Water-soluble class C β-lactamase catalytic residue mimic: Effect of proximally positioned functional groups on their pKa values

Tetrahedron Letters

Volumn 39, Issue 1-2, 1998, Pages 51-54

  Kato Toma, Yoko ^a   Imajo, Seiichi ^b   Ishiguro, Masaji ^a  

^a SUNTORY INSTITUTE FOR BIOORGANIC RESEARCH   (Japan)

^b SUNTORY LTD   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE; CEPHALOSPORIN DERIVATIVE; PENAM DERIVATIVE;

ARTICLE; CRYSTAL STRUCTURE; DRUG SYNTHESIS; ENZYME ACTIVITY; ENZYME KINETICS; STRUCTURE ACTIVITY RELATION;

EID: 0031973295     PISSN: 00404039     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0040-4039(97)10486-5     Document Type: Article

References (29)

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22. +), 391.15; found 391.2.
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26. (a) Energy minimized structures were obtained by using MM2 forcefield as implemented in MacroModel V3. Systematic minimization was employed, where the torsion angle of the exocyclic C-C bonds in B, C and D were varied by 10° increments prior to minimization. In the case of C where there are two sets of two different exocyclic C-C bonds, tortion α and β in compound E were minimized initially. After obtaining several α and β values giving rise to several low energy conformations, combinations of these values were used as starting values for α,α′,β and β′ to find the lowest energy conformation of C. (b) Minimizations and calculations of heats of formation were carried out using PM3 semiempirical methods as implemented in MOPAC V6 program package.
27. +. Stull, D.R.; Prophet, J. JANAF Thermochemical Tables; NSRDS-NBS37.
28. Using a glass electrode pH meter, a 50 to 90 point pH titration curve was obtained by titrating a solution, 10mM in 1, 2, 3 or 4, and 10 mM in HCl (500 μL to 1000 μL) with 50mM NaOH solution in increments of 5-20 μL at 297K.
29. UV measurements were made on a Shimadzu UV-2400PC UV-VIS Recording Spectrophotometer.