Home
Drugs
Targets
Pathways
Ontologies
Cyp450s
Adv.search
Help/FAQ

Drug-Target Interaction

Drug

show drug details
PubChem ID:5139
Structure:
Synonyms:
1071-37-0
1071-37-0 (mono-hydrobromide)
161722-89-0
2-Ethyl-2-thiopseudourea
2-Ethyl-2-thiopseudourea hydrobromide
2986-20-1
625-53-6
AC1L1JOU
AC1Q1UA8
AR-1E1436
Carbamimidothioic acid, ethyl ester
CCG-204582
CHEBI:275077
CHEBI:43633
CHEMBL321691
DB02234
DB02539
ethyl carbamimidothioate
ethyl imidothiocarbamate
ETHYLISOTHIOUREA
ethylsulfanylmethanimidamide
ethyron
etiron
HSCI1_000396
ITU
Lopac-E-3149
Lopac0_000491
NCGC00015407-01
NCGC00015407-02
NCGC00015407-03
NCGC00015407-04
NCGC00024835-01
NCGC00024835-02
Pseudourea, 2-ethyl-2-thio-
s-Ethyl isothiouronium bromide
S-Ethylisothiourea
S-Ethylisothiourea hydrobromide
S09-0122
SBB069241
SEU
STK370557
Tocris-0873
ZINC03806245

Target

show target details
Uniprot ID:Q62710_RAT
Synonyms:
Nitric oxide synthase
EC-Numbers:-
Organism:Rat
Rattus norvegicus
PDB IDs:-

Binding Affinities:

Ki: Kd:Ic 50:Ec50/Ic50:
----

References:

9576868
Nitroarginine and tetrahydrobiopterin binding to the haem domain of neuronal nitric oxide synthase using a scintillation proximity assay.. W K Alderton; A Boyhan; P N Lowe (1998) The Biochemical journal display abstract
Nitric oxide synthases (NOS) have a bidomain structure comprised of an N-terminal oxygenase domain and a C-terminal reductase domain. The oxygenase domain binds haem, (6R)-5,6,7,8-tetrahydro-l-biopterin (tetrahydrobiopterin) and arginine, is the site where nitric oxide synthesis takes place and contains determinants for dimeric interactions. A novel scintillation proximity assay has been established for equilibrium and kinetic measurements of substrate, inhibitor and cofactor binding to a recombinant N-terminal haem-binding domain of rat neuronal NOS (nNOS). Apparent Kd values for nNOS haem-domain-binding of arginine and Nomega-nitro-L-arginine (nitroarginine) were measured as 1.6 microM and 25 nM respectively. The kinetics of [3H]nitroarginine binding and dissociation yielded an association rate constant of 1.3x10(4) s-1.M-1 and a dissociation rate constant of 1.2x10(-4) s-1. These values are comparable to literature values obtained for full-length nNOS, suggesting that many characteristics of the arginine binding site of NOS are conserved in the haem-binding domain. Additionally, apparent Kd values were compared and were found to be similar for the inhibitors, L-NG-monomethylarginine, S-ethylisothiourea, N-iminoethyl-L-ornithine, imidazole, 7-nitroindazole and 1400W (N-[3-(aminomethyl) benzyl] acetamidine). [3H]Tetrahydrobiopterin bound to the nNOS haem domain with an apparent Kd of 20 nM. Binding was inhibited by 7-nitroindazole and stimulated by S-ethylisothiourea. The kinetics of interaction with tetrahydrobiopterin were complex, showing a triphasic binding process and a single off rate. An alternating catalytic site mechanism for NOS is proposed.