[157] Lysine biosynthesis (yeast)

Broquist, Harry P.

doi:10.1016/0076-6879(71)17021-8

Cited by 57 publications

(44 citation statements)

References 2 publications

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“…Another possible explanation for the attenuated virulence of the C. albicans sod1\sod1 cells observed here is likely to involve lysine biosynthesis. Since host cells do not possess the ability to synthesize lysine, an essential nutrient, infecting C. albicans cells can only utilize this limited nutrient via a de novo pathway (Broquist, 1971). However, this possibility seems to be very unlikely because the differences, if any, in the doubling times and yields between sod1\sod1 and wild-type or revertant pathogenic Ura + strains were very small when the strains were grown in minimal medium (Table 2).…”

Section: Discussionmentioning

confidence: 95%

Copper- and zinc-containing superoxide dismutase (Cu/ZnSOD) is required for the protection of Candida albicans against oxidative stresses and the expression of its full virulence

et al. 2002

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Copper-and zinc-containing superoxide dismutase (Cu/ZnSOD) is suspected to be one of the anti-oxidant enzymes and virulence determinants active in some pathogenic micro-organisms. To elucidate the role of Cu/ZnSOD in the major human fungal pathogen Candida albicans, its gene, designated SOD1, was disrupted by the URA-blaster technique. The resulting sod1/sod1 mutant showed delayed hyphal growth on Spider medium but could still form hyphae on other solid media or in liquid media, particularly in response to serum. Moreover, the sod1/sod1 mutant was more sensitive to menadione, a redoxcycling agent, than the isogenic wild-type strain, although it still showed an adaptive oxidative stress response. Furthermore, the sod1/sod1 mutant cells exhibited slow growth in minimal medium when compared to the wild-type cells, but their growth was restored by the addition of lysine to the medium. Interestingly, C. albicans cells lacking Cu/ZnSOD showed increased susceptibility to macrophage attack and had attenuated virulence in mice. Thus, these results suggest that Cu/ZnSOD is required for the protection of C. albicans against oxidative stresses and for the full virulence of the organism to be expressed.

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Section: Discussionmentioning

confidence: 95%

Copper- and zinc-containing superoxide dismutase (Cu/ZnSOD) is required for the protection of Candida albicans against oxidative stresses and the expression of its full virulence

et al. 2002

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“…thermophilus HB27 was cultivated as described previously [1,9,10]. Escherichia coli DH5K and JM105 [11] were used for DNA manipulation and E. coli BL21-CodonPlus (DE3)-RIL [F 3 , ompT, hsdS (r vation of E. coli cells.…”

Section: Strains Media and Chemicalsmentioning

confidence: 99%

“…One is the diaminopimelate (DAP) pathway starting from aspartate via DAP, as seen in most bacteria and plants, the other is the Kaminoadipate (AAA) pathway from 2-oxoglutarate via AAA, as seen in yeast [1] and fungi [2,3]. In our recent studies, however, an extremely thermophilic bacterium, Thermus thermophilus HB27, was shown to synthesize lysine not via DAP, but through AAA [4].…”

Section: Introductionmentioning

confidence: 99%

Characterization of a lysK gene as an argE homolog in Thermus thermophilus HB27

et al. 2002

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We conducted a chromosome walk to obtain a DNA fragment downstream of lysJ and found an argE homolog in a putative operon composed of lysJ^orfC^orfD^argE homologs. A knockout mutant of the argE homolog showed significantly slow growth on a minimal medium, and the growth was markedly improved by addition of lysine. We therefore termed this gene lysK. Purified LysK protein has deacetylating activities for both N 2 -acetyllysine and N 2 -acetylornithine at almost equal efficiency. These results suggest that lysK which may share an ancestor with argE functions not only for the lysine biosynthesis, but also for arginine biosynthesis in Thermus thermophilus. ß 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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“…In the lysine biosynthesis pathway of yeast, α-AA reductase catalyses the conversion of α-AA to α-AA semialdehyde in a three-step reaction: (a) adenylation of α-AA with ATP to form α-AA-δ-adenylate and inorganic pyrophosphate; (b) reduction of α-AA-δ-adenylate by NADPH to α-AA-δ-adenyl-semialdehyde and NADP; (c) hydrolysis of α-aminoadipic-δ-adenyl-semialdehyde to α-AA semialdehyde and AMP (Bhattacherjee, 1992;Broquist, 1971;Sagisaka and Shimura, 1962). Accordingly, it has been found that the sequences of α-AA reductases contain several distinctive domains in common, supposed to be involved in catalytic activities (Casqueiro et al, 1998;Hijarrubia et al, 2001): the adenylating domain shows homology with enzymes involved in amino acid activation via adenylation and is characterized by nine conserved motifs, including the AMP-binding and ATP-binding domains; the reductive domain, responsible for the reduction of the activated α-AA to its semialdehyde, showing homologies with dehydrogenases; a region is involved in phosphopantetheinylation, a post-translational modification mediated by the product of LYS5 gene and required for the activation of the LYS2-encoded α-AA reductase (Ehmann et al, 1999).…”

Section: Sequence Of Kllys2 Genementioning

confidence: 99%

LYS2 gene and its mutation in Kluyveromyces lactis

Alberti

Ferrero

Lodi

2003

Yeast

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The KlLYS2 gene, encoding the α-aminoadipate reductase of Kluyveromyces lactis, was isolated by complementation of a lysA1 mutant. The deduced amino acid sequence shared an identity of 73% with the LYS2 product of Saccharomyces cerevisiae. Despite the high sequence homology of the α-aminoadipate reductase genes, the two yeast species differently responded to the presence of α-aminoadipate in the medium. Wildtype S. cerevisiae is known to be sensitive to α-aminoadipate, but becomes resistant when mutated to lys2. In contrast, K. lactis strains were found to be naturally resistant to α-aminoadipate. Therefore, the positive selection procedure for the isolation of lys2 mutants on α-aminoadipate, as practised in S. cerevisiae, cannot be applied to K. lactis. A possible reason of this difference may be that the catalytic rate of the α-aminoadipate reductase differs in the two yeasts. The EMBL/Genbank Accession No. for the KlLYS2 gene is AJ504405.

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[157] Lysine biosynthesis (yeast)

Cited by 57 publications

References 2 publications

Copper- and zinc-containing superoxide dismutase (Cu/ZnSOD) is required for the protection of Candida albicans against oxidative stresses and the expression of its full virulence

Copper- and zinc-containing superoxide dismutase (Cu/ZnSOD) is required for the protection of Candida albicans against oxidative stresses and the expression of its full virulence

Characterization of a lysK gene as an argE homolog in Thermus thermophilus HB27

LYS2 gene and its mutation in Kluyveromyces lactis

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