Interaction between phosphofructokinase and aldolase from Saccharomyces cevisiae studied by aqueous two-phase partitioning

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Abstract

Phosphofructokinase (EC 2.7.1.11) and aldolase (EC 4.1.2.13) have been highly purified from Saccharomyces cerevisiae
by improved protocols. Partitioning of the enzymes in aqueous polymer two-phase systems was used to detect complex
formation. The partition of each enzyme was found to be affected by the presence of the other enzyme. AMP affected the
partition of the individual enzymes as well as the mixture of the two. The activities of the respective enzymes were
stimulated in the putative complex in an AMP-dependent manner. Two strictly conserved residues belonging to an acidic
surface loop of class II aldolases, are a potential site for electrostatic interaction with the positively charged regions close to
the active site in phosphofructokinase. Ó 2001 Elsevier Science B.V. All rights reserved.

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Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Biologiska vetenskaper
Originalspråkengelska
Sidor (från-till)341-348
TidskriftJournal of Chromatography. B
Volym751
Utgåva nummer2
StatusPublished - 2001
PublikationskategoriForskning
Peer review utfördJa