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S4503

Sigma-Aldrich

DL-Serine hydroxamate

≥97% (TLC), suitable for ligand binding assays

Synonyme(s) :

SHX

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About This Item

Formule empirique (notation de Hill):
C3H8N2O3
Numéro CAS:
Poids moléculaire :
120.11
Numéro MDL:
Code UNSPSC :
12352209
ID de substance PubChem :
Nomenclature NACRES :
NA.26

product name

DL-Serine hydroxamate, seryl-tRNA synthetase inhibitor

Pureté

≥97% (TLC)

Forme

powder

Technique(s)

ligand binding assay: suitable

Couleur

white to off-white

Application(s)

cell analysis

Température de stockage

−20°C

Chaîne SMILES 

NC(CO)C(=O)NO

InChI

1S/C3H8N2O3/c4-2(1-6)3(7)5-8/h2,6,8H,1,4H2,(H,5,7)

Clé InChI

LELJBJGDDGUFRP-UHFFFAOYSA-N

Application

Serine has been used as an inhibitor of seryl-tRNA synthetase. DL-Serine hydroxamate is used to induce metabolic synthesis of guanosine 3′-diphosphate 5′-diphosphate (ppGpp) in E. coli by amino acid starvation. It is also used to synchronize cell cycle in E. coli cultures by inhibition of tRNA charging.

Actions biochimiques/physiologiques

Serine is involved in the one-carbon unit metabolism. It is associated with the biosynthesis of cysteine, ceramide, phosphatidylserine, purine and pyrimidine. In bacteria, it participates in tryptophan synthesis. Gluconeogenesis, one of the important biochemical processes, involves serine, particularly in ruminants. Protein phosphorylation is one such event that utilizes serine. Glycine, a metabolic product of serine, serves as an antioxidant and a neurotransmitter. D-serine is known to activate the N-methyl-D-aspartate (NMDA) receptors of the brain. Serine hydroxamate, a structural analogue of serine prevents seryl-tRNA (transfer ribonucleic acid) charging and thereby decreases phospholipid and nucleic acid synthesis in Escherichia coli.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

C van Delden et al.
Journal of bacteriology, 183(18), 5376-5384 (2001-08-22)
During nutrient starvation, Escherichia coli elicits a stringent response involving the ribosome-associated protein RelA. Activation of RelA results in a global change in the cellular metabolism including enhanced expression of the stationary-phase sigma factor RpoS. In the human pathogen Pseudomonas
D Riesenberg et al.
Journal of general microbiology, 130(10), 2549-2558 (1984-10-01)
The accumulation of RNA and protein and the kinetics of nucleoside triphosphate and guanosine polyphosphate pools during amino acid starvation and carbon source downshift were investigated in Streptomyces hygroscopicus. RNA accumulation was controlled stringently during both amino acid starvation and
M P Patricelli et al.
Proteomics, 1(9), 1067-1071 (2002-05-07)
The field of biochemistry is currently faced with the enormous challenge of assigning functional significance to more than thirty thousand predicted protein products encoded by the human genome. In order to accomplish this daunting task, methods will be required that
David L Erickson et al.
Infection and immunity, 72(10), 5638-5645 (2004-09-24)
The stringent response is a mechanism by which bacteria adapt to nutritional deficiencies through the production of the guanine nucleotides ppGpp and pppGpp, produced by the RelA enzyme. We investigated the role of the relA gene in the ability of
H J Cha et al.
Applied and environmental microbiology, 65(2), 409-414 (1999-01-30)
We constructed and characterized three stress probe plasmids which utilize a green fluorescent protein as a noninvasive reporter in order to elucidate Escherichia coli cellular stress responses in quiescent or resting cells. Cellular stress levels were easily detected by fusing

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