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The Glyoxylate Pathway in Acanthamoeba Sp.*

Gus Tomlinson

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Abstract

SYNOPSIS. Cell‐free extracts of encysting Acanthamoeba were assayed for the key enzymes of the glyoxylate pathway, viz., isocitrate lyase and malate synthase. Both enzymes were present at the onset of encystment but their activities changed as cyst‐wall formation proceeded to completion. Isocitrate lyase activity decreased during the first 4 hr of encystment to a minimum at 4 hr which was 70% of its initial activity. Activity then increased reaching a maximum at 9 hr which was 144% of its initial activity. After 9 hr a decrease in isocitrate lyase activity began which reached 70% of its initial activity at 35 hr. Malate synthase activity slowly decreased throughout encystment to 50% of its initial activity after 35 hr. From these data and others cited, it is concluded that this small soil amoeba has a functional glyoxylate pathway.

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SYNOPSIS. Cell‐free extracts of encysting Acanthamoeba were assayed for the key enzymes of the glyoxylate pathway, viz., isocitrate lyase and malate synthase. Both enzymes were present at the onset of encystment but their activities changed as cyst‐wall formation proceeded to completion. Isocitrate lyase activity decreased during the first 4 hr of encystment to a minimum at 4 hr which was 70% of its initial activity. Activity then increased reaching a maximum at 9 hr which was 144% of its initial activity. After 9 hr a decrease in isocitrate lyase activity began which reached 70% of its initial activity at 35 hr. Malate synthase activity slowly decreased throughout encystment to 50% of its initial activity after 35 hr. From these data and others cited, it is concluded that this small soil amoeba has a functional glyoxylate pathway.

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Available abstract

SYNOPSIS. Cell‐free extracts of encysting Acanthamoeba were assayed for the key enzymes of the glyoxylate pathway, viz., isocitrate lyase and malate synthase. Both enzymes were present at the onset of encystment but their activities changed as cyst‐wall formation proceeded to completion. Isocitrate lyase activity decreased during the first 4 hr of encystment to a minimum at 4 hr which was 70% of its initial activity. Activity then increased reaching a maximum at 9 hr which was 144% of its initial activity. After 9 hr a decrease in isocitrate lyase activity began which reached 70% of its initial activity at 35 hr. Malate synthase activity slowly decreased throughout encystment to 50% of its initial activity after 35 hr. From these data and others cited, it is concluded that this small soil amoeba has a functional glyoxylate pathway.

Key concepts: Isocitrate lyase, Malate synthase, Glyoxylate cycle, Enzyme, Acanthamoeba, Lyase, Biochemistry, Enzyme assay

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