Deciphered enzyme that causes tooth decay from sticking to teeth
December 20, 2010
The teachers Groningen Bauke Dijkstra and Lubbert Dijkhuizen have deciphered the structure and mechanism of functional enzyme that is responsible glucansucrase plaque sticking to teeth. This knowledge will encourage the identification of substances that inhibit the enzyme. Just add the chemical to toothpaste, or even candy and tooth decay will be a thing of the past.
The research results were published this week in the journal Proceedings of the National Academy of Sciences (PNAS).
Groningen University researchers analyzed the Lactobacillus reuteri glucansucrase lactic acid bacteria, which is in the human mouth and digestive tract. The bacteria use the enzyme glucansucrase to convert sugar from food into long chains, sticky sugar. They use this glue to adhere to tooth enamel. The main cause of tooth decay, Streptococcus mutans, bacteria, also use this enzyme. Once attached to the tooth enamel, these bacteria ferment sugars releasing acids that dissolve calcium teeth. This is how decay develops.
dimensional structure
Using protein crystallography, the researchers were able to elucidate the three dimensional (3D) structure of the enzyme. Groningen researchers are the first to succeed in glucansucrase crystallization. The crystal structure revealed that the mechanism of protein folding is unique. The various areas of the enzyme is not formed from a single linear chain of amino acids, but from two pieces joined by a U-shaped structure of the chain, this is the first report on a folding mechanism in the literature.
functional mechanism
The collapse of the 3D structure provide researchers with detailed information on the functional mechanism of the enzyme. The enzyme splits sucrose into fructose and glucose, and then add the glucose molecule to a sugar chain growing. So far the scientific community is that both processes were carried out by different parts of the enzyme. However, the model created by researchers at Groningen has shown that both activities occur in the same active site of the enzyme. Inhibitors
expected
Dijkhuizen specific inhibitors glucansucrase the enzyme may help prevent the adhesion of bacteria to tooth enamel. Information on the mechanism and functional structure of the enzyme is crucial for the development of such inhibitors. Until now, such research has not succeeded, Dijkhuizen states: Several inhibitors have not been studied glucansucrase only blocked but also the digestive enzyme amylase in our saliva, which is necessary to degrade the starch. Evolution
The crystal structure also provides an explanation for this dual inhibition. The data published by scientists shows that Groningen glucansucrase proteins probably evolved from enzymes that degrade starch amylase. We knew that the two enzymes were similar, Dijkhuizen said, but the crystal structure revealed that the active sites are virtually identical. inhibitors future which should be directed to very specific objectives and that both enzymes are evolutionary closely related.
Toothpaste and sweets
Dijkhuizen said that in future glucansucrase inhibitors can be added to toothpaste and mouthwash. But it may still be possible to add to sweets, he suggests. An inhibitor can prevent the sugars released cause damage in the mouth. But do not expect Dijkhuizen toothbrushes have had their day:. You will always need clean teeth
Disclaimer: This article is not intended to provide medical advice, diagnosis or treatment. The opinions expressed herein do not necessarily reflect those of ScienceDaily or its staff.
Source: akronoticias.com
The teachers Groningen Bauke Dijkstra and Lubbert Dijkhuizen have deciphered the structure and mechanism of functional enzyme that is responsible glucansucrase plaque sticking to teeth. This knowledge will encourage the identification of substances that inhibit the enzyme. Just add the chemical to toothpaste, or even candy and tooth decay will be a thing of the past.
The research results were published this week in the journal Proceedings of the National Academy of Sciences (PNAS).
Groningen University researchers analyzed the Lactobacillus reuteri glucansucrase lactic acid bacteria, which is in the human mouth and digestive tract. The bacteria use the enzyme glucansucrase to convert sugar from food into long chains, sticky sugar. They use this glue to adhere to tooth enamel. The main cause of tooth decay, Streptococcus mutans, bacteria, also use this enzyme. Once attached to the tooth enamel, these bacteria ferment sugars releasing acids that dissolve calcium teeth. This is how decay develops.
dimensional structure
Using protein crystallography, the researchers were able to elucidate the three dimensional (3D) structure of the enzyme. Groningen researchers are the first to succeed in glucansucrase crystallization. The crystal structure revealed that the mechanism of protein folding is unique. The various areas of the enzyme is not formed from a single linear chain of amino acids, but from two pieces joined by a U-shaped structure of the chain, this is the first report on a folding mechanism in the literature.
functional mechanism
The collapse of the 3D structure provide researchers with detailed information on the functional mechanism of the enzyme. The enzyme splits sucrose into fructose and glucose, and then add the glucose molecule to a sugar chain growing. So far the scientific community is that both processes were carried out by different parts of the enzyme. However, the model created by researchers at Groningen has shown that both activities occur in the same active site of the enzyme. Inhibitors
expected
Dijkhuizen specific inhibitors glucansucrase the enzyme may help prevent the adhesion of bacteria to tooth enamel. Information on the mechanism and functional structure of the enzyme is crucial for the development of such inhibitors. Until now, such research has not succeeded, Dijkhuizen states: Several inhibitors have not been studied glucansucrase only blocked but also the digestive enzyme amylase in our saliva, which is necessary to degrade the starch. Evolution
The crystal structure also provides an explanation for this dual inhibition. The data published by scientists shows that Groningen glucansucrase proteins probably evolved from enzymes that degrade starch amylase. We knew that the two enzymes were similar, Dijkhuizen said, but the crystal structure revealed that the active sites are virtually identical. inhibitors future which should be directed to very specific objectives and that both enzymes are evolutionary closely related.
Toothpaste and sweets
Dijkhuizen said that in future glucansucrase inhibitors can be added to toothpaste and mouthwash. But it may still be possible to add to sweets, he suggests. An inhibitor can prevent the sugars released cause damage in the mouth. But do not expect Dijkhuizen toothbrushes have had their day:. You will always need clean teeth
Disclaimer: This article is not intended to provide medical advice, diagnosis or treatment. The opinions expressed herein do not necessarily reflect those of ScienceDaily or its staff.
Source: akronoticias.com
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