منابع مشابه
Structural and Functional Consequences of Circular Permutation on the Active Site of Old Yellow Enzyme
Circular permutation of the NADPH-dependent oxidoreductase Old Yellow Enzyme from Saccharomyces pastorianus (OYE1) can significantly enhance the enzyme's catalytic performance. Termini relocation into four regions of the protein (sectors I-IV) near the active site has proven effective in altering enzyme function. To better understand the structural consequences and rationalize the observed func...
متن کاملMechanism-Based Studies of the Active Site-Directed Inhibition and Activation of Enzyme Transketolase
Derivatives of phenyl-keto butenoic acids have been reported to be inhibitors of pyruvate decarboxylase, (PDC). The inhibition of transketolase, a thiamine requiring enzyme such as PDF, by meta nitrophenyl derivative of 2-oxo-3-butenoic acid (MNPB) is reported here. These studies indicate that the inhibitor binds to the enzyme at the active site. A two-step inhibition was observed, first th...
متن کامل'New uses for an Old Enzyme'--the Old Yellow Enzyme family of flavoenzymes.
As the first flavin-dependent enzyme identified, and by virtue of its simplicity, the yeast Old Yellow Enzyme (OYE) has been characterized in detail by the whole gamut of physical techniques. Despite this scrutiny, the true physiological role of the enzyme remains a mystery. After 60 years in isolation, OYE has become the archetype of a growing family of flavoenzymes that have been discovered t...
متن کاملThe role of glutamine 114 in old yellow enzyme.
Glutamine 114 of OYE1 is a well conserved residue in the active site of the Old Yellow Enzyme family. It forms hydrogen bonds to the O2 and N3 of the flavoprotein prosthetic group, FMN. Glutamine 114 was mutated to asparagine, introducing an R-group that is one methylene group shorter. The resultant enzyme was characterized to determine the effect of the mutation on the mechanistic behavior of ...
متن کاملPotentiometric studies of native and flavin-substituted Old Yellow Enzyme.
We have measured the redox potentials for the flavin cofactor of native Old Yellow Enzyme and for a series of chemically modified flavin derivatives bound to the apoprotein. These flavin derivatives have midpoint potentials ranging from -120 to -300 mV in free solution. For the native enzyme, the midpoint potential of the first one-electron couple EFMNox + e- in equilibrium EFMN-. is E1 = -245 ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1998
ISSN: 0021-9258
DOI: 10.1074/jbc.273.49.32753