S4503
DL-Serine hydroxamate
≥97% (TLC), suitable for ligand binding assays
Synonym(s):
SHX
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All Photos(3)
About This Item
Empirical Formula (Hill Notation):
C3H8N2O3
CAS Number:
Molecular Weight:
120.11
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
Recommended Products
product name
DL-Serine hydroxamate, seryl-tRNA synthetase inhibitor
Assay
≥97% (TLC)
form
powder
technique(s)
ligand binding assay: suitable
color
white to off-white
application(s)
cell analysis
storage temp.
−20°C
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
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.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
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
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
Dao Nguyen et al.
Science (New York, N.Y.), 334(6058), 982-986 (2011-11-19)
Bacteria become highly tolerant to antibiotics when nutrients are limited. The inactivity of antibiotic targets caused by starvation-induced growth arrest is thought to be a key mechanism producing tolerance. Here we show that the antibiotic tolerance of nutrient-limited and biofilm
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