Fat metabolism in higher plants

Stumpf, P.K.

doi:10.1016/0003-9861(70)90019-6

Cited by 26 publications

(2 citation statements)

References 32 publications

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“…The higher affinity of the pine seed enzyme for propionate than for acetate as judged by PPI-ATP exchange and fatty acyl-CoA synthesis, and the higher affinity for propionyl-AMP than for acetyl-AMP as judged by ATP synthesis, distinguishes the short-chain fatty acyl-CoA synthetase of Pinus seeds from the acetyl-CoA synthetases of spinach (Millerd & Bonner, 1954) and potato tuber (Huang & Stumpf, 1970). The spinach enzyme did not catalyse the synthesis of propionyl-CoA, and the affinity of the potato enzyme for propionate was less than for acetate.…”

Section: Discussionmentioning

confidence: 96%

“…These were identified as their hydroxamates as described by Huang (1970). Reaction mixtures contained 7.6,ug of purified enzyme protein, 2mM- 35°C, 0.2ml of salt-free 3.25M-hydroxylamine was added and the mixtures were incubated for a further 10min, and then reactions were terminated with 0.1 ml of 17.5 M-acetic acid or 13.4M-propionic acid; samples (80u1l) were analysed as described by Huang (1970). Acetohydroxamic acid and propionohydroxamic acid were used as markers and were detected as their ferric salts (Stadtman & Barker, 1950).…”

Section: Methodsmentioning

confidence: 99%

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Properties and substrate specificity of some reactions catalysed by a short-chain fatty acyl-coenzyme A synthetase from seeds of Pinus radiata

Young

Anderson

1974

Biochemical Journal

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1. Crude extracts of seeds of Pinus radiata catalysed acetate-, propionate-, n-butyrate- and n-valerate-dependent PP(i)-ATP exchange in the presence of MgCl(2), which was apparently due to a single enzyme. Propionate was the preferred substrate. Crude extracts did not catalyse medium-chain or long-chain fatty acid-dependent exchange. 2. Ungerminated dry seeds contained short-chain fatty acyl-CoA synthetase activity. The activity per seed was approximately constant for 11 days after imbibition and then declined. The enzyme was located only in the female gametophyte tissue. 3. The synthetase was purified 70-fold. 4. Some properties of the enzyme were studied by [(32)P]PP(i)-ATP exchange. K(m) values for acetate, propionate, n-butyrate and n-valerate were 4.7, 0.21, 0.33 and 2.1mm respectively. Competition experiments between acetate and propionate demonstrated that only one enzyme was involved and confirmed that the affinity of the enzyme for propionate was greater than that for acetate. CoA inhibited fatty acid-dependent PP(i)-ATP exchange. The enzyme catalysed fatty acid-dependent [(32)P]PP(i)-dATP exchange. 5. The enzyme also catalysed the fatty acyl-AMP-dependent synthesis of [(32)P]ATP from [(32)P]PP(i). Apparent K(m) (acetyl-AMP) and apparent K(m) (propionyl-AMP) were 57mum and 7.5mum respectively. The reaction was inhibited by AMP and CoA. 6. Purified enzyme catalysed the synthesis of acetyl-CoA and propionyl-CoA. Apparent K(m) (acetate) and apparent K(m) (propionate) were 16mm and 7.5mm respectively. The rate of formation of acetyl-CoA was enhanced by pyrophosphatase. 7. It was concluded that fatty acyl adenylates are intermediates in the formation of the corresponding fatty acyl-CoA.

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Section: Discussionmentioning

confidence: 96%

Section: Methodsmentioning

confidence: 99%

Properties and substrate specificity of some reactions catalysed by a short-chain fatty acyl-coenzyme A synthetase from seeds of Pinus radiata

Young

Anderson

1974

Biochemical Journal

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Miscellaneous

Scandalios¹,

Sorenson²,

Howland³

et al. 1977

Applied and Fundamental Aspects of Plant Cell, Tissue, and Organ Culture

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Fatty-acid metabolism in senescing and regreening soybean cotyledons

Place

Morgan

Rutkoski

et al. 1979

Planta

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Changes in fatty-acid metabolism were studied in soybean (Glycine max Merr.) cotyledons during senescence as well as in cotyledons which had been caused to regreen by removal of the epicotyl from the seedling. The activities of the enzymes acetyl-CoA synthetase (EC 6.2.1.1) and fatty-acid synthetase in plastids isolated from the cotyledons decreased during senescence but increased in response to regreening. These changes in enzyme activities followed the same pattern as changes in the quantities of chlorophyll and polyunsaturated fatty acids in this tissue. The in-vivo incorporation of [(14)C]acetate into total fatty acids in the senescing and regreening cotyledons did not vary markedly with age. In addition, the quantity of label in fatty acids did not decrease for as much as 60 h after the removal of the substrate. During this 60-h period however, there was substantial redistribution of the label among the individual fatty acids. While the labelling pattern of the individual fatty acids did not vary significantly with respect to age in the senescing cotyledons, there was a substantial increase in the synthesis of labelled polyunsaturated fatty acids in the regreening tissue. Thus, the incorporation of [(14)C]acetate into fatty acids did not reflect the changes in the quantities of the individual fatty acids in senescing tissue as well as they did in regreening tissue.

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Fat metabolism in higher plants

Cited by 26 publications

References 32 publications

Properties and substrate specificity of some reactions catalysed by a short-chain fatty acyl-coenzyme A synthetase from seeds of Pinus radiata

Properties and substrate specificity of some reactions catalysed by a short-chain fatty acyl-coenzyme A synthetase from seeds of Pinus radiata

Miscellaneous

Fatty-acid metabolism in senescing and regreening soybean cotyledons

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