1 describe how β-lactam antibiotics (e. g. penicillins, carbapenems) harm or kill bacteria (research on your own).
2 explain the relationship amongst β-lactamases, β-lactam ring and β-lactams to describe how bacteria can be resistant to antibiotics such as penicillin (research on your own).
3 this is the chemical structure of meropenem, a carbapenem antibiotic. the β- lactam ring is common to all antibiotics in this class. circle the β-lactam ring (research on your own)
4 explain the role of clavulanic acid in augmentin? what is it about clavulanic acid’s chemical structure that allows this role (see appropriate web page). what name (given in the video on biochemistry you watch earlier) is given to the action of clavulanic acid on β-lactamase? circle the β-lactam ring.
clavulanic acid
5 figures 1b, 1c and 1d show the results of three assays where enzyme activity (“residual activity”) is the dependent variable. these assays use nitrocefin as a substrate.
explain how the nitrocefin assay can be used to assess β-lactamase activity (including metallo-beta- lactamases; see the appropriate web page).
circle the β-lactam ring. what enzyme described in the paper would hydrolyze the β-lactam ring in
nitrocefin?
nitrocefin >
what color is created when the product is formed?
hydrolyzed nitrocefin

6 figure 1c provides evidence regarding whether the inhibition of ndm -1 by ama is reversible. ndm-1 and ama were mixed together in the presence of zinc. then ndm-1 and ama were separated by chromatography. the separated ndm-1 was also used to create the results shown in figure 1d.
explain how the pd10 column was used to separate ndm-1 and ama (refer to the appropriate web page). note that when this type of chromatography is done, the eluent is collected as different samples after it has passed through (not as a whole). the ndm-1 and ama will end up in different samples. ama has a molecular weight of approximately 307 g/mol. ndm-1 has a mass 28,000 times that of hydrogen.
7 explain how figures 1c and 1d lead to the conclusion about the relationship amongst ama, ndm-1 and zinc.
8 predict how figure 1c would be different if the inhibition of ndm-1 by ama was reversible (enzyme function was restored after ama was removed).
9 predict how figure 1d would be different if the same assay were run but ama was present in excess (what ama is going to do will be done with 100% efficiency).