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- W2023706341 abstract "Abstract 1. 1. Hexokinase from Hyalophora cecropia fat body has been partially purified and characterized. 2. 2. Hexokinase has a broad band of activity between pH 7·0–8·8, with an optimum at pH 8·4. 3. 3. Employing sucrose density gradient centrifugation of a partially purified preparation, a preliminary mol. wt of 64,000 was obtained. 4. 4. Larval and pupal fat body hexokinase had—toward glucose—identical K m 's (1·3 × 10 −3 M ), and K i 's (3·5 × 10 −3 M ) for GIP. 5. 5. The enzyme is non-competitively inhibited by G6P and F6P ( K i 's = 3·0 × 10 −4 M and 4·0 × 10 −4 M), and un-competitively inhibited by ADP and AMP ( K i = 1·5 × 10 −3 M and 0·9 × 10 −2 M). 6. 6. F1P, F16P, ATP T6P, UDP-Glucose, Trehalose and 3′,5′-cyclic AMP were without effect on the rate of hexokinase-catalyzed G6P formation. 7. 7. Since even small quantities of G1P or G6P will inhibit hexokinase, it is proposed that phosphoglucomutase and G1P-uridyltransferase play key roles in regulating the fiow of exogenous and endogenous precursors into synthesized trehalose." @default.
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- W2023706341 date "1976-01-01" @default.
- W2023706341 modified "2023-10-17" @default.
- W2023706341 title "Regulation of Hyalophora cecropia fat body hexokinase by hexose phosphates common to the pathways of glycolysis, glycogen and trehalose synthesis" @default.
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- W2023706341 doi "https://doi.org/10.1016/0305-0491(76)90349-7" @default.
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