Occurrence of a novel yeast enzyme, l-Lysine  -dehydrogenase, which catalyses the first step of lysine catabolism in Candida albicans

Hammer, T.; Bode, R.; Birnbaum, D.

doi:10.1099/00221287-137-3-711

Cited by 13 publications

(7 citation statements)

References 10 publications

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“…These pathways have never been identified in S. cerevisiae isolates, confirming the inability of this yeast to consume Lys as sole nitrogen source (Neschich et al, 2012). However, they were detected in other yeast species, including some species close to the Starmerella clade (Hammer et al, 1991;Zhang et al, 2017), which is in line with the results of the present study. The main metabolic route responsible for His assimilation in most organisms, involves in a first step a histidine ammonialyase.…”

Section: Discussionsupporting

confidence: 93%

Influence of Single Nitrogen Compounds on Growth and Fermentation Performance ofStarmerella bacillarisandSaccharomyces cerevisiaeduring Alcoholic Fermentation

Englezos

Cocolin

Rantsiou

et al. 2021

Appl Environ Microbiol

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Nitrogen is among the essential nutriments that govern interactions between yeast species in the wine environment. A thorough knowledge of how these yeasts assimilate the nitrogen compounds of grape juice is an important prerequisite for a successful co- or sequential fermentation. In the present study, we investigated the efficiency of 18 nitrogen sources for sustaining the growth and fermentation of two Starm. bacillaris strains displaying metabolic properties, compared to the reference yeast S. cerevisiae. The analysis of growth and fermentation parameters provided a comprehensive picture of Starm. bacillaris preferences with respect to nitrogen sources for sustained growth and fermentation. Important differences were observed in S. cerevisiae regarding rates, final population and CO2 production. In particular, Lys and His supported substantial Starm. bacillaris growth and fermentation contrary to S. cerevisiae, while only 3 nitrogen sources, Arg, NH4+ and Ser, promoted S. cerevisiae growth more efficiently than that of Starm. bacillaris strains. Furthermore, Starm. bacillaris strains displayed a higher fermentative activity than S. cerevisiae during the first phase of culture with Gly or Thr, when the former species consumed solely fructose. Finally, no correlation has been shown between the ability of nitrogen sources to support growth and their fermentation efficiency. The specificities of Starm. bacillaris regarding nitrogen sources preferences are related to its genetic background, but further investigations are needed to elucidate the molecular mechanisms involved. These data are essential elements to be taken into account in order to make the best use of the potential of the two species.IMPORTANCE Mixed fermentations combining non-Saccharomyces and S. cerevisiae strains are increasingly implemented in the wine sector as they offer promising opportunities to diversify the flavour profile of end-products. However, competition for nutrients between species can cause fermentation problems, which is a severe hindrance to the development of these approaches. With the knowledge provided in this study on the nitrogen preferences of Starm. bacillaris, winemakers will be able to set up a nitrogen nutrition scheme adapted to the requirement of each species during mixed fermentation, through must supplementation with relevant nitrogen compounds. This will prevent nitrogen depletion or competition between yeasts for nitrogen sources, and consequently potential issues during fermentation. The data of this study highlight the importance of an appropriate nitrogen resource management during co- or sequential fermentation for fully exploiting the phenotypic potential of non-Saccharomyces yeasts.

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Section: Discussionsupporting

confidence: 93%

Influence of Single Nitrogen Compounds on Growth and Fermentation Performance ofStarmerella bacillarisandSaccharomyces cerevisiaeduring Alcoholic Fermentation

Englezos

Cocolin

Rantsiou

et al. 2021

Appl Environ Microbiol

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“…In this regard, GluDH may have a preference for NAD, NADP, or both dependent on cellular location and function (14). The bacterial L-lysine ε-dehydrogenase is specific for NAD (15), while the yeast enzyme is NADP-specific (16). All known examples of LeuDH (17) are specific for NAD, as are PheDH (18) and AlaDH (19).…”

Section: Inhibitory Nucleotide Analogues-k I Values For Dead-end Inhimentioning

confidence: 99%

“…Many of the dehydrogenases have been studied with respect to alternative dinucleotide substrates (15)(16)(17)(18)(19). 3-APAD is a better substrate for LeuDH (166%) and PheDH (241%) than is NAD, and thio-NAD (101%) is as good as NAD for PheDH.…”

Section: Inhibitory Nucleotide Analogues-k I Values For Dead-end Inhimentioning

confidence: 99%

Determinants of Substrate Specificity for Saccharopine Dehydrogenase from Saccharomyces cerevisiae

West

Cook

2007

Biochemistry

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A survey of NADH, α-Kg, and lysine analogues has been undertaken to define the substrate specificity of saccharopine dehydrogenase, and to identify functional groups on all substrates and dinucleotides important for substrate binding. A number of NAD analogues, including NADP, 3-acetylpyridine adenine dinucleotide (3-APAD), 3-pyridinealdehyde adenine dinucleotide (3-PAAD), and thionicotinamide adenine dinucleotide (thio-NAD), can serve as a substrate in the oxidative deamination reaction, as can a number of α-keto analogues, including glyoxylate, pyruvate, α-ketobutyrate, α-ketovalerate, α-ketomalonate, and α-ketoadipate. Inhibition studies using nucleotide analogues suggest that the majority of the binding energy of the dinucleotides comes from the AMP portion, and that distinctly different conformations are generated upon binding of the oxidized and reduced dinucleotides. Addition of the 2'-phosphate as in NADPH causes poor binding of subsequent substrates, but has little effect on coenzyme binding and catalysis. In addition, the 10-fold decrease in affinity of 3-APAD in comparison to NAD suggests that the nicotinamide ring binding pocket is hydrophilic. Extensive inhibition studies using aliphatic and aromatic keto acid analogues have been carried out to gain insight into the keto acid binding pocket. Data suggest that a side chain with 3 carbons (from the α-keto group up to and including the side chain carboxylate) is optimal. In addition, the distance between the C1-C2 unit and the C5 carboxylate of the α-keto acid is also important for binding; the α-oxo group contributes a factor of 10 in affinity. The keto acid binding pocket is relatively large and flexible, can accommodate the bulky aromatic ring of a pyridine dicarboxylic acid, and a negative charge at the C3 but not the C4 position. However, the amino acid binding site is hydrophobic and the optimal length of the hydrophobic portion of amino acid carbon side chain is 3 or 4 carbons. In addition, the amino acid binding pocket can accommodate a branch at the γ-carbon, but not at the β-carbon.Saccharopine dehydrogenase (N6-(glutaryl-2)-L-lysine: NAD oxidoreductase (L-lysine forming); (EC 1.5.1.7)) (SDH 1 ) catalyzes the last step of the α-aminoadipate (AAA) pathway for the de novo synthesis of L-lysine in fungi. The reaction involves the reversible pyridine † This work is supported by the Grayce B. Kerr Endowment to the University of Oklahoma (to P. F. C.), and a grant (GM 071417) from the National Institutes of Health (to P. F. C. and A. H. W.). *Corresponding author: E-mail: pcook@chemdept.chem.ou.edu Tel: 405−325−4581 Fax: 405−325−7182. 1 Abbreviations: SDH, saccharopine dehydrogenase; AAA, α-aminoadipate pathway; NAD(P), β-nicotinamide adenine dinucleotide (phosphate) (the + charge is omitted for convenience); NADH(P), reduced β-nicotinamide adenine dinucleotide (phosphate); NADD, reduced nicotinamide adenine dinucleotide with deuterium in the 4R position; AMP, adenosine 5'-monophosphate; ADP, adenosine 5'-

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“…Since then, this enzyme has been purified, characterized (8,15,18), and utilized for L-lysine determination (4,9). In addition to the A. tumefaciens LysDH, the enzyme from the yeast Candida albicans has been partially characterized (7). In contrast, there has been only one report of a human liver L-lysine 2-dehydrogenase catalyzing the deamination of the ␣-amino group (2).…”

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Highly Stable l -Lysine 6-Dehydrogenase from the Thermophile Geobacillus stearothermophilus Isolated from a Japanese Hot Spring: Characterization, Gene Cloning and Sequencing, and Expression

Heydari

Ohshima

Nunoura-Kominato

et al. 2004

Appl Environ Microbiol

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L-Lysine dehydrogenase, which catalyzes the oxidative deamination of L-lysine in the presence of NAD, was found in the thermophilic bacterium Geobacillus stearothermophilus UTB 1103 and then purified about 3,040-fold from a crude extract of the organism by using four successive column chromatography steps. This is the first report showing the presence of a thermophilic NAD-dependent lysine dehydrogenase. The product of the enzyme catalytic activity was determined to be ⌬ 1 -piperideine-6-carboxylate, indicating that the enzyme is L-lysine 6-dehydrogenase (LysDH) (EC 1.4.1.18). The molecular mass of the purified protein was about 260 kDa, and the molecule was determined to be a homohexamer with subunit molecular mass of about 43 kDa. The optimum pH and temperature for the catalytic activity of the enzyme were about 10.1 and 70°C, respectively.

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Occurrence of a novel yeast enzyme, l-Lysine -dehydrogenase, which catalyses the first step of lysine catabolism in Candida albicans

Cited by 13 publications

References 10 publications

Influence of Single Nitrogen Compounds on Growth and Fermentation Performance ofStarmerella bacillarisandSaccharomyces cerevisiaeduring Alcoholic Fermentation

Influence of Single Nitrogen Compounds on Growth and Fermentation Performance ofStarmerella bacillarisandSaccharomyces cerevisiaeduring Alcoholic Fermentation

Determinants of Substrate Specificity for Saccharopine Dehydrogenase from Saccharomyces cerevisiae

Highly Stable l -Lysine 6-Dehydrogenase from the Thermophile Geobacillus stearothermophilus Isolated from a Japanese Hot Spring: Characterization, Gene Cloning and Sequencing, and Expression

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