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ChemicalBook--->CAS DataBase List--->519170-13-9

519170-13-9

519170-13-9 Structure

519170-13-9 Structure
IdentificationBack Directory
[Name]

OU749
[CAS]

519170-13-9
[Synonyms]

OU749
N-[5-(4-Methoxybenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
Benzenesulfonamide, N-[5-[(4-methoxyphenyl)methyl]-1,3,4-thiadiazol-2-yl]-
[Molecular Formula]

C16H15N3O3S2
[MDL Number]

MFCD03351667
[MOL File]

519170-13-9.mol
[Molecular Weight]

361.44
Chemical PropertiesBack Directory
[storage temp. ]

2-8°C
[solubility ]

DMSO: >20mg/mL
[form ]

solid
[color ]

white to off-white
Safety DataBack Directory
[Symbol(GHS) ]


GHS07
[Signal word ]

Warning
[Hazard statements ]

H302
[Precautionary statements ]

P264-P270-P301+P312-P330-P501
[Hazard Codes ]

Xn
[Risk Statements ]

22
Hazard InformationBack Directory
[Uses]

OU749 is a potent γ-glutamyl transpeptidase (GGT) inhibitor with a Ki value of 17.6 μM. OU749 shows cytotoxicity[1].
[Biological Activity]

ou749 is a competitive inhibitor of γ-glutamyl transpeptidase (ggt) [1].expression of γ-glutamyl transpeptidase (ggt) in tumors contributes to the resistance to radiation and chemotherapy. ggt is inhibited by glutamine analogues which compete with the substrate for the γ-glutamyl binding site [1].ou749 inhibited human kidney ggt with an intrinsic ki of 17.6 m [1]. in 786-o cells, a human renal tumor cell line, ou749 showed more than 150-fold less toxic than the ggt inhibitor acivicin toward dividing cells. ou749 inhibited ggt isolated from human kidney in a dose-dependent manner [1]. ou749 was 7-fold less potent as inhibitor of ggt isolated from rat kidney and 10-fold less potent inhibiting ggt from mouse kidney [1]. ou749 did not inhibit degradation of glutathione by ggt from rat kidney. inhibition of ggt by ou749 is species-specific [1]. ou749 showed no inhibitory effect on ggt from pig cells. ou749 inhibited human ggt expressed in mouse fibroblasts by a similar extent to the ggt from human cells, indicated that the species specificity was determined by differences in the primary structure of the protein rather than species-specific, post-translational modifications [1].
[References]

[1] king j b, west m b, cook p f, et al. a novel, species-specific class of uncompetitive inhibitors of γ-glutamyl transpeptidase[j]. journal of biological chemistry, 2009, 284(14): 9059-9065.
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