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Drug-Target Interaction

Drug

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PubChem ID:7516
Structure:
Synonyms:
1-PHENYLHYDRAZINE
100-63-0
2545-79-1
2545-79-1 (monosulfate)
27140-08-5
27140-08-5 (hydrochloride)
4-15-00-00050 (Beilstein Handbook Reference)
59-88-1
59-88-1 (mono-hydrochloride)
78670_FLUKA
78672_FLUKA
AB1003540
AC1L1OXS
AC1Q5536
AG-D-06072
AI3-15399
AKOS000268993
BB_SC-6741
BIDD:ER0251
BRN 0606080
C02304
CCRIS 511
CHEBI:27924
CHEMBL456807
EINECS 202-873-5
Fenilidrazina
Fenilidrazina [Italian]
Fenylhydrazine
Fenylhydrazine [Dutch]
HSDB 1117
Hydrazine, phenyl-
HYDRAZINE,PHENYL
Hydrazine-benzene
Hydrazinobenzene
Hydrazobenzene
I01-1976
LS-7655
MolPort-000-872-047
Monophenylhydrazine
NCGC00159378-02
NCGC00159378-03
NCGC00159378-04
NCGC00159378-05
NCGC00159378-06
P0183
P26252_ALDRICH
Phenyldiazane
Phenylhydrazin
Phenylhydrazin [German]
Phenylhydrazine
Phenylhydrazine and its salts
Phenylhydrazine [UN2572] [Poison]
Phenylhydrazine [UN2572] [Poison]
PHZ
ST5214481
UN2572
ZINC00388099

Target

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Uniprot ID:A4TB13_MYCGI
Synonyms:
Amine oxidase (Copper-containing)
EC-Numbers:1.4.3.6
Organism:Mycobacterium flavescens (strain ATCC 700033 / PYR-GCK
Mycobacterium gilvum
strain PYR-GCK
PDB IDs:-

Binding Affinities:

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

References:

8694842
Inhibition of bovine lung semicarbazide-sensitive amine oxidase (SSAO) by some hydrazine derivatives.. J M Lizcano; A FernŠndez de Arriba; K F Tipton; M Unzeta (1996) Biochemical pharmacology display abstract
Microsomal semicarbazide-sensitive amine oxidase (SSAO) from bovine lung was shown to be inhibited by a number of hydrazine derivatives, but the mechanisms of inhibition were found to differ. Hydralazine behaved as an irreversible and partially time-dependent inhibitor with an IC50 value of 1 microM under the conditions used. Phenylhydrazine was found to be a potent irreversible inhibitor of SSAO (IC50 30 nM). Semicarbazide behaved as a specific irreversible inhibitor (active-site-directed irreversible inhibitor) in first forming a non-covalent enzyme-semicarbazide complex (with a Ki value of 85 microM), which then reacted to give an irreversibly inhibited enzyme species in a reaction defined by the first-order rate constant k2 = 0.065 min-1. Phenelzine behaved as a reversible inhibitor, but dialysis at 37 degrees C was found to be necessary to obtain full recovery of enzyme activity. The dependence of inhibition on phenelzine concentration was complex and consistent with multiple binding sites for this inhibitor. This diversity in the action of a family of compounds with the same functional group must be taken into account in attempts to design more specific inhibitors of this enzyme.