Page last updated: 2024-12-07

serine hydroxamate

Description Research Excerpts Clinical Trials Roles Classes Pathways Study Profile Bioassays Related Drugs Related Conditions Protein Interactions Research Growth Market Indicators

Description

Serine hydroxamates are potent inhibitors of serine hydrolases, a large and diverse family of enzymes that play crucial roles in a wide range of biological processes. They are often synthesized by reacting a serine derivative with hydroxylamine under appropriate conditions. The hydroxamate moiety acts as a transition state analog, mimicking the tetrahedral intermediate formed during the enzymatic reaction, and thus, effectively blocking the active site of the enzyme. This inhibition can lead to various effects depending on the specific enzyme targeted, including modulation of inflammation, regulation of lipid metabolism, and interference with bacterial growth. Due to their broad spectrum of biological activity, serine hydroxamates have become a focus of research in various fields, including drug discovery, chemical biology, and medicinal chemistry. They hold promise as potential therapeutic agents for treating a variety of diseases, ranging from cancer to infectious diseases.'

serine hydroxamate: RN given refers to (L)-isomer [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

serine hydroxamate : A hydroxamic acid obtained by formal condensation of the carboxy group of serine with the amino group of hydroxylamine. [Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res]

Cross-References

ID SourceID
PubMed CID101173
CHEMBL ID568191
CHEBI ID75494
SCHEMBL ID2484491
MeSH IDM0090565

Synonyms (23)

Synonym
4370-83-6
nsc517349
nsc-517349
dl-serine hydroxamate, seryl-trna synthetase inhibitor
serine hydroxamate
2-amino-n,3-dihydroxypropanamide
chebi:75494 ,
CHEMBL568191
AKOS006375343
propanamide, 2-amino-n,3-dihydroxy-
n-hydroxyserinamide
(+-)-serine hydroxamate
nsc 517349
55779-32-3
dl-serine hydroxamate
SCHEMBL2484491
dl-serine hydroxa-mate
amino acid hydroxamates dl-serine hydroxamate
Q27145350
propanamide, 2-amino-n,3-dihydroxy-, (a+/-)-
DTXSID301301599
CS-0142371
HY-131894

Research Excerpts

[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Roles (1)

RoleDescription
EC 6.1.1.11 (serine--tRNA ligase) inhibitorAn EC 6.1.1.* (ligases forming aminoacyl tRNA and related compounds) inhibitor that specifically inhibits the action of seryl-tRNA synthetase (EC 6.1.1.11).
[role information is derived from Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res]

Drug Classes (2)

ClassDescription
hydroxamic acidA compound, RkE(=O)lNHOH, derived from an oxoacid RkE(=O)l(OH) (l =/= 0) by replacing -OH with -NHOH, and derivatives thereof. Specific examples of hydroxamic acids are preferably named as N-hydroxy amides.
serine derivativeAn amino acid derivative resulting from reaction of serine at the amino group or the carboxy group, or from the replacement of any hydrogen of serine by a heteroatom. The definition normally excludes peptides containing serine residues.
[compound class information is derived from Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res]

Bioassays (3)

Assay IDTitleYearJournalArticle
AID443633Inhibition of mouse recombinant serine racemase expressed in Escherichia coli MC1061 assessed as formation of D-serine at 5 mM after 30 mins by HPLC analysis2009Journal of medicinal chemistry, Oct-08, Volume: 52, Issue:19
Hydroxamic acids as a novel family of serine racemase inhibitors: mechanistic analysis reveals different modes of interaction with the pyridoxal-5'-phosphate cofactor.
AID443654Binding affinity to pyridoxal-5'-phosphate assessed as formation of PLP-aldimine at active site by ESI-MS analysis2009Journal of medicinal chemistry, Oct-08, Volume: 52, Issue:19
Hydroxamic acids as a novel family of serine racemase inhibitors: mechanistic analysis reveals different modes of interaction with the pyridoxal-5'-phosphate cofactor.
AID443653Binding affinity to 30 mM pyridoxal-5'-phosphate assessed as formation of PLP-aldimine by ESI-MS analysis2009Journal of medicinal chemistry, Oct-08, Volume: 52, Issue:19
Hydroxamic acids as a novel family of serine racemase inhibitors: mechanistic analysis reveals different modes of interaction with the pyridoxal-5'-phosphate cofactor.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (39)

TimeframeStudies, This Drug (%)All Drugs %
pre-19904 (10.26)18.7374
1990's11 (28.21)18.2507
2000's16 (41.03)29.6817
2010's8 (20.51)24.3611
2020's0 (0.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 24.36

According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be moderate demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index24.36 (24.57)
Research Supply Index3.71 (2.92)
Research Growth Index4.74 (4.65)
Search Engine Demand Index26.67 (26.88)
Search Engine Supply Index2.00 (0.95)

This Compound (24.36)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews0 (0.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other40 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]