Definition for Difference between revisions of "Serine"
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− | One of the standard set of 20 amino acids. The side chain of serine is chemically equivalent to a substituted methanol. The hydroxyl group of the serine side chain can act as a hydrogen bond donor or acceptor, and has nucleophilic character. The latter property is utilized by the serine proteases, a class of proteolytic enzymes that includes trypsin, chymotrypsin, and subtilisin. Serine is one of the most frequently modified residues in proteins by post-translational phosphorylation - attachment of a phosphate group - of the side chain hydroxyl. Other residues commonly modified in this way are the other hydroxyl-containing amino acids threonine and tyrosine. The hydroxyl group of serine residues in proteins also often serves as a point of attachment for carbohydrate moieties, a post-translational modification termed O-glycosylation. In the case of serine and threonine, the proximal O-linked sugar is usually N-acetylgalactosamine, which is typically attached to proteins passing through the Golgi apparatus. Serine is also involved in lipid biochemistry, as its hydroxyl group is found esterified to phosphatidic acid in phosphatidylserine, a common phosphoglyceride. Codons UCN, AGU, AGC. (Serine is one of three amino acids with six codons - the others are arginine and leucine.) Symbols: Ser, S. | + | One of the standard set of 20 amino acids. The side chain of serine is chemically equivalent to a substituted methanol. The hydroxyl group of the serine side chain can act as a hydrogen bond donor or acceptor, and has nucleophilic character. The latter property is utilized by the serine proteases, a class of proteolytic enzymes that includes trypsin, chymotrypsin, and subtilisin. Serine is one of the most frequently modified residues in proteins by post-translational phosphorylation - attachment of a phosphate group - of the side chain hydroxyl. Other residues commonly modified in this way are the other hydroxyl-containing amino acids threonine and tyrosine. The hydroxyl group of serine residues in proteins also often serves as a point of attachment for carbohydrate moieties, a post-translational modification termed O-glycosylation. In the case of serine and threonine, the proximal O-linked sugar is usually N-acetylgalactosamine, which is typically attached to proteins passing through the Golgi apparatus. Serine is also involved in lipid biochemistry, as its hydroxyl group is found esterified to phosphatidic acid in phosphatidylserine, a common phosphoglyceride. |
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+ | Codons UCN, AGU, AGC. (Serine is one of three amino acids with six codons - the others are arginine and leucine.) | ||
+ | Symbols: Ser, S. |
Revision as of 19:09, 12 January 2012
One of the standard set of 20 amino acids. The side chain of serine is chemically equivalent to a substituted methanol. The hydroxyl group of the serine side chain can act as a hydrogen bond donor or acceptor, and has nucleophilic character. The latter property is utilized by the serine proteases, a class of proteolytic enzymes that includes trypsin, chymotrypsin, and subtilisin. Serine is one of the most frequently modified residues in proteins by post-translational phosphorylation - attachment of a phosphate group - of the side chain hydroxyl. Other residues commonly modified in this way are the other hydroxyl-containing amino acids threonine and tyrosine. The hydroxyl group of serine residues in proteins also often serves as a point of attachment for carbohydrate moieties, a post-translational modification termed O-glycosylation. In the case of serine and threonine, the proximal O-linked sugar is usually N-acetylgalactosamine, which is typically attached to proteins passing through the Golgi apparatus. Serine is also involved in lipid biochemistry, as its hydroxyl group is found esterified to phosphatidic acid in phosphatidylserine, a common phosphoglyceride.
Codons UCN, AGU, AGC. (Serine is one of three amino acids with six codons - the others are arginine and leucine.) Symbols: Ser, S.