A D-Lactic Dehydrogenase from Leuconostoc mesenteroides

Kaufmann, E.; Dikstein, S.

doi:10.1038/190346a0

Cited by 16 publications

(8 citation statements)

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“…These enzymes appear to be soluble, although particulate enzymes have been described (12). The iLDHs in the third group occur in the lactic acid bacteria, where they are soluble and are known in a number of species (27,34,55,65,83). The concentrations of the iLDH's in the cells are usually low, and they are probably inert when a cell is actively forming lactate.…”

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confidence: 99%

Bacterial lactate dehydrogenases.

Garvie¹

1980

Microbiological Reviews

338

201

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confidence: 99%

Bacterial lactate dehydrogenases.

Garvie¹

1980

Microbiological Reviews

338

201

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“…A wide variety of different lactic dehydrogenases has been found among the bacteria, in contrast to the similarity of the animal lactic dehydrogenases. Bacterial lactic dehydrogenases differ in such properties as stereospecificity, cofactor and activator requirements, reversibility, sensitivity to inhibitors, stability, and molecular weight (13,14,18,34,38). This report describes the occurrence and characteristics of lactic dehydrogenases found among the fermentative mycoplasmas.…”

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“…NAD-independent i(-)-lactic dehydrogenase was determined at pH 6.5 by following the reduction of 2,6-dichlorophenol-indophenol (DCPIP) at 620 nm (18). Yeast-type lactic dehydrogenase was assayed as described by Dixon (11), using the supematant fluid from an autolyzed aqueous suspension of dried yeast as a control.…”

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Occurrence and Properties of Lactic Dehydrogenases of Fermentative Mycoplasmas

Neimark

Lemcke

1972

J Bacteriol

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Eight fermentative mycoplasmas differing in genome size, deoxyribonucleic acid (DNA) base composition, or sterol dependence were examined for lactic dehydrogenase composition by spectrophotometric assay and polyacrylamide gel electrophoresis. Three completely different patterns of lactic dehydrogenase composition were found. (i) A nicotinamide adenine dinucleotide (NAD)-dependent L(+)-lactic dehydrogenase was found in Mycoplasma pneumoniae, M. gallisepticum, M. mycoides var. mycoides, mycoplasma UM 30847, M. neurolyticum, and Acholeplasma axanthum. Electrophoresis of cell-free extracts of each of these mycoplasmas produced, with the exception of M. mycoides var. mycoides and UM 30847, single, different enzyme bands. M. mycoides var. mycoides and UM 30847 were similar and formed multiple bands of enzyme activity. We were unable to establish whether these multiple bands were due to lactic dehydrogenase isoenzymes or artifacts. (ii) An NAD-dependent D(-)lactic dehydrogenase which could not be reversed to oxidize lactate was found in M. fermentans. (iii) A. laidlawii A possessed an NAD-independent D(-)lactic dehydrogenase capable of reducing dichlorophenol-indophenol, and an NAD-dependent L(+)-lactic dehydrogenase which is specifically activated by fructose-1, 6-diphosphate. Heretofore, this enzyme regulatory mechanism was known to occur only among the Lactobacillaceae. No yeast-type lactic dehydrogenase activity was found in any of the mycoplasmas examined. The stereoisomer of lactic acid accumulated during growth correlated perfectly with the type of NAD-dependent lactic dehydrogenase found in each mycoplasma. The types of lactic dehydrogenase activity found in these mycoplasmas were not related to genome size, DNA base composition, or sterol dependence.of the fermentative mycoplasmas, we searched 633 on July 31, 2020 by guest

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“…This type of enzyme has been reported for a variety of species (Dennis & Kaplan, 1960;van den Hamer, 1960). A second system, which is relatively less active and which is not NAD linked (independent), has also been found in several species (Snoswell, 1963;van den Hamer, 1960;Kaufmann & Dikstein, 1961). The function of this second system is not yet clear; Snoswell (I 963) reported the conversion lactate +.…”

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Lactic Dehydrogenases of Strains of the Genus Leuconostoc

Garvie

1969

Journal of General Microbiology

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S U M M A R YThe lactic dehydrogenases of 11 strains of the genus Leuconostoc were examined. All possessed a D( -) but no L( +) NAD-dependent lactic dehydrogenase, and three strains (I L. mesenteroides and 2 L. paramesenteroides) also had D( -) and L( +) NAD-independent lactic dehydrogenases. The NADdependent enzyme of the seven strains belonging to the species L. mesenteroides, L. dextranicum, L. paramesenteroides, L. Iactis and L. cremoris moved together during electrophoresis in acrylamide gel. The enzymes of the other four strains, all L. oenos, were close together but widely separated from the enzyme of the other species. One strain of L. mesenteroides oxidized NADH without added pyruvate. The enzyme responsible was located after electrophoresis. I N T R O D U C T I O NLactic acid bacteria have two types of enzyme for which lactate is substrate. The most active system catalyses the frequently reversible reaction pyruvate+lactate and is NAD-dependent. This type of enzyme has been reported for a variety of species (Dennis & Kaplan, 1960;van den Hamer, 1960). A second system, which is relatively less active and which is not NAD linked (independent), has also been found in several species (Snoswell, 1963;van den Hamer, 1960;Kaufmann & Dikstein, 1961). The function of this second system is not yet clear; Snoswell (I 963) reported the conversion lactate +. pyruvate by the NAD-independent enzymes of a strain of Lactobacillus (Lb) plantarum but was unable to reverse the reaction. Another type of enzyme forming lactic acid was found by van den Hamer (1960) in Lb casei. In this case methyl glyoxal and not pyruvate was the substrate and the product was D( -) lactic acid. In the genus Leuconostoc the species are ill defined and appear to merge one into the other. A study of the electrophoretic pattern of the lactic dehydrogenase of strains of this genus was made in an attempt to assist in their classification. METHODSStrains. These were selected from the National Collection of Dairy Organisms (NCDO) as typical of their species; they were grown in the media and under the conditions described by Garvie (1967a). The identity of the strains used is given in Fig. 3.Preparation of cell extracts for electrophoresis Media. Two media were used, each prepared in two parts, A and B. Part A of Medium I consisted of (yo, w/v): Bacteriological peptone (Oxoid), 1.0; Bacto yeast extract (Difco), 0.5 ; KH2P0,, 0.5 ; triammonium citrate, 0.5 ; sodium acetate, 0.25 ; MgS04.7H20, 0.02; MnS04.4Hz0, 0.005; Tween 80,0-1 yo (v/v). Amounts to make

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A D-Lactic Dehydrogenase from Leuconostoc mesenteroides

Cited by 16 publications

References 14 publications

Bacterial lactate dehydrogenases.

Bacterial lactate dehydrogenases.

Occurrence and Properties of Lactic Dehydrogenases of Fermentative Mycoplasmas

Lactic Dehydrogenases of Strains of the Genus Leuconostoc

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