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

London, Jack; Meyer, Ernest A.

doi:10.1128/jb.98.2.705-711.1969

Cited by 55 publications

(23 citation statements)

References 15 publications

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“…Furthermore, gl'ucose did not inhibit malate decarboxylation by resting L-malate-induced cells of L. plantarum. In group D streptococcus, glucose inhibited malate decarboxylation, but not the induction of malic enzyme (13). Whereas acetate is not essential to the growth of L. plantarum or to the induction of ,B-galactosidase, nevertheless it improves the rate of both.…”

Section: Discussionmentioning

confidence: 89%

Induction of β-Galactosidase in Lactobacillus plantarum

Hasan

Durr

1974

J Bacteriol

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galactosidase (d-galactoside galactohydrolase, EC 3.2.1.23) is inducible in Lactobacillus plantarum by D-galactose or thiomethyl galactoside, and to a much lesser extent by lactose, isopropyl thiomethyl galactoside, and D-fucose. Isopropyl thiomethyl galactoside is a competitive inhibitor of the enzyme with a K1 of 4.2 mM. The Km of the crude enzyme for o-nitrophenyl fl-D-galactoside is 0.87 6 on July 31, 2020 by guest http://jb.asm.org/ Downloaded from 70

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Section: Discussionmentioning

confidence: 89%

Induction of β-Galactosidase in Lactobacillus plantarum

Hasan

Durr

1974

J Bacteriol

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“…Three groups of malic enzymes, depending on coenzyme specificity and ability to catalyse the decarboxylation of oxalacetate, have been reported (Figure 1). L-Malate : NAD+ oxidoreductase (oxalacetatedecarboxylating; EC 1.1.1.38) uses NAD+ as coenzyme, and has been found in lactobacilli (Korkes et al, 1950), streptococci (London and Meyer, 1969), Escherichia coli (Murai et al, 1972;Yamaguchi et al, 1973) and Schizosaccharomyces pombe (Temperli et al, 1965). L-Malate : NAD+ oxidoreductase (decarboxylating; EC 1.1.1.39) is the malic enzyme most commonly found in the mitochondria of plants and animals ( Edward, 1985).…”

Section: Introductionmentioning

confidence: 99%

Molecular analysis of the malic enzyme gene (mae2) of Schizosaccharomyces pombe

Viljoen

Subden

Krizus

et al. 1994

Yeast

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Sequence analysis of a 4.6-kb HindIII fragment containing the malic enzyme gene (mae2) of Schizosaccharomyces pombe, revealed the presence of an open reading frame of 1695 nucleotides, coding for a 565 amino acid polypeptide. The mae2 gene is expressed constitutively and encodes a single mRNA transcript of 2.0 kb. The mae2 gene was mapped on chromosome III by chromoblotting. The coding region and inferred amino acid sequence showed significant homology with 12 malic enzyme genes and proteins from widely different origins. Eight highly homologous regions were found in these malic enzymes, suggesting that they contain functionally conserved amino acid sequences that are indispensable for activity of malic enzymes. Two of these regions have previously been reported to be NAD- and NADP-binding sites.

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“…Cultivation of organisms. The complex medium containing 0.3% (NH4)2-L(+)-malate used for the maintenance and cultivation of the streptococci was described previously (14). The complex "carrying medium" of Rogosa (22) supplemented with 0.5% ammonium-L(+)malate or 0.5% ammonium-L(+)-malate and 0.15% D- M40 CL-28 liter conical flasks containing 500 ml of the appropriate medium were inoculated with malate-adapted cultures and incubated at 30 C without aeration.…”

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Comparative Biochemical and Immunological Study of Malic Enzyme from Two Species of Lactic Acid Bacteria: Evolutionary Implications

1971

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Representatives of both Streptococcus faecalis and Lactobacillus casei produce isofunctional malic enzymes. All 10 strains of S. faecalis tested could be induced to synthesize malic enzyme and readily adapted to growth on malate. Although 17 of 21 L. casei strains could be induced to produce malic enzyme, only 9 of 14 strains tested grew at the expense of malate. A comparison of catalytic and regulatory properties suggested that the malic enzymes from S. faecalis and L. casei were very similar. Immunological analyses showed that the numerous similarities in function actually reflected partial protein homologies; however, two distinct forms of the malic enzyme were detected among different strains of L. casei by immunochemical and serological procedures. The division of L. casei into two subgroups based on the immunological type of malic enzyme synthesized corresponds to two subspecies currently recognized by microbial taxonomists.An inducible nicotinamide adenine dinucleotide (NAD)-specific malic enzyme from Streptococcus faecalis was shown to be a regulatory protein capable of interacting with three negative effectors which are intermediate products of glucose dissimilation, namely, fructose-1,6-diphosphate (FDP), 3-phosphoglycerate (3PGA), and 6phosphogluconate (6PG; reference 13). A survey of several strains of Lactobacillus casei revealed that at least one of these organisms could also be induced to synthesize an NAD-specific malic enzyme and subsequently grow at the expense of malate. The L. casei malic enzyme bore a striking resemblance to the streptococcal enzyme (London, Meyer, and Kulczyk, Biochim. Biophys. Acta, in press). In addition to similarities in catalytic properties, the Lactobacillus malic enzyme was also inhibited by FDP and 3PGA.A comparison of the physical, catalytic, and regulatory properties of a number of S. faecalis glucose was used to maintain and cultivate the strains of L. casei. Both species were grown as follows. One-126 on July 16, 2020 by guest

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

Cited by 55 publications

References 15 publications

Induction of β-Galactosidase in Lactobacillus plantarum

Induction of β-Galactosidase in Lactobacillus plantarum

Molecular analysis of the malic enzyme gene (mae2) of Schizosaccharomyces pombe

Comparative Biochemical and Immunological Study of Malic Enzyme from Two Species of Lactic Acid Bacteria: Evolutionary Implications

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