Rafik Hariri philanthropic and developmental contributions are countless. The most remarkable being the multifaceted support to educate more than 36,000 Lebanese university students within Lebanon, and beyond.
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INHIBITION AND INACTIVATION OF HYDROLASES
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Mohammed Taleb H. AKSAMAWATY
|
Univ. |
Bristol |
Spéc. |
Organic Chemistry |
Deg. |
Year |
# Pages |
|
Ph.D. |
1989 |
113 |
The Synthesis of 1,4-dideoxy-1,4-imino-L-threitol has been improved. Compound has been tested together with 1,4-dideoxy-1,4-imino-L-arabinitol as inhibitors of α-L-arabinofuranosidase AFIII of Monilinia Fructigena. Both compounds were competitive inhibitors of AFIII. 1,4-dideoxy-1,4-imino-L-arabinitol was approximately 1200 fold tighter binding than the 1,4-dideoxy-1,4-imino-L-threitol.
The pH variation of the affinity (1/Kj) of both compounds, with dissociation constant, pKa, well above that of the acid catalytic group of the enzyme, were not likely to be transition state analogues for the α -L-arabinofuranosidase.
Aryl and Alkyl n-butyl ethyl diazoacetato borinate derivatives were synthesized as inactivators of serine proteases. Attempted inactivation of α-chymotrypsin by phenyl n-butyl ethyl diazoacetato borinate was not successful and the compound decomposed with the time of addition.
Attempted acid catalyzed enzyme catalyzed hydrolysis of n-butyl ethyl diazoacetato borinate was not successful. Decomposition of the compound occurred very quickly. n-Butyl ethyl diazoacetato borinates were air and moisture sensitive and thermally unstable compounds.
