| Standard Name | GND2 |
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| Systematic Name | YGR256W |
| Feature Type | ORF, Verified |
| Description | 6-phosphogluconate dehydrogenase (decarboxylating); catalyzes an NADPH regenerating reaction in the pentose phosphate pathway; required for growth on D-glucono-delta-lactone; GND2 has a paralog, GND1, that arose from the whole genome duplication (1 and see Summary Paragraph) |
| Chromosomal Location | |
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| View Computational GO annotations for GND2 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
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| Classical genetics | |
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| unspecified | |
| Large-scale survey | |
| null |
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| Resources |
| 34 total interaction(s) for 30 unique genes/features. | |
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| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
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| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000003488 |
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In Saccharomyces cerevisiae, GND1 encodes the major isoform of phosphogluconate dehydrogenase, accounting for approximately 80% of activity, and GND2 encodes the minor isoform (1). Phosphogluconate dehydrogenase (EC:1.1.1.44) is a key enzyme in the cytosolic oxidative branch of the pentose phosphate pathway (2), and catalyzes the second oxidative reduction of NADP+ to NADPH (3, 4, 1). Phosphogluconate dehydrogenase is also important for protecting yeast from oxidative stress, since NADPH is an essential cofactor for the Glr1p glutathione reductase as well as the Trr1p and Trr2p thioredoxin reductases, which defend cells against oxidative damage (5).
GND2 is induced in mot1-14 mutants, during aerobic growth as compared to anaerobic growth, and in response to alpha-factor or stress (6, 7, 8, 9). gnd2 null mutants are viable (1), but display reduced growth on D-glucono-delta-lactone and reduced induction of 6-phosphogluconolactonase (SOL3 & SOL4) in response to D-glucono-delta-lactone (1). Gnd2p displays similarity to Gnd1p, and the 6-phosphogluconate dehydrogenases of Candida parapsilosis, Cryptococcus neoformans, and human (10, 11).
| 1) | Sinha A and Maitra PK (1992) Induction of specific enzymes of the oxidative pentose phosphate pathway by glucono-delta-lactone in Saccharomyces cerevisiae. J Gen Microbiol 138(9):1865-73 |
| 2) | Maaheimo H, et al. (2001) Central carbon metabolism of Saccharomyces cerevisiae explored by biosynthetic fractional (13)C labeling of common amino acids. Eur J Biochem 268(8):2464-79 |
| 3) | Bro C, et al. (2004) Genome-wide transcriptional response of a Saccharomyces cerevisiae strain with an altered redox metabolism. Biotechnol Bioeng 85(3):269-76 |
| 4) | Palecek SP, et al. (2002) Depression of Saccharomyces cerevisiae invasive growth on non-glucose carbon sources requires the Snf1 kinase. Mol Microbiol 45(2):453-69 |
| 5) | Izawa S, et al. (1998) Importance of glucose-6-phosphate dehydrogenase in the adaptive response to hydrogen peroxide in Saccharomyces cerevisiae. Biochem J 330 ( Pt 2)():811-7 |
| 6) | Bro C, et al. (2003) Transcriptional, proteomic, and metabolic responses to lithium in galactose-grown yeast cells. J Biol Chem 278(34):32141-9 |
| 7) | Dasgupta A, et al. (2002) Mot1 activates and represses transcription by direct, ATPase-dependent mechanisms. Proc Natl Acad Sci U S A 99(5):2666-71 |
| 8) | Ter Linde JJ, et al. (1999) Genome-wide transcriptional analysis of aerobic and anaerobic chemostat cultures of Saccharomyces cerevisiae. J Bacteriol 181(24):7409-13 |
| 9) | Zhang W, et al. (2003) Microarray analyses of the metabolic responses of Saccharomyces cerevisiae to organic solvent dimethyl sulfoxide. J Ind Microbiol Biotechnol 30(1):57-69 |
| 10) | Caubet R, et al. (1988) Comparative studies on the glycolytic and hexose monophosphate pathways in Candida parapsilosis and Saccharomyces cerevisiae. Arch Microbiol 149(4):324-9 |
| 11) | Niehaus WG, et al. (1995) Polyethylene sulfonate: a tight-binding inhibitor of 6-phosphogluconate dehydrogenase of Cryptococcus neoformans. Arch Biochem Biophys 324(2):325-30 |






