List 4 major types of inhibition modes and clearly indicate the effect on Vmax and KM for each mode?

4. a. Calculate the KM (Michaelis constant) and the vmax (the maximum initial rate) for both substrates (sphingosine and ATP). Show your work, and be careful about units. b. threo-dihydrosphingosine, a stereoisomer of sphingosine, is an inhibitor of sphingosine kinase. What kind of inhibitor (competitive, uncompetitive, noncompetitive) is threo-dihydrosphingosine? Citing information from the Lineweaver-Burke plots, explain how you can tell.

1. ( . tion can be represented by the so-called Michaelis equation ) The velocity of an enzyme catalyzed reac- Vmax [S] Vo = Km Vo = max kcat [Eo] [So] (Км + [Sol) V max where [So] is the initial substrate concentration, [Eo] is the total enzyme concentration, kcat is the cataly- tic rate constant or turnover number, and KM repre- sents the Michaelis constant. The graph on the right illustrates the dependence of the velocity of the reaction as a function of substrate concentration. Ex- Km [S] (mm) plain why the maximal velocity can be represented by the expression Vmax = Kcat [Eo] at very high substrate concentrations. Vo (µm/min)

Part 1: Assess the following partial results section below by editing it for brevity by omitting any unnecessary parts (1 point), explain why you decided to remove certain sections (1 point): To evaluate inhibitory effects of the selected molecules, 10mM stock solutions of each molecule were prepared in DMSO. A reaction mixture (200μl) was prepared with the same formula optimized for the enzyme activity assay (0.1 M Tris-HCl ph 8, 0.1 M KCI, 25 mM NaCl, 0.25 mM ATP, and two units of inorganic yeast pyrophosphatase) with 10 µM of the sample molecule. The reaction mixture was incubated for 20 minutes at ambient temperature. Enzymatic reaction was triggered by addition of the substrate B (0.2 mM) and the absorbance of the product was monitored at 290 nm for 10 minutes. Six out of 15 sample molecules showed appreciable inhibition at 10 μM (Figure 5). Three of the molecules, A3, A6, and A7 exhibited more than 50% inhibition of the enzyme activity and were further diluted to find the minimal…

1F. Please help me in detail. for molecular Mechanism of ATP versus GTP selectivity of adenylate kinase, Draw a reaction scheme that includes both the substrate and the inhibitor under study here. Be sure to label KI, Ks, kp