[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"$fV0-suvpsigZjVqjhHu0Gw4nftKgOutXoNrj7KtVfPhY":3},{"answer":4,"createTime":5,"id":6,"options":7,"origin":12,"question":19,"related":20,"source":24,"type":25},[],"2025-04-19 17:47:47",183728138,[8,9,10,11],"cysteine","serine","lysine","threonine",{"count":13,"courseId":14,"courseImg":15,"courseName":16,"workId":17,"workName":18},122,"ecb63186fd2348dd972900f765a15722","https:\u002F\u002Ftihai-oss-cloud.itihey.com\u002Fimg\u002Fe91b8b9d3b83a0d6a9d655b826214095.jpg","Biochemistry 《生物化学》一 专业基础课（全英教学）","95936388516c4372bf3d3a582c34e47d","Test 6 - Lecture 6","Chymotrypsin is a ________ protease",[21,26,35,44,53,62,71,80,85,95],{"answer":22,"createTime":5,"id":6,"options":23,"question":19,"source":24,"type":25},[],[8,9,10,11],"v1",0,{"answer":27,"createTime":5,"id":28,"options":29,"question":34,"source":24,"type":25},[],183728139,[30,31,32,33],"Cu2+","Ni2+","Mn2+","Fe2+","The metal cofactor for urease is _______",{"answer":36,"createTime":5,"id":37,"options":38,"question":43,"source":24,"type":25},[],183728140,[39,40,41,42],"apparent Vmax= 2 μM s-1; apparent Km = 2 μM","apparent Vmax = 1 μM s-1; apparent Km = 1 μM","apparent Vmax = 1 μM s-1; apparent Km = 2 μM","apparent Vmax = 2 μM s-1; apparent Km = 4 μM","An enzyme catalyzes the reaction A ⇌ B. The enzyme is present at a concentration of 1 nM, and the Vmax is 2 μM s-1. The Km for substrate M is 4 μM. What values of Vmax and Km would be observed in the presence of sufficient amounts of an uncompetitive inhibitor to generate an α' of 2.0",{"answer":45,"createTime":5,"id":46,"options":47,"question":52,"source":24,"type":25},[],183728141,[48,49,50,51],"acyl groups","one-carbon groups","amino groups","electrons","The functional groups transferred by tetrahydrofolate are ___________________",{"answer":54,"createTime":5,"id":55,"options":56,"question":61,"source":24,"type":25},[],183728142,[57,58,59,60],"apoenzyme","semienzyme","dienzyme","monoenzyme","The protein part of a holoenzyme is called the ______________",{"answer":63,"createTime":5,"id":64,"options":65,"question":70,"source":24,"type":25},[],183728143,[66,67,68,69],"2.4 × 10-4 M","2.4 × 10-5 M","2.4 × 10-6 M","2.4 × 10-7 M","To approximate the concentration of enzymes in a liver cell, assume that the cell contains equal concentrations of 1,000 different enzymes in solution in the cytosol and that each protein has a molecular weight of 100,000. Assume also that the cell is a cylinder (diameter = 1.0 μm, height = 2.0 μm), that the cytosol (specific gravity = 1.20) is 20% soluble protein by weight, and that the soluble protein consists entirely of enzymes. Calculate the average molar concentration of each enzyme in this cell",{"answer":72,"createTime":5,"id":73,"options":74,"question":79,"source":24,"type":25},[],183728144,[75,76,77,78],"0.61","0.71","0.81","0.91","Assume a reaction follows Michaelis-Menten kinetics. Determine the fraction of Vmax that would be obtained at a substrate concentration that is 10Km",{"answer":81,"createTime":5,"id":82,"options":83,"question":84,"source":24,"type":25},[],183728145,[66,67,68,69],"To approximate the concentration of enzymes in a human cell, assume that the cell contains equal concentrations of 1,000 different enzymes in the cytosol and that each enzyme has a molecular weight of 100,000. Assume also that the cell is a ball (diameter 30 μm), that the cytosol (specific gravity 1.20) is 20% soluble protein by weight, and that the soluble protein consists entirely of enzymes. Calculate the average molar concentration of each enzyme in this hypothetical cell",{"answer":86,"createTime":87,"id":88,"options":89,"question":94,"source":24,"type":25},[],"2025-04-19 17:47:48",183728146,[90,91,92,93],"△GA","△GB","△GC","△GD","The binding energy ______ is a major source of free energy used by enzymes to lower the activation energies of reactions",{"answer":96,"createTime":87,"id":97,"options":98,"question":103,"source":24,"type":25},[],183728147,[99,100,101,102],"0.7 μM s-1","0.8 μM s-1","0.9 μM s-1","0.95 μM s-1","An enzyme catalyzes the reaction A ⇌ B. The enzyme is present at a concentration of 2 nM, and the Vmax is 1.2 μM s-1. The Km for substrate A is 10 μM. Calculate the initial velocity of the reaction, V0, when the substrate concentration is 30 μM"]