Enzyme- substrate complex Short-lived intermediate* (acylation) Chymotrypsin (free enzyme) Asp 1 2 YHis" YHis" Active site Oxyanion hole Substrate (a polypeptide) AA HH -N-C-C-N-C-C-AA HH HN AA- -HN -AA OHN Ser HN Ser Ser Hydrophobic H N N pocket Gly Gly Product 1 3 Product 2 HH AA.-C-C-N-C-C-OH HN-CH-C-AA R'O 7 Acyl-enzyme intermediate R' YHis AA,-CH -C HN Enzyme-product 2 complex H OHN Ser R His AA-CH -C N Gly HN -c Short-lived intermediate* OHN Sers (deacylation) Gly 7 His " Acyl-enzyme intermediate YHis" HN AA,-CH- HN HN Ser R HN Sers Gly

From the complete oxidation of glucose (glucose  →  6CO2), how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation?

Compare and contrast the c4 pathway and the malate–aspartate shuttle in bullet format, meaning list the similarities and differences.

The purified OXA-M290 enzyme can now be tested to determine which β-lactamase inhibitor is most effective. This inhibitor could be prescribed in combination with a β-lactam antibiotic to treat the infection caused by the E. coli KGH1 strain. Before testing inhibitors against OXA-M290, the kinetic activity of this enzyme must first be measured. The activity of OXA-M290 is measured using nitrocefin, a chromogenic β-lactam antibiotic. When nitrocefin is hydrolyzed by a β-lactamase, it changes from yellow to red in colour. The nitrocefin hydrolysis product has an extinction coefficient of 20,500 M-1 cm-1 at 486 nm. The hydrolysis of 60 μM nitrocefin by 1 nM OXA-M290 is monitored using a microplate reader. The absorbance of the wells in the plate is measured at 486 nm every 30 seconds. This experiment is carried out with three replicates, generating the following data: Time (min) Absorbance of Replicate 1 Absorbance of Replicate 2 Absorbance of Replicate 3 0.5 0.0984…