Sandbox Reserved 1476
From Proteopedia
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==PDB ID 3AIE== | ==PDB ID 3AIE== | ||
| - | This enzyme is a glucansucrase from ''Streptococcus mutans''.<ref name="Ito">PMID:21354427</ref> These enzymes are large and extracellularly expressed by few other bacterial species.<ref name="Leemhuis">PMID:22796091</ref> Their main function is to catalyze the production of glucose polymers from sucrose substrates.<ref name="Ito" /> These polymers comprise the dental plaque that promotes tooth decay in humans. For this reason, knowledge of the structure, genome, and proteome of this enzyme is critical for the development of an inhibitor in an effort to reduce the prevalence of cavities and periodontal disease. | + | This enzyme is a glucansucrase from ''Streptococcus mutans''.<ref name="Ito">PMID:21354427</ref> These enzymes are large and extracellularly expressed by few other bacterial species.<ref name="Leemhuis">PMID:22796091</ref> Their main function is to catalyze the production of glucose polymers from sucrose substrates.<ref name="Ito" /> These polymers comprise the dental plaque that promotes tooth decay in humans. For this reason, knowledge of the structure, <u>genome, and proteome</u> of this enzyme is critical for the development of an inhibitor in an effort to reduce the prevalence of cavities and periodontal disease. |
<StructureSection load='3aie' size='350' side='right' caption='GTF-SI of Streptococcus mutans (PDB entry [[3aie]])' scene=''> | <StructureSection load='3aie' size='350' side='right' caption='GTF-SI of Streptococcus mutans (PDB entry [[3aie]])' scene=''> | ||
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Domain A is regarded as the catalytic domain.<ref name="Ito" /> Within it, exists a highly conserved <scene name='80/800655/Catalytic_triad_2/1'>catalytic triad</scene>, which includes two aspartic acid residues and a general acid/base glutamate.<ref name="Ito" /> A calcium ion is also bound to help stabilize the formation of the catalytic domain.<ref name="Ito" /> | Domain A is regarded as the catalytic domain.<ref name="Ito" /> Within it, exists a highly conserved <scene name='80/800655/Catalytic_triad_2/1'>catalytic triad</scene>, which includes two aspartic acid residues and a general acid/base glutamate.<ref name="Ito" /> A calcium ion is also bound to help stabilize the formation of the catalytic domain.<ref name="Ito" /> | ||
===Supersecondary Structure=== | ===Supersecondary Structure=== | ||
| - | This enzyme features two well-known motifs. Domain A consists of a TIM barrel.<ref name="Ito" /> It is composed of a ring of beta strands surrounded by a ring of alpha helices. Domain C contains a greek key motif, which is four antiparallel beta strands that form a sheet.<ref name="Leemhuis" /> | + | This enzyme features two well-known motifs. Domain A consists of a TIM barrel.<ref name="Ito" /> It is composed of a ring of beta strands surrounded by a ring of alpha helices. Domain C contains a greek key motif, which is four antiparallel beta strands that form a sheet.<ref name="Leemhuis" /> <u>Include images of super secondary structure from Chimera</u> |
== Function == | == Function == | ||
| - | The major functions of this enzyme include synthesis of glucan, a glucosylated acceptor molecule, or release of free glucose.<ref name="Monchois">PMID:10234842</ref> All of the various products are released from the same active site and from a glucose-enzyme intermediate.<ref name="Ito" /> The sole natural donor for all of these reactions is sucrose.<ref name="Hamada">PMID:6446023</ref> No cofactors or energy-carriers are required for these reactions.<ref name="Monchois" /> The energy required for bond formation is solely provided by the energy released from sucrose hydrolysis.<ref name="Monchois" />This particular glucansucrase is a mutansucrase, meaning it catalyzes the formation of α(1,3) linked glucose moieties.<ref name="Ito" /> The latest research proposes that the glucose moieties are most likely added to the non-reducing end of the glucan chain.<ref name="Moulis">PMID:16864576</ref> Binding of a glucan chain to the active site may cause a conformational change within the enzyme that favors elongation of the glucan chain instead of the formation of the other products.<ref name="Monchois" /> Acceptor molecules include maltose and isomaltose.<ref name="Leemhuis" /> Free glucose may be released upon hydrolysis of the glucose-enzyme intermediate.<ref name="Leemhuis" /> | + | The major functions of this enzyme include synthesis of glucan, a glucosylated acceptor molecule, or release of free glucose.<ref name="Monchois">PMID:10234842</ref> All of the various products are released from the same active site and from a glucose-enzyme intermediate.<ref name="Ito" /> The sole natural donor for all of these reactions is sucrose.<ref name="Hamada">PMID:6446023</ref> No cofactors or energy-carriers are required for these reactions.<ref name="Monchois" /> The energy required for bond formation is solely provided by the energy released from sucrose hydrolysis.<ref name="Monchois" />This particular glucansucrase is a mutansucrase, meaning it catalyzes the formation of α(1,3) linked glucose moieties.<ref name="Ito" /> The latest research proposes that the glucose moieties are most likely added to the non-reducing end of the glucan chain.<ref name="Moulis">PMID:16864576</ref> Binding of a glucan chain to the active site may cause a conformational change within the enzyme that favors elongation of the glucan chain instead of the formation of the other products.<ref name="Monchois" /> Acceptor molecules include maltose and isomaltose.<ref name="Leemhuis" /> Free glucose may be released upon hydrolysis of the glucose-enzyme intermediate.<ref name="Leemhuis" /> <u>Include image of reaction breakdown</u> |
== Disease == | == Disease == | ||
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| - | == Relevance == | ||
Based on the enzyme's contributions to dental cavity formation, this enzyme and its genes are attractive targets for inhibition. | Based on the enzyme's contributions to dental cavity formation, this enzyme and its genes are attractive targets for inhibition. | ||
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Revision as of 18:41, 5 December 2018
| This Sandbox is Reserved from November 5 2018 through January 1, 2019 for use in the course "CHEM 4923: Senior Project taught by Christina R. Bourne at the University of Oklahoma, Norman, USA. This reservation includes Sandbox Reserved 1471 through Sandbox Reserved 1478. |
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PDB ID 3AIE
This enzyme is a glucansucrase from Streptococcus mutans.[1] These enzymes are large and extracellularly expressed by few other bacterial species.[2] Their main function is to catalyze the production of glucose polymers from sucrose substrates.[1] These polymers comprise the dental plaque that promotes tooth decay in humans. For this reason, knowledge of the structure, genome, and proteome of this enzyme is critical for the development of an inhibitor in an effort to reduce the prevalence of cavities and periodontal disease.
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