, CBM3 (BBa_K4011000) which binds to fibrin, CBM5 (BBa_K5185002) which binds to chitosan, and VbCBMxx (BBa_K5185008) which binds to sodium alginate. Human integrins α1 domain (BBa_K5185003) and α2 domain (BBa_K5185004), linking functional proteins to collagen. This part collection can help to achieve modification of cellulose membranes using different modification/functionalization proteins.
Because chitosan already possesses stand-alone antimicrobial properties, it could be made into a wound dressing with enhanced antimicrobial strength to combat especially severe instances of infection.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 61
Illegal NgoMIV site found at 126 - 1000COMPATIBLE WITH RFC[1000]