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Merck
CN

P1053

O-Phospho-L-threonine

≥98.0% (TLC)

Synonym(s):

(S)-2-Amino-3-hydroxybutanoic acid 3-phosphate, L-Threonine O-phosphate

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About This Item

Empirical Formula (Hill Notation):
C4H10NO6P
CAS Number:
Molecular Weight:
199.10
PubChem Substance ID:
eCl@ss:
32160406
UNSPSC Code:
12352209
EC Number:
214-217-5
MDL number:
Beilstein/REAXYS Number:
1727078
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Product Name

O-Phospho-L-threonine,

InChI key

USRGIUJOYOXOQJ-GBXIJSLDSA-N

InChI

1S/C4H10NO6P/c1-2(3(5)4(6)7)11-12(8,9)10/h2-3H,5H2,1H3,(H,6,7)(H2,8,9,10)/t2-,3+/m1/s1

SMILES string

C[C@@H](OP(O)(O)=O)[C@H](N)C(O)=O

assay

≥98.0% (TLC)

form

powder

color

white

storage temp.

−20°C

Quality Level

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Biochem/physiol Actions

O-Phospho-L-threonine is an amino acid derivative.

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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H Christian Reinhardt et al.
Nature reviews. Molecular cell biology, 14(9), 563-580 (2013-08-24)
Coordinated progression through the cell cycle is a complex challenge for eukaryotic cells. Following genotoxic stress, diverse molecular signals must be integrated to establish checkpoints specific for each cell cycle stage, allowing time for various types of DNA repair. Phospho-Ser/Thr-binding
Alzbeta Trancikova et al.
PloS one, 7(10), e47784-e47784 (2012-10-20)
Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene are a common cause of autosomal dominant familial Parkinson's disease (PD). LRRK2 encodes a multi-domain protein containing GTPase and kinase enzymatic domains. Disease-associated mutations in LRRK2 variably influence enzymatic activity with
Daniel Feltrin et al.
PLoS biology, 10(12), e1001439-e1001439 (2012-12-12)
Local mRNA translation in neurons has been mostly studied during axon guidance and synapse formation but not during initial neurite outgrowth. We performed a genome-wide screen for neurite-enriched mRNAs and identified an mRNA that encodes mitogen-activated protein kinase kinase 7
Dennis Wong et al.
Scientific reports, 8(1), 155-155 (2018-01-11)
Protein phosphorylation plays a key role in Mycobacterium tuberculosis (Mtb) physiology and pathogenesis. We have previously shown that a secreted protein tyrosine phosphatase, PtpA, is essential for Mtb inhibition of host macrophage acidification and maturation, and is a substrate of
Christian B Oehlenschlæger et al.
Frontiers in plant science, 8, 2005-2005 (2017-12-13)
PSY1R is a leucine-rich repeat (LRR) receptor-like kinase (RLK) previously shown to act as receptor for the plant peptide hormone PSY1 (peptide containing sulfated tyrosine 1) and to regulate cell expansion. PSY1R phosphorylates and thereby regulates the activity of plasma

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