Pathway of proline oxidation in insect flight muscle

Brosemer, Ronald W.; Veerabhadrappa, Patnagere S.

doi:10.1016/s0926-6593(65)80099-6

Cited by 56 publications

(12 citation statements)

References 17 publications

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“…However, the capacity to use proline is also clearly associated with another important physiological role: enhancing the oxidation of carbohydrates. This observation is not only supported by our experiments on hymenopterans, but also by previous work on dipterans [39][40][41] as well as coleopterans [33][34][35][36][37][38]. Proline is used as a single or combined fuel in many groups of insects and, therefore, should be considered an important metabolic feature for this class of animals.…”

Section: Discussion (A) Proline Metabolism In Hymenopteranssupporting

confidence: 88%

“…Proline is indeed an important metabolite used to replenish TCA cycle intermediates and maintain the potential for pyruvate oxidation ( [7,[39][40][41]65], and possibly [24]). In such a scenario, proline metabolism maintains metabolites of the TCA cycle and the oxygen consumed by the mitochondria would be largely NAD-linked.…”

Section: (B) Flight Muscle Metabolic Propertiesmentioning

confidence: 99%

“…Proline oxidation involves a few steps catalysed by enzymes of the mitochondrial matrix before integration in the tricarboxylic acid cycle (TCA; figure 1). Initial accounts in insects showed that proline acts as a carbon source to replenish TCA cycle intermediates (defined as an anaplerotic role), thereby allowing maximal flux through the TCA cycle during the oxidation of carbohydrates [39][40][41], especially important during the transition from rest to flight [42]. A wide range of strategies is found across beetle species, with some using proline as a co-substrate with carbohydrates and others using proline nearly exclusively as a metabolic fuel [33].…”

Section: Introductionmentioning

confidence: 99%

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Proline as a fuel for insect flight: enhancing carbohydrate oxidation in hymenopterans

et al. 2016

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Bees are thought to be strict users of carbohydrates as metabolic fuel for flight. Many insects, however, have the ability to oxidize the amino acid proline at a high rate, which is a unique feature of this group of animals. The presence of proline in the haemolymph of bees and in the nectar of plants led to the hypothesis that plants may produce proline as a metabolic reward for pollinators. We investigated flight muscle metabolism of hymenopteran species using high-resolution respirometry performed on permeabilized muscle fibres. The muscle fibres of the honeybee, Apis mellifera, do not have a detectable capacity to oxidize proline, as those from the migratory locust, Locusta migratoria, used here as an outgroup representative. The closely related bumblebee, Bombus impatiens, can oxidize proline alone and more than doubles its respiratory capacity when proline is combined with carbohydrate-derived substrates. A distant wasp species, Vespula vulgaris, exhibits the same metabolic phenotype as the bumblebee, suggesting that proline oxidation is common in hymenopterans. Using a combination of mitochondrial substrates and inhibitors, we further show that in B. impatiens, proline oxidation provides reducing equivalents and electrons directly to the electron transport system. Together, these findings demonstrate that some bee and wasp species can greatly enhance the oxidation of carbohydrates using proline as fuel for flight.

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Section: Discussion (A) Proline Metabolism In Hymenopteranssupporting

confidence: 88%

Section: (B) Flight Muscle Metabolic Propertiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Proline as a fuel for insect flight: enhancing carbohydrate oxidation in hymenopterans

et al. 2016

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“…There was about 20 % more proline in ABB than EBB. Insects can detect proline in their food and can use it as an energy substrate to fuel flight and other high energy activities (Brosemer and Veerabhadrappa 1965;Crabtree and Newsholme 1970;Carter et al 2006). Honey bees have a feeding preference for nectars with higher concentrations of this amino acid (Carter et al 2006;Bertazzini et al 2010).…”

Section: Discussionmentioning

confidence: 99%

A comparison of bee bread made by Africanized and European honey bees (Apis mellifera) and its effects on hemolymph protein titers

2012

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-The influence of genotype on the conversion of pollen to bee bread and on the protein titers of bees feeding on it was examined using European and Africanized honey bees (EHB and AHB). Bee bread was more acidic than the pollen, and that made by EHB was slightly more acidic than AHB. Protein concentration in bee bread was similar for both subspecies and lower than in the pollen. In general, amino acid concentrations were higher in bee bread compared with pollen. The only exception was tryptophan. Concentrations of most amino acids in bee bread made by either EHB or AHB were similar. Both subspecies consumed more bee bread made by AHB than EHB. EHB and AHB consumed similar amounts of each type of bee bread, but protein concentrations in AHB were higher than in EHB. Differences in protein acquisition between AHB and EHB might reflect environmental adaptations related to the geographic region where each evolved and could contribute to the successful establishment of AHB populations in the New World.nutrition / microbes / protein / amino acids

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“…Labeled A&-pyrroline-5-carboxylic acid has been recovered from plant extracts after exposure of the tissue to 14C-proline (5). In animals and microorganisms, the first enzyme in the proline to glutamate conversion is proline oxidase (2,6,7,9). This enzyme requires molecular oxygen, is particulate, is inhibited by cyanide, and cytochrome c will serve as the electron acceptor.…”

Section: Introductionmentioning

confidence: 99%

Nicotinamide Adenine Dinucleotide-dependent Proline Dehydrogenase in Chlorella

McNamer¹,

Stewart²

1974

Plant Physiol.

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An NAD-linked dehydrogenase from Chlorella pyrenoidosa Chick catalyzing the conversion of L-proline to A1-pyrroline-5-carboxylic acid was partially purified. A.-Pyrroline-5-carboxylic acid was identified as the product by co-chromatography of it and its o-aminobenzaldehyde derivative with authentic compounds. The enzyme is NAD and L-proline specific and is not an oxidase; NADP is not inhibitory. The Michaelis constant for NAD is 0.08 mM and for proline is 0.73 mM.Plants catabolize proline to glutamate (1,5,14,17), and recently it has been shown that extensive catabolism of proline can occur in leaves low in carbohydrate and high in proline (17) and in Chlorella (14). Labeled A&-pyrroline-5-carboxylic acid has been recovered from plant extracts after exposure of the tissue to 14C-proline (5). In animals and microorganisms, the first enzyme in the proline to glutamate conversion is proline oxidase (2,6,7,9). This enzyme requires molecular oxygen, is particulate, is inhibited by cyanide, and cytochrome c will serve as the electron acceptor. The product of the reaction is P5C.2 A similar enzyme has not been isolated from plant tissue. Recently, a proline dehydrogenase has been isolated from peanut (13) and there are preliminary reports that proline dehydrogenase can be isolated from wheat germ (12) and pumpkin cotyledons (16).This paper reports the presence of a proline dehydrogenase in extracts from Chlorella cells. It has been reported that proline dehydrogenase from peanut (13) does not produce P5C; however, we present evidence that P5C is the product of proline dehydrogenase from Chlorella pyrenoidosa. Molecular oxygen is not required for the production of PSC. yellow complex produced by reaction of P5C with oAB; P2C-oAB: yellow complex produced by reaction of P2C with oAB; DEAE: diethylaminoethyl. MATERIALS AND METHODSAfter washing twice, the cells were resuspended in 0.1 time the original volume of 50 mm phosphate buffer (pH 7.2) containing 1 mM Na2EDTA and 1 mm dithiothreitol. The material was passed twice through a French pressure cell at 20,000 p.s.i. Subsequently, the extracts were kept chilled on ice or the operations were done in a coldroom. After centrifugation at 1 OOOg for 10 min, solid (NH4)2SO4 was added to the supernatant at the rate of 176 g/l. After centrifugation at 10,000g for 10 min, the new supernatant was treated with 273 g of (NH4),SO4/ 1. After centrifugation, the pellet was dissolved in the homogenizing buffer.Some purification was obtained by passing the extract through a DEAE-cellulose column (2.1 X 30 cm). A linear gradient of 100 ml of 0.05 M phosphate (pH 7.2) to 100 ml of 0.2 M phosphate (pH 7.2) was used to elute the enzyme. The enzyme solution was dialyzed against a saturated solution of (NH4),S04 (4 C) for 12 hr. Storage was either in saturated (NH4)2SO4 or by freezing after removal of the (NH4)2SO4.Assay for Proline Dehydrogenase. A typical reaction solution contained initial concentrations of 0.17 M Na-carbonate buffer (pH 10.2), 0.48 to 1.9 mm NAD, 6.7 mm proline, and ...

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Pathway of proline oxidation in insect flight muscle

Cited by 56 publications

References 17 publications

Proline as a fuel for insect flight: enhancing carbohydrate oxidation in hymenopterans

Proline as a fuel for insect flight: enhancing carbohydrate oxidation in hymenopterans

A comparison of bee bread made by Africanized and European honey bees (Apis mellifera) and its effects on hemolymph protein titers

Nicotinamide Adenine Dinucleotide-dependent Proline Dehydrogenase in Chlorella

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