Purification and Characterization of Isocitrate Lyase from<i>Rhodopseudomonas</i>sp. No. 7

Tahama, Hirotsugu; Shinoyama, Hirofumi; ANDO, AKIKAZU; Fujii, Tomoyuki

doi:10.1080/00021369.1990.10870489

Cited by 2 publications

(3 citation statements)

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“…The properties of purified isocitrate lyase and malate synthase correspond to previously reported data for these enzymes from other sources, e.g. plants and microorganisms [15,16]. However, ADP stimulation has not been reported previously.…”

Section: Discussionsupporting

confidence: 86%

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Induction of glyoxylate cycle enzymes in rat liver upon food starvation

Popov¹,

Igamberdiev²,

Schnarrenberger³

et al. 1996

FEBS Letters

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The key enzymes of the glyoxylate cycle, isocitrate lyase and malate synthase, have been detected in liver of foodstarved rats. Activities became measurable 3 days and peaked 5 days after the beginning of starvation. Both enzymes were found in the peroxisomal cell fraction after organelle fractionation by isopycnic centrifugation. Isocitrate lyase was purified ll2-fold by ammonium sulfate precipitation, and chromotography on DEAE-cellulose and Toyopearl HW-65. The specific activity of the purified enzyme was 9.0 units per mg protein. The Km(isocitrate) was 68 Iz2VI and the pH optimum was at pH 7.4. Malate synthase was enriched 4-fold by ammonium sulfate precipitation. The enzyme had a Km(acetyl-CoA) of 0.2 [aM, a Km(glyoxylate) of 3 mM and a pH optimum of 7.6.

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Section: Discussionsupporting

confidence: 86%

“…plants and microorganisms [15,16] previously. It may correspond to the physiological significance of this phenomenon, as mobilization of fatty acids is necessary for supporting energy balance and carbohydrate levels during starvation.…”

Section: Discussionmentioning

confidence: 99%