Molecular analysis of the malic enzyme gene (<i>mae2</i>) of <i>Schizosaccharomyces pombe</i>

Viljoen, Marinda; Subden, R. E.; Krizus, Aldis; Vuuren, H. J. J. Van

doi:10.1002/yea.320100506

Cited by 42 publications

(47 citation statements)

References 71 publications

(49 reference statements)

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“…choose two primers for PCR amplification of an approximately 580 bp region of the mle gene from thirteen LAB strains. In Lactococcus lactis, this region consisted of 36% of mleS gene which contains the malate-binding site (Viljoen et al, 1994), the ADPbinding pap fold region (Wierenga et al, 1985) and a region described as the malic enzyme signature in protein databases (Bairoch,199 1). Moreover, two corresponding primers were chosen from the E. coli malic enzyme gene.…”

Section: Pcr Amplification Of 580 Bp Mle Gene Fragments and Sequence mentioning

confidence: 99%

Comparison of partial malolactic enzyme gene sequences for phylogenetic analysis of some lactic acid bacteria species and relationships with the malic enzyme

Groisillier

Lonvaud-Funel

1999

International Journal of Systematic and Evolutionary Microbiology

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DNA sequences covering 36% of the mle gene that encodes the malolactic enzyme were determined for 13 strains of lactic acid bacteria, representing Pediococcus, Leuconostoc, Lactobacillus and Oenococcus genera. The sequences were aligned with the corresponding region of mleS in Lactococcus lactis. The phylogenetic distance matrix tree of all mle sequences was compared with the 165 rRNA phylogenetic tree. The analysis showed that the mle fragment evolved more rapidly than the 16s gene and differently. Pediococcus and Lactobacillus species were intermixed in the 165 rRNA tree whereas they were separated in the mle tree. Leuconostoc mesenteroides and Oenococcus oeni were distinct from other species in the 16s rRNA tree, whereas they were intermixed with Lactobacillus species and Lactococcus lactis in the mle tree.The amino acid sequences deduced from partial mle genes were aligned with 22 malic enzyme sequences and the corresponding phylogenetic tree was constructed. Malic and malolactic enzymes were distinct a t the phylogenetic level, except for malic enzymes of yeast and Escherichia coli which were nearer the malolactic enzymes than the other malic enzymes. The analysis of conserved sites showed several interesting amino acids specific to either malic enzyme or malolactic enzyme.

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Section: Pcr Amplification Of 580 Bp Mle Gene Fragments and Sequence mentioning

confidence: 99%

Comparison of partial malolactic enzyme gene sequences for phylogenetic analysis of some lactic acid bacteria species and relationships with the malic enzyme

Groisillier

Lonvaud-Funel

1999

International Journal of Systematic and Evolutionary Microbiology

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“…The apparent universal possession of malic enzyme and the similarity, at the amino acid and DNA level, of malic enzymes from disparate sources (Hodnett et al, 1996 ;Viljoen et al, 1994 ;Walter et al, 1994) suggest a fundamental and crucial cellular function for this enzyme. Amongst the suggested functions for malic enzyme are roles in the metabolism of acetate (McCullough & Roberts, 1974), involvement in anaerobic growth (Boles et al, 1998), and generation of NADPH for lipid biosynthesis (Evans & Ratledge, 1985 ;Frenkel, 1975 ;Hodnett et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

A pre-genetic study of the isoforms of malic enzyme associated with lipid accumulation in Mucor circinelloides

Song

Wynn

et al. 2001

Microbiology

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The oleaginous fungus Mucor circinelloides possesses at least six isoforms of malic enzyme (EC 1 .1 .1 .40), a key lipogenic enzyme in filamentous fungi. These isoforms were detected using a specific stain for activity after native PAGE of cell extracts. Only one isoform (isoform IV) was associated with lipid accumulation, appearing only after N-exhaustion from the medium (which is a pre-requisite for lipid accumulation) in glucose-growing cells. Isoforms I, II, V and VI were involved in anaerobic growth and only appeared under O 2 -limited conditions. Isoform III appeared to be constitutive and was formed under conditions of active (balanced) growth and is therefore thought to play a crucial role in basic metabolism. Growth on acetate increased the amount of cell lipid (from 25-27 % in glucose-grown cells to 37-38 % in acetate-grown cells) accumulated by M. circinelloides and this was associated with the appearance of isoform IV of malic enzyme prior to N-exhaustion in these cultures. Amino acid sequence analysis of isoforms III and IV suggests that these two malic enzymes may be encoded by a single gene and that isoform IV is formed from isoform III by post-translational modification initiated by either N-limitation (when glucose was the carbon source) or growth on acetate as the sole carbon source.

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“…Intracellularly, Sz. pombe decarboxylates L-malic acid to pyruvate and CO 2 by means of a cytosolic malic enzyme encoded by the mae2 gene (Viljoen et al, 1994). Under fermentative conditions, pyruvate is further metabolized to ethanol and CO 2 (Mayer and Temperli, 1963;Osothsilp and Subden, 1986), resulting in the so-called malo-ethanolic fermentation.…”

Section: Yeastmentioning

confidence: 99%

Malo‐ethanolic fermentation in grape must by recombinant strains of Saccharomyces cerevisiae

Volschenk

Viljoen-Bloom

Subden

et al. 2001

Yeast

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Recombinant strains of Saccharomyces cerevisiae with the ability to reduce wine acidity could have a significant influence on the future production of quality wines, especially in cool climate regions. L-Malic acid and L-tartaric acid contribute largely to the acid content of grapes and wine. The wine yeast S. cerevisiae is unable to effectively degrade L-malic acid, whereas the fission yeast Schizosaccharomyces pombe efficiently degrades high concentrations of L-malic acid by means of a malo-ethanolic fermentation. However, strains of Sz. pombe are not suitable for vinification due to the production of undesirable off-flavours. Heterologous expression of the Sz. pombe malate permease (mae1) and malic enzyme (mae2) genes on plasmids in S. cerevisiae resulted in a recombinant strain of S. cerevisiae that efficiently degraded up to 8 g/l L-malic acid in synthetic grape must and 6.75 g/l L-malic acid in Chardonnay grape must. Furthermore, a strain of S. cerevisiae containing the mae1 and mae2 genes integrated in the genome efficiently degraded 5 g/l of L-malic acid in synthetic and Chenin Blanc grape musts. Furthermore, the malo-alcoholic strains produced higher levels of ethanol during fermentation, which is important for the production of distilled beverages.

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

Cited by 42 publications

References 71 publications

Comparison of partial malolactic enzyme gene sequences for phylogenetic analysis of some lactic acid bacteria species and relationships with the malic enzyme

Comparison of partial malolactic enzyme gene sequences for phylogenetic analysis of some lactic acid bacteria species and relationships with the malic enzyme

A pre-genetic study of the isoforms of malic enzyme associated with lipid accumulation in Mucor circinelloides

Malo‐ethanolic fermentation in grape must by recombinant strains of Saccharomyces cerevisiae

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