7331-08-0

Basic information

• Product Name: O-PHOSPHO-L-SERINE
• CAS NO: 7331-08-0
• Molecular Formula: C3H8NO6P
• Molecular Weight: 0
• Mol File: 7331-08-0.mol
• Article Data: 10

Chemical Properties

• Appearance: /
• CAS DataBase Reference: O-PHOSPHO-L-SERINE(CAS DataBase Reference)
• NIST Chemistry Reference: O-PHOSPHO-L-SERINE(7331-08-0)
• EPA Substance Registry System: O-PHOSPHO-L-SERINE(7331-08-0)

Safety Data

• Hazardous Substances Data: 7331-08-0(Hazardous Substances Data)

Usage

General Description

O-Phospho-L-serine is a chemical compound that is a derivative of the amino acid serine. It is a phosphoserine, where a phosphate group is attached to the hydroxyl group of the serine residue. O-phospho-L-serine is involved in various biological processes, particularly in the regulation of cellular signaling and metabolism. It plays an essential role in the synthesis of phospholipids, which are important components of cell membranes. O-phospho-L-serine also serves as a precursor for the synthesis of other important molecules, such as nucleotides and amino acids. Due to its significance in cellular functions, O-phospho-L-serine is being studied for its potential therapeutic applications in the treatment of various diseases, including neurological disorders and cancer.

Upstream product

• 17885-08-4 O-phospho-DL-serine 
• 3695-66-7 N-(O-phosphono-L-seryl)-L-glutamic acid 
• 1195249-63-8 N-benzyloxycarbonyl-O-diphenoxyphosphoryl-L-serine benzyl ester 
• 112839-94-8 (S)-3-amino-2-oxetanone trifluoroacetic acid salt 
• 56-45-1 L-serin 
• 59-30-3 folate 
• 56-86-0 L-glutamic acid 
• 865-05-4 nicotinamide adenine dinucleotide 
• 144509-68-2 α-ketoglutarate 
• 121656-85-7 N-benzyloxycarbonyl-O-diphenoxyphosphoryl-D-serine benzyl ester 
• 312-84-5 D-Serine 
• 302-84-1 serin 
• 89019-92-1 N-benzyloxycarbonyl-O-diphenoxyphosphoryl-DL-serine benzyl ester 
• 86119-84-8 phosphoric acid 

Downstream Products

• 1637-71-4 S-sulfo-L-cysteine 

Relevant articles and documents

Library Selection with a Randomized Repertoire of (βα)8-Barrel Enzymes Results in Unexpected Induction of Gene Expression

The potential of the frequently encountered (βα)8-barrel fold to acquire new functions was tested by an approach combining random mutagenesis and selection in vivo. For this purpose, the genes encoding 52 different phosphate-binding (βα)8-barrel proteins were subjected to error-prone PCR and cloned into an expression plasmid. The resulting mixed repertoire was used to transform different auxotrophic Escherichia coli strains, each lacking an enzyme with a phosphate-containing substrate. After plating of the different transformants on minimal medium, growth was observed only for two strains, lacking either the gene for the serine phosphatase SerB or the phosphoserine aminotransferase SerC. The same mutants of the E. coli genes nanE (encoding a putative N-acetylmannosamine-6-phosphate 2-epimerase) and pdxJ (encoding the pyridoxine 5′-phosphate synthase) were responsible for rescuing both ΔserB and ΔserC. Unexpectedly, the complementing NanE and PdxJ variants did not catalyze the SerB or SerC reactions in vitro. Instead, RT-qPCR, RNAseq, and transcriptome analysis showed that they rescue the deletions by enlisting the help of endogenous E. coli enzymes HisB and HisC through exclusive up-regulation of histidine operon transcription. While the promiscuous SerB activity of HisB is well-established, our data indicate that HisC is promiscuous for the SerC reaction, as well. The successful rescue of ΔserB and ΔserC through point mutations and recruitment of additional amino acids in NanE and PdxJ provides another example for the adaptability of the (βα)8-barrel fold.

Elucidation of a Self-Sustaining Cycle in Escherichia coli l -Serine Biosynthesis That Results in the Conservation of the Coenzyme, NAD+

The equilibrium of the reaction catalyzed by d-3-phosphoglycerate dehydrogenase (PGDH), the first enzyme in the l-serine biosynthetic pathway, is far in the direction away from serine synthesis. As such, the enzyme is usually assayed in this direction. To

Metal Nanoparticles

A metal nanoparticle-phosphopeptide complex comprising a metal nanoparticle and a phosphopeptide is provided. The phosphopeptide comprises two or more contiguous peptide motifs and two or more phosphorus-containing groups capable of interacting with the surface of the metal nanoparticle. The amino acids at the equivalent position in each peptide motif have similar structural and/or electronic properties. Each phosphorus-containing group is bound to an amino acid in the two or more contiguous peptide motifs. Methods for preparing the metal nanoparticle-phosphopeptide complex are also provided.