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Only the L-stereoisomer appears naturally in proteins. It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine. Serine was first obtained from silk protein, a particularly rich source, in 1865 by Emil Cramer. [5] Its name is derived from the Latin for silk, sericum. Serine's structure ...
In enzymology, a serine—tRNA ligase (EC 6.1.1.11) is an enzyme that catalyzes the chemical reaction. ATP + L-serine + tRNASer AMP + diphosphate + L-seryl-tRNASer. The 3 substrates of this enzyme are ATP, L-serine, and tRNA(Ser), whereas its 3 products are AMP, diphosphate, and L-seryl-tRNA(Ser).
3-Phosphoglycerate dehydrogenase catalyzes the transition of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the committed step in the phosphorylated pathway of L-serine biosynthesis. It is also essential in cysteine and glycine synthesis, which lie further downstream. [7]
The phosphorylation of the alcohol functional group in serine to produce phosphoserine is catalyzed by various types of kinases. [2] [3] Through the use of technologies that utilize an expanded genetic code, phosphoserine can also be incorporated into proteins during translation. [4] [5] [6] It is a normal metabolite found in human biofluids. [7]
Serine C-palmitoyltransferase is expressed in a large number of species from bacteria to humans. The bacterial enzyme is a water-soluble homodimer [2] whereas in eukaryotes the enzyme is a heterodimer which is anchored to the endoplasmic reticulum. [3] Humans and other mammals express three paralogous subunits SPTLC1, SPTLC2, and SPTLC3.
Serine dehydratase has also been found to be absent in human colon carcinoma and rat sarcoma. The observed enzyme imbalance in these tumors shows that an increased capacity for the synthesis of serine is coupled to its utilization for nucleotide biosynthesis as a part of the commitment to cellular replication in cancer cells.
The synthesis of aspartate kinase (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids, is feed-back inhibited by lysine, isoleucine, and threonine, which prevents the synthesis of the amino acids derived from aspartate. So, in addition to inhibiting the first enzyme of the aspartate ...
In enzymology, a serine-pyruvate transaminase (EC 2.6.1.51) is an enzyme that catalyzes the chemical reaction. L-serine + pyruvate 3-hydroxypyruvate + L-alanine. Thus, the two substrates of this enzyme are L-serine and pyruvate, whereas its two products are 3-hydroxypyruvate and L-alanine.