S4503
DL-Serine hydroxamate
≥97% (TLC), suitable for ligand binding assays
Synonyme(s) :
SHX
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A propos de cet article
Formule empirique (notation de Hill) :
C3H8N2O3
Numéro CAS:
Poids moléculaire :
120.11
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
MDL number:
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Laissez-nous vous aiderNom du produit
DL-Serine hydroxamate, seryl-tRNA synthetase inhibitor
SMILES string
NC(CO)C(=O)NO
InChI
1S/C3H8N2O3/c4-2(1-6)3(7)5-8/h2,6,8H,1,4H2,(H,5,7)
InChI key
LELJBJGDDGUFRP-UHFFFAOYSA-N
assay
≥97% (TLC)
form
powder
technique(s)
ligand binding assay: suitable
color
white to off-white
application(s)
cell analysis
storage temp.
−20°C
Quality Level
Catégories apparentées
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.
Biochem/physiol Actions
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.
Classe de stockage
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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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
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
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
Daniel J Ferullo et al.
PLoS genetics, 4(12), e1000300-e1000300 (2008-12-17)
The bacterial stringent response, triggered by nutritional deprivation, causes an accumulation of the signaling nucleotides pppGpp and ppGpp. We characterize the replication arrest that occurs during the stringent response in Escherichia coli. Wild type cells undergo a RelA-dependent arrest after
B Belitsky et al.
The Journal of biological chemistry, 257(9), 4677-4679 (1982-05-10)
Lack of three different amino acids or treatment with the analogue DL-serine hydroxamate does not induce the accumulation of ppGpp and pppGpp, the 3'-pyrophosphates of GDP and GTP, respectively, in Rhizobium meliloti strain 41. Surprisingly, RNA accumulation is controlled under
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