407-41-0

Basic information

• Product Name: O-Phospho-L-serine
• Synonyms: L-O-PHOSPHOSERINE;L-SERINE-O-PHOSPHATE;L-PHOSPHOSERINE;H-SER(PO3H2)-OH;PHOSPHATIDYLETHANOLAMINE(EGG)(RG);O-Phosho-L-serine;O-Phosphorylserine;Phospho-L-serine
• CAS NO: 407-41-0
• Molecular Formula: C₃H₈NO₆P
• Molecular Weight: 185.07
• EINECS: 206-986-0
• Product Categories: Amino Acids;Biochemistry;Biological-modified Amino Acids;Glutamate receptor
• Mol File: 407-41-0.mol
• Article Data: 9

Chemical Properties

• Melting Point: 190 °C(lit.)
• Boiling Point: 475.4 °C at 760 mmHg
• Flash Point: 241.3 °C
• Appearance: White/Crystalline Powder
• Density: 1.809 g/cm³
• Vapor Pressure: 2.4E-10mmHg at 25°C
• Storage Temp.: Store at 0°C
• Solubility: H2O: 50 mg/mL hot, clear, colorless to slightly yellow
• PKA: pK1:2.08;pK2:5.65;pK3:9.74 (25°C)
• Water Solubility: 28.34g/L at 20℃
• Merck: 14,7363
• BRN: 1726826
• CAS DataBase Reference: O-Phospho-L-serine(CAS DataBase Reference)
• NIST Chemistry Reference: O-Phospho-L-serine(407-41-0)
• EPA Substance Registry System: O-Phospho-L-serine(407-41-0)

Safety Data

• Hazard Codes: Xn
• Statements: 21/22
• Safety Statements: 36/37
• RIDADR: UN 3261 8 / PGII
• WGK Germany: 3
• F: 10
• Hazardous Substances Data: 407-41-0(Hazardous Substances Data)

Usage

Description

O-Phospho-L-Serine is an agonist of the group III metabotropic glutamate receptors mGluR4a and mGluR6 (EC50s = 2-5 μM). It mimics the phosphatidylserine head group and has been shown to inhibit the proliferation of microglia and to enhance neuronal differentiation of progenitor cells.

Chemical Properties

White powder

Uses

Different sources of media describe the Uses of 407-41-0 differently. You can refer to the following data:
1. roborant
2. L-O-Phosphoserine is the catalytic domain of human protein kinase C β II when complexed with a malemide inhibitor. It is also used in the purification of the Epstein-Barr virus nuclear antigen 2A.
3. O-Phospho-L-Serine is an agonist of the group III metabotropic glutamate receptors mGluR4a and mGluR6 (EC50s = 2-5 μM). It mimics the phosphatidylserine head group and has been shown to inhibit the proliferation of microglia and to enhance neuronal differentiation of progenitor cells.

General Description

Monoclonal Anti-Phosphoserine (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse.

Flammability and Explosibility

Notclassified

Biological Activity

Group III metabotropic glutamate receptor agonist; analog of L-AP4 (L-(+)-2-Amino-4-phosphonobutyric acid ). Inhibits proliferation and enhances neuronal differentiation in progenitor cells.

Biochem/physiol Actions

Protein phosphorylation and dephosphorylation are basic signaling mechanisms that modify protein function in eukaryotic cells. Phosphorylation is a rare posttranslational event in normal tissues, however, the abundance of phosphorylated cellular proteins increases several folds following various activation processes. The main amino acids that are phosphorylated are tyrosine, serine, or threonine (pTyr/pSer/pThr), each having specific kinases that phosphorylate them and specific phosphatases that dephosphorylate them. Mono and polyclonal antibodies directed against phosphorylated residues were generated and found useful as analytical and preparative tools by enabling the identification, quantification, and immunoaffinity isolation of phosphorylated cellular proteins.

Purification Methods

Recrystallise the phospho-serine by dissolving 10g in H2O (150mL) at 25o, stirring for up to 20minutes. Undissolved material is filtered off (Büchner), and 95% EtOH (85mL) is added dropwise during 4minutes, and set aside at 25o for 3hours, then at 3o overnight. The crystals are washed with 95% EtOH (100mL), then dry Et2O (50mL), and dried in a vacuum (yield 6.5g). A further quantity (1.5g) can be obtained by keeping the mother liquors and washings at -10o for 1 week. The DL-isomer has m 167-170o(dec) after recrystallisation from H2O/EtOH or MeOH. [Neuhaus & Korkes Biochemical Preparations 6 75 1958, Neuhaus & Byrne J Biol Chem 234 113 1959, IR: F.lsch & Mellander Acta Chem Scand 11 1232 1957, Beilstein 4 IV 3120.]

InChI:InChI=1/C3H8NO6P/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H2,7,8,9)/p-2/t2-/m0/s1

Upstream product

• 17885-08-4 O-phospho-DL-serine 
• 3913-50-6 hydroxypyruvic acid phosphate 
• 56-45-1 L-serin 
• 56-65-5 ATP 
• 56-86-0 L-glutamic acid 
• 865-05-4 nicotinamide adenine dinucleotide 
• 144509-68-2 α-ketoglutarate 
• 59-30-3 folate 
• 158171-14-3 (S)-3-(Benzyloxy-hydroxy-phosphoryloxy)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionic acid 
• 112839-94-8 (S)-3-amino-2-oxetanone trifluoroacetic acid salt 
• 1195249-63-8 N-benzyloxycarbonyl-O-diphenoxyphosphoryl-L-serine benzyl ester 
• 3695-66-7 N-(O-phosphono-L-seryl)-L-glutamic acid 

Downstream Products

• 56-41-7 C₃H₆NO₂*H⁽¹⁺⁾ 
• 56-88-2 L-cystathionine 
• 14066-20-7 dihydrogen phosphate 
• 498-40-8 L-Cysteic acid 
• 2936-69-8 S-(2-aminoethyl)-L-cysteine 
• 1023971-15-4 Fudosteine 
• 1637-71-4 S-sulfo-L-cysteine 
• 73243-10-4 S-(4-hydroxyphenyl)-L-cysteine 
• 4819-36-7 (S)-β-triazolylalanine 
• 405150-23-4 S-thienyl-L-cysteine 
• 405150-20-1 S-(2-thiazolyl)-L-cysteine 
• 60115-34-6 S-(2-aminophenyl)-L-cysteine 
• 5463-52-5 S-(4-methylphenyl)-cysteine 
• 55288-30-7 S-(4-nitrophenyl)-L-cysteine 

Relevant articles and documents

SbnI is a free serine kinase that generates O-phospho-L-serine for staphyloferrin B biosynthesis in Staphylococcus aureus

Staphyloferrin B (SB) is an iron-chelating siderophore produced by Staphylococcus aureus in invasive infections. Proteins for SB biosynthesis and export are encoded by the sbnABCDEFGHI gene cluster, in which SbnI, a member of the ParB/Srx superfamily, acts as a heme-dependent transcriptional regulator of the sbn locus. However, no structural or functional information about SbnI is available. Here, a crystal structure of SbnI revealed striking structural similarity to an ADP-dependent free serine kinase, SerK, from the archaea Thermococcus kodakarensis. We found that features of the active sites are conserved, and biochemical assays and31P NMR and HPLC analyses indicated that SbnI is also a free serine kinase but uses ATP rather than ADP as phosphate donor to generate the SB precursor O-phospho- L-serine (OPS). SbnI consists of two domains, and elevated B-factors in domain II were consistent with the open-close reaction mechanism previously reported for SerK. Mutagenesis of Glu20 and Asp58 in SbnI disclosed that they are required for kinase activity. The only known OPS source in bacteria is through the phosphoserine aminotransferase activity of SerC within the serine biosynthesis pathway, and we demonstrate that an S. aureus serC mutant is a serine auxotroph, consistent with a function in L-serine biosynthesis. However, the serC mutant strain could produce SB when provided L-serine, suggesting that SbnI produces OPS for SB biosynthesis in vivo. These findings indicate that besides transcriptionally regulating the sbn locus, SbnI also has an enzymatic role in the SB biosynthetic pathway.

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.

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.