Protein factor which induces conversion between Physarum ornithine decarboxylase forms in vitro

Mitchell, John L.A.; Augustine, Tom A.; Wilson, Judith

doi:10.1016/0005-2744(81)90149-2

Cited by 21 publications

(4 citation statements)

References 16 publications

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“…The isolation procedure that we reported previously produced a conversion factor that was unstable in the A-form-B-form conversion assay, resulting in a cessation of catalytic activity after 45-60min (Mitchell et al, 1981b). Our current methods for partial purification of this converting protein, and the indicated improved assay conditions that include poly(ethylene glycol), result in a reaction that proceeds at constant velocity for at least 90min.…”

Section: Resultsmentioning

confidence: 94%

Amine-specificity of the inactivating ornithine decarboxylase modification in Physarum polycephalum

Mitchell¹,

Mitchell²,

Carter³

1982

Biochemical Journal

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The enzyme catalysing the polyamine-stimulated modification of Physarum ornithine decarboxylase in vivo was partially purified and its activity on purified ornithine decarboxylase was examined with respect to its specificity for various amines. Spermidine, spermine and several polyamine analogues strongly promoted this reaction in vitro (apparent Km in the 0.1--0.5 mM range), whereas putrescine (apparent Km 5.33 mM) and several related diamines were not nearly as effective. In agreement with this, sensitivity studies performed in vivo also suggested that cellular spermidine, and not putrescine, is critical in modulating ornithine decarboxylase activity by this post-translational control. Unlike putrescine, or other diamines, 1,3-diaminopropane demonstrated a functional similarity to the polyamines in stimulating this reaction. This study has demonstrated a method whereby non-physiological amines capable of depressing ornithine decarboxylase activity by this natural feedback mechanism can be readily identified for further evaluation of their potential use in the experimental and medical control of polyamine biosynthesis.

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Section: Resultsmentioning

confidence: 94%

Amine-specificity of the inactivating ornithine decarboxylase modification in Physarum polycephalum

Mitchell¹,

Mitchell²,

Carter³

1982

Biochemical Journal

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“…A quite different mechanism works in Physarum polycepharum. Thus, polyamines induce reversible conversion of active A form into less active B form, which is catalysed by ODC-modifying protein [142,143].…”

Section: Comparative Biochemistrymentioning

confidence: 99%

Rapid and regulated degradation of ornithine decarboxylase

Hayashi

Murakami

1995

Biochemical Journal

194

131

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“…In rat liver, 80% of the cellular antizyme is found localized in the nucleus partially bound to OrnDCase (7). Recently, Mitchell et aL (10) reported an antizyme-like factor in the slime mold Physarum polycephalum that requires spermidine or spermine to complex to OrnDCase.…”

mentioning

confidence: 99%

Phosphorylation of ornithine decarboxylase by a polyamine-dependent protein kinase.

Atmar¹,

Kuehn²

1981

Proc. Natl. Acad. Sci. U.S.A.

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Protein factor which induces conversion between Physarum ornithine decarboxylase forms in vitro

Cited by 21 publications

References 16 publications

Amine-specificity of the inactivating ornithine decarboxylase modification in Physarum polycephalum

Amine-specificity of the inactivating ornithine decarboxylase modification in Physarum polycephalum

Rapid and regulated degradation of ornithine decarboxylase

Phosphorylation of ornithine decarboxylase by a polyamine-dependent protein kinase.

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