Method for determining glucose, comprising the steps: (a) bringing a sample containing the analyte into contact with a diagnostic element comprising a dry reagent layer which contains (i) a mutated glucose dehydrogenase (EC 1.1.1.47), and (ii) an artificial coenzyme, and (b) determining the presence or/and the quantity of the analyte, wherein the mutated glucose dehydrogenase has an increased thermal or hydrolytic stability compared with the corresponding wild-type enzyme (EC 1.1.1.47) and comprises a mutation at position 170 or/and position 252 of the amino acid sequence of the corresponding wild-type glucose dehydrogenase, wherein the mutation at position 170 comprises an amino acid substitution of glutamic acid for arginine or lysine or/and the mutation at position 252 comprises an amino acid substitution of lysine for leucine and wherein the artificial coenzyme has an increased hydrolytic stability compared with the native coenzyme and a compound having the general formula is used as the artificial coenzyme: where A = adenine or an analogue thereof, T = in each case independently, O, S, U = in each case independently, OH, SH, BH 3 -, BCNH 2 -, V = in each case independently, OH or a phosphate group, or two groups which form a cyclic phosphate group; W = COOR, CON 2, COR, CSN 2 and R = in each case independently, H or C 1-2 -alkyl, X 1, X 2 = in each case independently, O, CH 2, CHCH 3, C(CH 3) 2, NH, NCH 3, Y = NH, S, O, CH 2 Z = a linear or cyclic organic group, with the condition that Z and the pyridine group are not linked by a glycosidic bond, or a salt or, if applicable, a reduced form thereof. (a) bringing a sample containing the analyte into contact with a diagnostic element comprising a dry reagent layer which contains (i) a mutated glucose dehydrogenase (EC 1.1.1.47), and (ii) an artificial coenzyme, and (i) a mutated glucose dehydrogenase (EC 1.1.1.47), and (ii) an artificial coenzyme, and (b) determining the presence or/and the quantity of the analyte, wherein the mutated glucose dehydrogenase has an increased thermal or hydrolytic stability compared with the corresponding wild-type enzyme (EC 1.1.1.47) and comprises a mutation at position 170 or/and position 252 of the amino acid sequence of the corresponding wild-type glucose dehydrogenase, wherein the mutation at position 170 comprises an amino acid substitution of glutamic acid for arginine or lysine or/and the mutation at position 252 comprises an amino acid substitution of lysine for leucine and wherein the artificial coenzyme has an increased hydrolytic stability compared with the native coenzyme and a compound having the general formula is used as the artificial coenzyme: where A = adenine or an analogue thereof, T = in each case independently, O, S, U = in each case independently, OH, SH, BH 3 -, BCNH 2 -, V = in each case independently, OH or a phosphate group, or two groups which form a cyclic phosphate group; W = COOR, CON 2, COR, CSN 2 and R = in each case independently, H or C 1-2 -alkyl, X 1, X 2 = in each case independently, O, CH 2, CHCH 3, C(CH 3) 2, NH, NCH 3, Y = NH, S, O, CH 2 Z = a linear or cyclic organic group, with the condition that Z and the pyridine group are not linked by a glycosidic bond, or a salt or, if applicable, a reduced form thereof. A = adenine or an analogue thereof, T = in each case independently, O, S, U = in each case independently, OH, SH, BH 3 -, BCNH 2 -, V = in each case independently, OH or a phosphate group, or two groups which form a cyclic phosphate group; W = COOR, CON 2, COR, CSN 2 and R = in each case independently, H or C 1-2 -alkyl, X 1, X 2 = in each case independently, O, CH 2, CHCH 3, C(CH 3) 2, NH, NCH 3, Y = NH, S, O, CH 2 Z = a linear or cyclic organic group, with the condition that Z and the pyridine group are not linked by a glycosidic bond, or a salt or, if applicable, a reduced form thereof.