The role of complex metal ions in the yeast hexokinase reaction.

It is known that many of the enzyme systems which ut,ilize ATPl are activated by inorganic cations. In most instances a divalent cation is required (2) and in some cases monovalent cations are also required (3-5). These effects have usually been assumed to be due to activation of the enzyme by the cation. The demonstration that many of these cations react with ATP to form complex ions (6-10) makes it necessary to consider these molecular species in any attempt to interpret the activating or inhibiting effects of metal ions on enzyme systems which utilize ATP. Melchior (8) has pointed out t.he variety of molecular configurations which are to be expected in solutions of ATP in the presence of various positive ions, emphasizing the possibility that one of these configurations may be preferred or required by the enzyme. The detailed mechanism of the interaction of magnesium and ATP with various kinases has not been established. Hers (7) suggested that the magnesium-ATP complex was the specific substrate for liver fructokinase, Liebecq (11) reached a similar conclusion in the case of muscle hexokinase, Lardy and Parks (12) pointed out several possibilities in connection with their work on liver fructokinase, muscle phosphohexokinase, and ATPcreatine transphosphorylase, and Raaflaub and Leupin (13) concluded that MgATP-2 is not the substrate for yeast hexokinase. None of these authors presented a quantitative analysis of their dat,a.

• Publication year

  1958

• Venue

  Journal of Biological Chemistry

• Publication date

  1958-04-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/s0021-9258(18)70427-4PMID 13538997
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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