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LYS2 Lys2p

LYS2, Lys5, alpha-aminoadipate reductase
The protein encoded by this gene is similar to Saccharomyces cerevisiae LYS5, which is required for the activation of the alpha-aminoadipate dehydrogenase in the biosynthetic pathway of lysine. Yeast alpha-aminoadipate dehydrogenase converts alpha-biosynthetic-aminoadipate semialdehyde to alpha-aminoadipate. It has been suggested that defects in the human gene result in pipecolic acidemia. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, STEP, POLYMERASE
Papers on LYS2
Identification of the Sfp-Type PPTase EppA from the Lichenized Fungus Evernia prunastri.
Bode et al., Frankfurt am Main, Germany. In Plos One, Dec 2015
The Sfp-type PPTase EppA was functionally characterized through heterologous expression in E. coli using the production of the blue pigment indigoidine as readout and by complementation of a lys5 deletion in S. cerevisiae.
Auxotrophic Mutations Reduce Tolerance of Saccharomyces cerevisiae to Very High Levels of Ethanol Stress.
Thevelein et al., Leuven, Belgium. In Eukaryot Cell, Sep 2015
Analysis of other auxotrophies also revealed significant linkage for LYS2, LEU2, HIS3, and MET15.
Toxicity, mutagenicity and transport in Saccharomyces cerevisiae of three popular DNA intercalating fluorescent dyes.
Serrano et al., Valencia, Spain. In Yeast, Sep 2015
All three compounds increase reversion of a chromosomal point mutation (lys2-801(amber) ), with Gelred being the most mutagenic and Redsafe the least.
Characterization of NpgA, a 4'-phosphopantetheinyl transferase of Aspergillus nidulans, and evidence of its involvement in fungal growth and formation of conidia and cleistothecia for development.
Jahng et al., Iksan, South Korea. In J Microbiol, 2015
Sequencing analysis of the complementing gene indicated that it contained a 4'-phosphopantetheinyl transferase (PPTase) superfamily domain.
Transcriptomic and biochemical evidence for the role of lysine biosynthesis against linoleic acid hydroperoxide-induced stress in Saccharomyces cerevisiae.
Wu et al., Sydney, Australia. In Free Radic Res, 2014
A comprehensive up-regulation of lysine biosynthetic genes (LYS1, LYS2, LYS4, LYS9, LYS12, LYS20 and LYS21) was revealed in dal80Δ following the oxidant challenge.
Cbc2p, Upf3p and eIF4G are components of the DRN (Degradation of mRNA in the Nucleus) in Saccharomyces cerevisiae.
Das et al., Calcutta, India. In Fems Yeast Res, 2014
IMP3 and YLR194c mRNAs); and (3) mutant mRNAs for example, lys2-187 and cyc1-512.
Disrupting the methionine biosynthetic pathway in Candida guilliermondii: characterization of the MET2 gene as counter-selectable marker.
Papon et al., Tours, France. In Yeast, 2014
The MET2 wild-type allele, flanked by two short repeated sequences, was then used to disrupt the LYS2 gene (encoding the α-aminoadipate reductase) in the C. guilliermondii met2 recipient strain.
MoLys2 is necessary for growth, conidiogenesis, lysine biosynthesis, and pathogenicity in Magnaporthe oryzae.
Zhang et al., Nanjing, China. In Fungal Genet Biol, 2014
In filamentous fungus Penicillium chrysogenum, disruption of the LYS2 gene blocked the lysine biosynthesis but promoted the production of the secondary metabolite penicillin.
[Effects of ceruloplasmin/PTEN on histone modifications induced by silica].
Ye et al., In Wei Sheng Yan Jiu, 2014
RESULTS: Silica could induce the high level of protein lysine acetylation and acetyl-histone H2B (lys5/12), acetyl-histone H3 (lys9/14), acetyl-histone H4 (lys12) and the low level of methyl-histone (arg2), which could be reversed by Cp, in no exception for acetyl-histone H2B (lys5/12).
Fitness costs of minimal sequence alterations causing protein instability and toxicity.
Korona et al., Kraków, Poland. In Mol Biol Evol, 2014
We derived collections of temperature-sensitive, and thus structurally unstable, mutants of the yeast ADE2 and LYS2 genes by introducing single or very few amino acids substitutions.
Use of advanced recombinant lines to study the impact and potential of mutations affecting starch synthesis in barley.
Smith et al., Norwich, United Kingdom. In J Cereal Sci, 2014
The lys5 mutation conditioned low grain weight and starch content, but exceptionally high β-glucan contents.
Acyl carrier protein-specific 4'-phosphopantetheinyl transferase activates 10-formyltetrahydrofolate dehydrogenase.
Krupenko et al., Charleston, United States. In J Biol Chem, 2010
Our study identifies human PPT as the FDH-modifying enzyme and supports the hypothesis that mammals utilize a single enzyme for all phosphopantetheinylation reactions.
Multimeric options for the auto-activation of the Saccharomyces cerevisiae FAS type I megasynthase.
Grininger et al., Martinsried, Germany. In Structure, 2009
Results structurally and functionally characterized the FAS type I PPT as part of the multienzyme protein and as an isolated domain.
Cloning and characterization of a novel human homolog* of mouse U26, a putative PQQ-dependent AAS dehydrogenase.
Mao et al., Shanghai, China. In Mol Biol Rep, 2005
Human 2-aminoadipic 6-semialdehyde dehydrogenase gene was cloned; its mRNA is ubiquitously expressed in adult tissues and is highly expressed in colon adenocarcinoma (CX-1) and colon adenocarcinoma (GI-112) cell lines.
Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity.
Smith et al., Oakland, United States. In J Biol Chem, 2003
humans appear to utilize a single, broad specificity enzyme, 4'-phosphopantetheine transferase, for all posttranslational 4'-phosphopantetheinylation reactions
Nuclear organization and transcriptional silencing in yeast.
Gasser et al., Lausanne, Switzerland. In Experientia, 1997
Elevation of the internal nuclear pools of Sir1p, Sir3p and Sir4p can relieve the lack of repression at the LYS2 locus in an additive manner, suggesting that in wild-type cells silencer function is facilitated by its juxtaposition to a pool of highly concentrated Sir proteins, such as those created by telomere clustering.
Association of increased spontaneous mutation rates with high levels of transcription in yeast.
Jinks-Robertson et al., Atlanta, United States. In Science, 1995
With the use of a lys2 frameshift allele under the control of a highly inducible promoter, the rate of spontaneous reversion was shown to increase when the mutant gene was highly transcribed.
alpha-Aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes.
Bhattacharjee, In Crit Rev Microbiol, 1984
The gene-enzyme relationships have been determined for ten of the lysine loci which include two unlinked gene functions required for each of AA reductase (LYS2 and LYS5) and Saccharopine reductase (LYS9 and LYS14).
Preferential integration of yeast transposable element Ty into a promoter region.
Philippsen et al., In Nature, 1984
We chose the LYS2 gene to investigate these questions because it allows direct selection of both mutants and revertants.
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