A direct pathway for the metabolism of propionate in cell extracts from <i>Moraxella Iwoffi</i>

Hodgson, Brian; McGarry, Julie

doi:10.1042/bj1070019

Cited by 12 publications

(3 citation statements)

References 14 publications

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“…Antifoam emulsion (21il.) was added to prevent foaming, and euvettes were gassed with N2 as described by Hodgson & McGarry (1968). Reactions, at 240, were started by adding 10moles of 2-furoate, which had been previously gassed with and stored under N2, and followed by measuring the decrease in E665 due to reduction of methylene blue.…”

Section: Resultsmentioning

confidence: 99%

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The metabolism of 2-furoic acid by Pseudomonas F2

Trudgill

1969

Biochemical Journal

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1. Pseudomonas F2 isolated by enrichment culture on 2-furoic acid and grown with it as carbon source oxidized the compound with a Q(o) (2) of 170mul./mg. dry wt./hr. and the overall consumption of 2.5mumoles of oxygen/mumole of substrate. 2. In the presence of 1mm-sodium arsenite, oxygen uptake was restricted to 0.54mumole/mumole of 2-furoate oxidized, with the formation of 0.86mumole of 2-oxoglutarate/mumole of 2-furoate. 3. Cell suspensions, disrupted in a French pressure cell and centrifuged at 27000g, yielded supernatants capable of catalysing the slow oxidation of 2-furoate (0.17mumole/mg. of protein/hr.). 4. Fractionation of 27000g supernatants at 200000g yielded a soluble enzyme fraction capable of catalysing the oxidation of 2-furoate only in the presence of added 200000g pellet or of Methylene Blue. 5. The 2-furoate-stimulated uptake of oxygen or the anaerobic reduction of Methylene Blue by dialysed 27000g supernatant required the addition of ATP and CoA, and the rate of oxygen uptake was further enhanced by the addition of magnesium chloride and NAD(+). 6. The role of ATP and CoA in the formation of 2-furoyl-CoA was demonstrated by the accumulation of 2-furoylhydroxamic acid in the presence of hydroxylamine. 7. Dialysed 200000g supernatant, treated with Dowex 1, required the addition of ATP, CoA and Methylene Blue before it could oxidize 2-furoate to 2-oxoglutarate, which was trapped in unitary stoicheiometric yield as its phenylhydrazone. Magnesium chloride and NAD(+) were not stimulatory in this system. The oxidation of 2-furoate to 2-oxoglutarate was not inhibited by substrate analogues, metal ion-chelating agents, thiol-active compounds or inhibitors of cytochrome-mediated electron transport. 8. No evidence was obtained for the intervention of 2,5-dioxovalerate as an intermediate in 2-oxoglutarate formation.

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Section: Resultsmentioning

confidence: 99%

“…& Adams, 1964& Adams, , 1965 was assayed by observing the increase in E340 P. W. TRUDGILL and 81.moles of sodium 2,5-dioxovalerate. The assays were performed at 240 under anaerobic conditions achieved as described by Hodgson & McGarry (1968).…”

Section: Methodsmentioning

confidence: 99%

The metabolism of 2-furoic acid by Pseudomonas F2

Trudgill

1969

Biochemical Journal

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“…For the last-named, extracts were prepared as described by Abeles (1966). Acetate kinase and phosphotransacetylase were assayed by the methods of Hodgson & McGarry (1968).…”

Section: Growth Ofmicro-organismsmentioning

confidence: 99%

Microbial metabolism of amino alcohols. 1-Aminopropan-2-ol and ethanolamine metabolism via propionaldehyde and acetaldehyde in a species of Pseudomonas

Jones

Turner

1973

Biochemical Journal

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1. Growth and manometric experiments showed that a Pseudomonas sp. P6 (N.C.I.B. 10431), formerly known as Achromobacter sp. P6, was capable of growth on both stereoisomers of 1-aminopropan-2-ol, and supported the hypothesis that assimilation involved metabolism to propionaldehyde, propionate and possibly 2-hydroxyglutarate. A number of alternative intermediary metabolites were ruled out. 2. Accumulation of propionaldehyde from 1-aminopropan-2-ol by intact cells occurred only during active growth, was transitory and was accompanied by morphological changes in the pseudomonad. 3. Enzymic and radioactive tracer evidence showed that 1-aminopropan-2-ol O-phosphate was the intermediate between amino alcohol and aldehyde. The operation of an inducibly formed ATP-amino alcohol phosphotransferase was established by measuring substrate disappearance, ADP formation and amino alcohol O-phosphate formation. This novel kinase had two activity peaks at about pH7 and 9. It acted on both l- and d-isomers of 1-aminopropan-2-ol, and also on l-threonine and ethanolamine, but had only low activity towards choline. The enzyme was partially purified by ion-exchange chromatography. 4. An amino alcohol O-phosphate phospho-lyase (deaminating) produced propionaldehyde from dl- and d-1-aminopropan-2-ol O-phosphate, and also formed acetaldehyde less rapidly from ethanolamine O-phosphate. It had optimum activity at about pH8 in Tris-HCl buffers. The enzyme was partially purified and evidence was obtained that a single enzyme was responsible for both activities. Apparent K(m) values for the substrates were determined. Activity was inhibited by dl-threonine O-phosphate, dl-serine O-phosphate, choline O-phosphate and P(i). Enzyme formation was induced by growth with either amino alcohol substrate. 5. Radioactive tracer experiments with dl-1-amino[3-(14)C]propan-2-ol confirmed the operation of the amino alcohol kinase and demonstrated coupling with the phospho-lyase enzyme in vitro to produce [(14)C]-propionaldehyde. 6. An aldehyde dehydrogenase, found in extracts of the pseudomonad after growth on 1-aminopropan-2-ol, was characterized and concluded to be responsible for propionaldehyde and acetaldehyde oxidation. The enzyme was inactive with methylglyoxal. 7. Propionate and acetate were concluded to be metabolized via propionyl-CoA and acetyl-CoA, and studies were made of a CoA ester synthase found in extracts. 8. Studies of a strain of Pseudomonas putida N.C.I.B. 10558 suggested that 1-aminopropan-2-ols were metabolized via their O-phosphates, propionaldehyde and propionate. Amino alcohol kinase activity was detected and extracts contained a phospho-lyase showing higher activity with the 1-aminopropan-2-ol O-phosphate than with ethanolamine O-phosphate.

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Les Polymères Bioactifs XI. Insolubilisation de la β‐Amylase Sur les Dérivés de la Cellulose

Bouzaher¹,

Dumitriu²,

Simionescu³

1982

Bulletin des Soc Chimique

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The immobilization of 6-amylase on acid chloride of carboxvmethylcellulose (DS = 2.02) and BIOZAN R is presented. Kinetic studies established the following conditions for a optimum coupling : pH = 8.4, time = 2 h, temperature = 5°C. The immobilization on BIOZAN R was carried out by usinq the BIOZAN R acid chloride or by activation with dicyclocarbodiimide. The results showed that the nature of the carrier and the method of immobilization determine directly the quantity and the activity of the coupled 6-amylase. INTRODUCTIONLes enzymes insolubilisees representent de nos jours un domaine de recherche trss vaste qui ne fait que se developper au fil des annees. Vue la diversification des mBthodes d'immobilisation d'enzymes et les supports qui les lient, elles trouvent des champs d'application trss importants en analvse" 2, en biochimie c o m e modsles des reactions cellulaires3' 4, en et surtout en chimie alimentaire'. Les supports utilises sont soit svnthetiques, soit naturels. Un interst particulier est accord6 aux derives de la cellulose. Parmi ceux constamment employes il y a la 4-aminobenzovlcellulose, la 4-aminobenzyl-

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A direct pathway for the metabolism of propionate in cell extracts from Moraxella Iwoffi

Cited by 12 publications

References 14 publications

The metabolism of 2-furoic acid by Pseudomonas F2

The metabolism of 2-furoic acid by Pseudomonas F2

Microbial metabolism of amino alcohols. 1-Aminopropan-2-ol and ethanolamine metabolism via propionaldehyde and acetaldehyde in a species of Pseudomonas

Les Polymères Bioactifs XI. Insolubilisation de la β‐Amylase Sur les Dérivés de la Cellulose

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