S4503
DL-Serine hydroxamate
≥97% (TLC), suitable for ligand binding assays
Synonym(s):
SHX
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About This Item
Empirical Formula (Hill Notation):
C3H8N2O3
CAS Number:
Molecular Weight:
120.11
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
MDL number:
Product Name
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
Related Categories
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
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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Yu Zeng et al.
Antimicrobial agents and chemotherapy, 53(11), 4619-4627 (2009-09-02)
The Trojan horse antibiotic albomycin, produced by Streptomyces sp. strain ATCC 700974, contains a thioribosyl nucleoside moiety linked to a hydroxamate siderophore through a serine residue. The seryl nucleoside structure (SB-217452) is a potent inhibitor of seryl-tRNA synthetase (SerRS) in
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
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
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
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