منابع مشابه
Flavoenzyme catalysis: substrate-competitive inhibition of D-amino acid oxidase.
In an earlier paper from this laboratory (1) there were described the characteristics of competitive inhibition resulting from the interference of certain aromatic compounds with the association of flavin adenine dinucleotide and the separated protein of n-amino acid oxidase. Included among the inhibitors were auramine, quinine, and various other quinolines and anilines. We now present our find...
متن کاملInhibition of pig kidney diamine oxidase by substrate analogues.
1. The oxidation of p-dimethylaminomethylbenzylamine was followed spectrophotometrically by measuring the change in E(250) caused by the p-dimethylaminomethylbenzaldehyde produced. 2. This reaction was inhibited by substrate analogues such as isothiouronium, guanidino, dimethylsulphonium and trimethylammonium compounds. 3. The inhibition by both mono- and bis-onium compounds has been studied an...
متن کاملDirect comparison of gluco-oligosaccharide oxidase variants and glucose oxidase: substrate range and H2O2 stability
Glucose oxidase (GO) activity is generally restricted to glucose and is susceptible to inactivation by H2O2. By comparison, the Y300A variant of gluco-oligosaccharide oxidase (GOOX) from Sarocladium strictum showed broader substrate range and higher H2O2 stability. Specifically, Y300A exhibited up to 40 times higher activity on all tested sugars except glucose, compared to GO. Moreover, fusion ...
متن کاملinvestigation of the effect of substrate conditions on electron transfer of glucose oxidase
direct electron transferring of glucose oxidase was investigated on reduced graphene and graphene oxide templates. the direct electrochemistry glucose oxidase on graphene showed a cyclic voltammograms corresponding to the fad/fadh 2 redox couple with an anodic, cathodic and formal potential of -430, -460 and -445 mv, respectively in 0.1 m phosphate buffer solution and air saturated ...
متن کاملSubstrate Inhibition of Maize Endosperm Sucrose Synthase by Fructose and Its Interaction with Glucose Inhibition*
Sucrose synthase (EC 2.4.1.13) was purified to homogeneity from developing maize lZea mays L.) endosperm. Substrate saturation and inhibitor kinetics were examined for the sucrose synthase reaction. The Km-values for fructose and uridine diphosphate glucose (UDPGlc) were estimated to be 7.8 mM and 76 IlM, respectively. Fructose concentrations over 20 mM inhibited sucrose synthase in an uncompet...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1966
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)99783-8