[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"$f6GRgn-l5W55zsLhGKsDTJXbG84KtWYoSdBfX3YB-2UM":3},{"answer":4,"createTime":5,"id":6,"options":7,"origin":12,"question":19,"related":20,"source":30,"type":31},[],"2025-04-19 17:47:47",183728145,[8,9,10,11],"2.4 × 10-4 M","2.4 × 10-5 M","2.4 × 10-6 M","2.4 × 10-7 M",{"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","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",[21,32,41,50,59,68,73,82,85,95],{"answer":22,"createTime":5,"id":23,"options":24,"question":29,"source":30,"type":31},[],183728138,[25,26,27,28],"cysteine","serine","lysine","threonine","Chymotrypsin is a ________ protease","v1",0,{"answer":33,"createTime":5,"id":34,"options":35,"question":40,"source":30,"type":31},[],183728139,[36,37,38,39],"Cu2+","Ni2+","Mn2+","Fe2+","The metal cofactor for urease is _______",{"answer":42,"createTime":5,"id":43,"options":44,"question":49,"source":30,"type":31},[],183728140,[45,46,47,48],"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":51,"createTime":5,"id":52,"options":53,"question":58,"source":30,"type":31},[],183728141,[54,55,56,57],"acyl groups","one-carbon groups","amino groups","electrons","The functional groups transferred by tetrahydrofolate are ___________________",{"answer":60,"createTime":5,"id":61,"options":62,"question":67,"source":30,"type":31},[],183728142,[63,64,65,66],"apoenzyme","semienzyme","dienzyme","monoenzyme","The protein part of a holoenzyme is called the ______________",{"answer":69,"createTime":5,"id":70,"options":71,"question":72,"source":30,"type":31},[],183728143,[8,9,10,11],"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":74,"createTime":5,"id":75,"options":76,"question":81,"source":30,"type":31},[],183728144,[77,78,79,80],"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":83,"createTime":5,"id":6,"options":84,"question":19,"source":30,"type":31},[],[8,9,10,11],{"answer":86,"createTime":87,"id":88,"options":89,"question":94,"source":30,"type":31},[],"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":30,"type":31},[],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"]