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Serine (symbol Ser or S) [3] [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α- amino group (which is in the protonated − NH + 3 form under biological conditions), a carboxyl group (which is in the deprotonated − COO −
Structure. Crystal data: Spectral data. UV-Vis: IR: NMR: MS ... ^a EINECS for Serine ^a CID 617 from PubChem ^a CID 5951 from PubChem This page was last edited on 12 ...
The triad is located in the active site of the enzyme, where catalysis occurs, and is preserved in all superfamilies of serine protease enzymes. The triad is a coordinated structure consisting of three amino acids: His 57, Ser 195 (hence the name "serine protease") and Asp 102. These three key amino acids each play an essential role in the ...
Sericin is composed of 18 different amino acids, of which 32% is serine. The secondary structure is usually a random coil, but it can also be easily converted into a β-sheet conformation, via repeated moisture absorption and mechanical stretching. The serine hydrogen bonds give its glue-like quality.
The structure is extended with several N-acetyllactosamine repeating sugar units added onto the xylose. This process is unusual and requires specific xylosyltransferases. [ 6 ] Keratan sulphate attaches to a serine or threonine residue through GalNAc, and is extended with two galactose sugars, followed by repeating units of glucuronic acid ...
Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the ...
Model of a phosphorylated serine residue Serine in an amino acid chain, before and after phosphorylation. Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group.
Many serine/threonine protein kinases do not have their own individual EC numbers and use 2.7.11.1, "non-specific serine/threonine protein kinase". This entry is for any enzyme that phosphorylates proteins while converting ATP to ADP (i.e., ATP:protein phosphotransferases.) [10] 2.7.11.37 "protein kinase" was the former generic placeholder and was split into several entries (including 2.7.11.1 ...