1995
DOI: 10.1021/bi00008a021 View full text |Buy / Rent full text
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Abstract: Crystallographic studies indicate that the loop between alpha-helix 8 and beta-strand H (the 8H loop) which borders the effector site of Bacillus stearothermophilus phosphofructokinase (BsPFK) is involved in the allosteric mechanism of the enzyme [Schirmer, T., and Evans, P.R. (1990) Nature 343, 140-145]. The residue at one end of this loop, glycine 212, has been proposed to be a pivot about which the loop hinges. Using site-directed mutagenesis, glycine 212 was replaced with valine (G212V). Steady-state kinet… Show more

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“…The residues Gly165 and Gly166 were mutated to the bulkier valine residue in order to disrupt the hydrogen bonding due to steric hindrance. There is ample precedent for mutation of glycine residues to disrupt hydrogen bonding between backbone amide NH groups and substrates, a few examples are: chlorobenzoyl‐CoA dehalogenase,30 carbamoyl phosphate synthetase,31 phosphofructokinase,32 glutathione synthetase,33 and adenylate kinase 23. In all of these examples, the mutations did not cause a gross conformational change and that is also observed with the mutations studied here.…”
Section: Discussionsupporting
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“…The residues Gly165 and Gly166 were mutated to the bulkier valine residue in order to disrupt the hydrogen bonding due to steric hindrance. There is ample precedent for mutation of glycine residues to disrupt hydrogen bonding between backbone amide NH groups and substrates, a few examples are: chlorobenzoyl‐CoA dehalogenase,30 carbamoyl phosphate synthetase,31 phosphofructokinase,32 glutathione synthetase,33 and adenylate kinase 23. In all of these examples, the mutations did not cause a gross conformational change and that is also observed with the mutations studied here.…”
Section: Discussionsupporting