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- W2037173612 abstract "The pyridine nucleotide transhydrogenase of Escherichia coli catalyzes the reversible transfer of hydride ion equivalents between NAD + and NADP + coupled to the translocation of protons across the cytoplasmic membrane. It is composed of two subunits (α, β) organized as an α 2 β 2 tetramer. This brief review describes the use of site-directed mutagenesis to investigate the structure, mechanism and assembly of the transhydrogenase. This technique has located the binding sites for NAD(H) and NADP(H) in the α and β subunits, respectively. Mutagenesis has shown that the cysteine residues of the enzyme are not essential for its function, and that inhibition of the enzyme by sulfhydryl-specific reagents must be due to perturbation of the three-dimensional structure. The sites of reaction of the inhibitors N , N ′-dicyclohexylcarbodiimide and N -(1-pyrene)maleimide have been located. Selective mutation and insertion of cysteine residues followed by cupric o -phenanthrolinate-induced disulfide crosslinking has defined a region of interaction between the α subunits in the holoenzyme. Determination of the accessibility of selectively inserted cysteine residues has been used to determine the folding pattern of the transmembrane helices of the β subunit. Site-directed matagenesis of the transmembrane domain of the β subunit has permitted the identification of histidine, aspartic acid and asparagine residues which are part of the proton-pumping pathway of the transhydrogenase. Site-directed matagenesis and amino acid deletions have shown that the six carboxy terminal residues of the α subunit and the two carboxy terminal residues of the β subunit are necessary for correct assembly of the transhydrogenase in the cytoplasmic membrane." @default.
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- W2037173612 date "1998-06-01" @default.
- W2037173612 modified "2023-10-17" @default.
- W2037173612 title "Site-directed mutagenesis of the proton-pumping pyridine nucleotide transhydrogenase of Escherichia coli" @default.
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- W2037173612 doi "https://doi.org/10.1016/s0005-2728(98)00049-8" @default.
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