Some properties of the malic enzyme of pigeon liver. 1. Conversion of malate into pyruvate

Stickland, R. G.

doi:10.1042/bj0730646

Cited by 39 publications

(10 citation statements)

References 9 publications

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“…The inducible malic enzyme found in S. faecalis is in many respects similar to others isolated from avian (12), fungal (17), and other bacterial sources (4,11) in its (i) requirement for a divalent metal activator, (ii) alkaline pH for optimal activity, and (iii) inhibition by oxaloacetate (unpublished results). However, the biochemical similarities apparently do not reflect a physiological function common to the various organisms and tissues where the enzyme is found.…”

Section: Discussionsupporting

confidence: 64%

Malate Utilization by a Group D Streptococcus : Physiological Properties and Purification of an Inducible Malic Enzyme

London

Meyer

1969

J Bacteriol

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Growth of Streptococcus faecalis in the presence of L-malate resulted in the induction of a "malic enzyme" [L-malate:nicotinamide adenine dinucleotide (NAD) oxidoreductase (decarboxylating), E.C. 1.1.1.39]. Synthesis of the malic enzyme did not appear to be subject to catabolite repression by intermediate products of glucose or fructose dissimilation. However, malate utilization was inhibited during growth in the presence of glucose or fructose. The purified enzyme was

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Section: Discussionsupporting

confidence: 64%

Malate Utilization by a Group D Streptococcus : Physiological Properties and Purification of an Inducible Malic Enzyme

London

Meyer

1969

J Bacteriol

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“…1979 Enzyme assays The activities of 'malic' enzyme, phosphoenolpyruvate carboxykinase and oxaloacetate decarboxylase were assayed at 37°C in freshly homogenized enterocyte suspensions. 'Malic' enzyme (NADP+requiring malate dehydrogenase) was assayed as described by Stickland (1959), phosphoenolpyruvate carboxykinase in the direction of oxaloacetate formation as described by Holton & Nordlie (1965), and oxaloacetate decarboxylase as described for 'supernatant decarboxylase' by Dean & Bartley (1973).…”

Section: Determination Ofmetabolitesmentioning

confidence: 99%

Isolation and metabolic characteristics of rat and chicken enterocytes

Watford¹,

Lund²,

Krebs³

1979

Biochemical Journal

247

149

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1. The recent recognition of the metabolic, as opposed to absorptive, functions of the small intestine prompted efforts the improve the preparation of metabolically competent columnar absorptive cells ('enterocytes') and to study their metabolic properties. 2. With this preparation, linear rates of O2 consumption are obtained for 40 min at 37 degrees C that are more than 50% higher than rates reported by other authors. 3. Among added substrates, glucose, glutamine and glutamate are the preferred fuels of respiration. The main nitrogenous products of glutamine metabolism are NH3, alanine and glutamate. Glutamine carbon was not detectable in citrulline or proline, in contrast with the findings of Windmueller & Spaeth [(1974) J. Biol. Chem. 249, 5070-5079] in the vascularly perfused small intestine. 4. The rates of O2 uptake in the presence of glutamine or glutamate are sufficient to account for the formation of the carbon skeleton of alanine from the amino acid substrate, i.e. the ratio of O2 used/alanine formed is greater than 1.5. 5. Added ADP and ATP are rapidly degraded to AMP and IMP to a large extent by release of hydrolytic enzymes from the enterocytes into the medium. 6. Chicken enterocytes isolated by the same method are more stable; linear rates of O2 uptake are maintained for 60-70 min.

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“…The 'malic' enzyme is inhibited by high concentrations of cations (Speck, 1949;Rutter & Lardy, 1958;Stickland, 1959). To provide information concerning the nature of cation inhibition and gain some insight into the bifunctionality of the 'malic' enzyme, this work was undertaken to investigate the effect of cations and the structural requirement of substrates for the component reactions of the 'malic' enzyme catalysis.…”

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confidence: 99%

Cations in component reactions of ‘malic’ enzyme catalysis

Tsai

Samad

1971

Biochemical Journal

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The ;malic' enzyme (EC 1.1.1.40) has been purified (300-fold) from wheat germ and its abilities to catalyse the decarboxylation and the hydrogenation of oxaloacetic acid and oxaloacetate esters was studied. The free 1-carboxyl group is essential for the interaction of oxaloacetates and substituted oxaloacetates with the enzyme via cations. The free 4-carboxyl group is required for the decarboxylation but is not indispensable for the hydrogenation. At high concentrations, cations inhibit the enzymic hydrogenation of oxaloacetic acid but not that of 4-ethyl oxaloacetate. A plausible inhibitory mechanism is proposed.

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Some properties of the malic enzyme of pigeon liver. 1. Conversion of malate into pyruvate

Cited by 39 publications

References 9 publications

Malate Utilization by a Group D Streptococcus : Physiological Properties and Purification of an Inducible Malic Enzyme

Malate Utilization by a Group D Streptococcus : Physiological Properties and Purification of an Inducible Malic Enzyme

Isolation and metabolic characteristics of rat and chicken enterocytes

Cations in component reactions of ‘malic’ enzyme catalysis

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