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W Suttimool

Publications and source records attributed to W Suttimool.

3 recordsLinked to original sources
PubMed1982

Synthesis of omega-(4-aminophenylsulfonamido)alkyl disulfides and thiosulfates and their activity against dihydropteroate synthetase from sulfanilamide-resistant Neisseria gonorrhoeae.

A series of omega-(4-aminophenylsulfonamido)alkyl disulfides and omega-(4-aminophenylsulfonamido)alkanethiosulfates was synthesized from the reaction of p-acetamidobenzenesulfanilyl chloride and either the aminoalkyl disulfide dihydrobromide or the aminoalkyl bromide hydrobromide followed by sodium thiosulfate. Several of the compounds showed inhibitory activity against dihydropteroate synthetase isolated from a sulfanilamide-resistant strain of Neisseria gonorrhoeae of the same order of activity as that of sulfanilamide. An increase in the hydrophobic nature of the sulfanilamide structure did not increase inhibitory activity against this enzyme.

Chemical Phenomena↗
PubMed1978

Rate constants of individual steps in papain-catalysed reactions.

Rate constants for acylation of papain (EC 3.4.22.2) by specific substrates and its subsequent deacylation are derived from kinetic analysis of the reactions in the presence of aminoacetonitrile and methanol. Methyl and ethyl hippurate and methyl N-benzyloxycarbonylglycinate have marginally higher values of rate constants for acylation than for deacylation, while the reverse is true for ethyl N-benzoyl-L-arginate. Both acylation and deacylation are rate-determining for these substrates, while only deacylation irate-determining for methyl-N-acetyl-L-phenylalanylglycinate. Deacylation is the only rate-determining step for p-nitrophenyl esters of hippuric acid, N-benzyloxycarbonylglycine and N-acetyl-L-phenylalanylglycine. These results are discussed in relation to those from inactivation of the enzyme by alkylating agent in the presence of substrate.

Kinetics↗