Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

When studying mutants affecting lysyl-tRNA synthetase or tRNAlys (hisT, hisW), a lack of correlation is clearly observed between the amount of lysyl-tRNA and the level of derepression of several lysine biosynthetic enzymes. This exlcudes the possible role of lysyl-tRNA as the specific corepressor of the lysine regulon. However, the level of derepression of DAP-decarboxylase, the last enzyme of the lysine pathway, is very low in the hisT mutant; this indicates that tRNAlys is a secondary effector involved in the regulation of the synthesis of this enzyme.
Mol Gen Genet 1978 Feb 07
PMID:Effect of mutations affecting lysyl-tRNAlys on the regulation of lysine biosynthesis in Escherichia coli. 34 82

Pseudomonas syringae pv. tabaci strain PTBR2.024 produces tabtoxin and causes wildfire disease on tobacco and green bean. PTBR7.000, a Tn5 mutant of PTBR2.024, does not produce tabtoxin, is nonpathogenic on tobacco, and is prototrophic. A 3-kb fragment from a genomic library of the parent strain PTBR2.024 complemented both mutant phenotypes. This 3-kb fragment contains two open reading frames (ORFs), ORF1 and ORF2, and two truncated ORFs, ORF3 and ORF4. The Tn5 insert in PTBR7.000 was mapped to ORF2, and complementation studies showed that an intact ORF2 was sufficient to restore tabtoxin production and pathogenicity. The deduced amino acid sequences of ORF2 and truncated ORF3 contain significant homology to bacterial lysine biosynthetic enzymes, diaminopimelate decarboxylase, and delta 1-piperidine-2,6-dicarboxylate succinyl transferase, respectively. ORF2, however, is not required for lysine biosynthesis. We designated the sequence corresponding to ORF2 as gene tabA and propose that the product of tabA is an enzyme in the tabtoxin biosynthetic pathway that recognizes a substrate analogue of a compound in the lysine biosynthetic pathway.
Mol Plant Microbe Interact
PMID:Identification of a lysA-like gene required for tabtoxin biosynthesis and pathogenicity in Pseudomonas syringae pv. tabaci strain PTBR2.024. 151 68

The Pseudomonas aeruginosa lysA gene encoding diaminopimelate decarboxylase (DAP-decarboxylase) was cloned into a broad host range vector. This gene complemented a lys mutation at the lys-12 locus of P. aeruginosa and a lysA defect in Escherichia coli. The P. aeruginosa DAP-decarboxylase was synthesized constitutively in P. aeruginosa as well as in E. coli, where the Pseudomonas lysA gene was poorly expressed. By contrast, the E. coli lysA gene was expressed well in P. aeruginosa and subject to lysine regulation when the E. coli LysR activator protein was provided. This indicates that the mechanism of transcriptional activation for the E. coli lysA gene is effective in the heterologous host.
Mol Gen Genet 1986 Jun
PMID:Heterologous expression and regulation of the lysA genes of Pseudomonas aeruginosa and Escherichia coli. 301 30

We utilized diaminopimelate-lysine mutants of Escherichia coli K12 to clone the genes specifically involved in the Corynebacterium glutamicum diaminopimelate-lysine anabolic pathway. From a cosmid genomic bank of C. glutamicum strain AS019, we isolated cosmids pSM71, pSM61 and pSM531, that are respectively able to complement dapA/dapB, dapD, and lysA mutants of E. coli. DNA hybridization analysis indicates that these complementing genes are located on the chromosome of C. glutamicum in at least three separate transcription units. Subcloning of parental cosmids in dapA, dapD, and lysA mutants of E. coli localized these genes, respectively, within 1.4, 3.4, and 1.8 kb fragments, cloned in an E. coli/C. glutamicum shuttle vector. Enzymatic analysis in C. glutamicum identified the dapA-complementing gene as L-2,3-dihydrodipicolinate synthetase (dapA), and the lysA-complementing gene as meso-diaminopimelate decarboxylase (lysA). In contrast, complementation of E. coli dapD8, presumably lacking L-delta 1-tetrahydrodipicolinate synthetase (dapD), led us to clone a diaminopimelate-lysine anabolic gene of C. glutamicum which does not exist in E. coli: meso-diaminopimelate dehydrogenase. Although meso-diaminopimelate is crucial in lysine formation and in cell wall biosynthesis, expression of the genomic copies of the cloned genes, which encode activities involved at key branching points of the diaminopimelate-lysine pathway of C. glutamicum, appears constitutive with regard to the addition of diaminopimelate and/or lysine during cell growth.
Mol Gen Genet 1988 Apr
PMID:General organization of the genes specifically involved in the diaminopimelate-lysine biosynthetic pathway of Corynebacterium glutamicum. 313 36

A number of B. subtilis mutants auxotrophic for lysine has been isolated and mapped in relation to the flanking ser2 marker. One of the mutants has been found to have a mutation in lys A gene coding for DAP-decarboxylase activity. The expression of DAP-decarboxylase is dependent on the product of lys R gene that is not linked with lysine genes cluster.
Mol Gen Mikrobiol Virusol 1988 Jun
PMID:[Analysis of mutants of Bacillus subtilis, auxotrophic for lysine]. 313 99

The allelic state of relA influences the phenotype of Escherichia coli strains carrying the lysA22 mutation:lysA22 relA strains are Lys- where lysA22 relA+ strains grow (slowly) in the absence of lysine. This physiological effect has been related to an effect of the expression of the relA locus on the regulation of lysine biosynthesis. The fully derepressed levels of some lysine enzymes (aspartokinase III, aspartic semialdehyde dehydrogenase, didhydrodipicolinate reductase) are observed under lysine limitation only in rel+ strains. And the induction of DAP-decarboxylase by DAP is much higher in rel+ than in rel- strains when an amino acid limitation of growth is also realised. These results are in agreement with the hypothesis of Stephens et al. (1975) on a possible role of the stringent regulation as a general signal for amino acid deficiency.
Mol Gen Genet 1980
PMID:The relA locus and the regulation of lysine biosynthesis in Escherichia coli. 611 Jan 61

The synthesis of diaminopimelate decarboxylase, which catalyzes the decarboxylation of diaminopimelate into lysine, is known to be repressed by lysine and induced by diaminopimelate in Escherichia coli K12. Until now only mutations in lysA, the structural gene for diaminopimelate decarboxylase, have been described that lead to a Lys- phenotype. A set of plasmids carrying adjacent inserts of the lysA region was constructed and employed to transform different Lys- mutants. The complementation pattern observed and the corresponding expression of the lysA gene show that in fact the Lys- phenotype can be obtained by mutations in two different and closely linked loci: one being the lysA structural gene, and the other called lysR. We propose that the lysR gene encodes a positive effector required for the full expression of the lysA gene. The synthesis of a hybrid lysA-lacZ protein constructed in vitro was observed to be decreased dramatically in lysR mutants. Moreover, all the regulatory features were lost, indicating that the LysR activator is necessary for the regulation of lysA expression. The gene order is thyA lysA lysR clockwise around 61 minutes on the chromosome, lysA being transcribed counter-clockwise.
J Mol Biol 1983 Aug 05
PMID:Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. I. Identification of a lysR gene encoding an activator of the lysA gene. 641 28

Regulation of aspartate kinase and diaminopimelate decarboxylase activities in Streptococcus bovis and Enterococcus faecium cell-free extracts was studied. The levels of synthesis of aspartate kinase and diaminopimelate decarboxylase in both microorganisms are growth-dependent. The synthesis of these enzymes is depressed by lysine, but the activity of aspartate kinase is induced by addition of this amino acid and threonine to the reaction system. Meso-diaminopimelate dehydrogenase activity was not found in the extracts of Streptococcus bovis and Enterococcus faecium. The data excludes the possibility of lysine formation via six enzyme reactions.
Mol Gen Mikrobiol Virusol
PMID:[Regulation of enzymes of the first and last stage of lysine biosynthesis in Streptococcus bovis and Enterococcus faecium]. 828 39

In the compatible interaction between Arabidopsis thaliana and the endoparasitic nematode Meloidogyne incognita, galls are formed on the roots of the host plant. Differential display was used to identify alterations of gene expression in young A. thaliana root galls caused by M. incognita. Six genes were confirmed as plant genes by DNA gel blot hybridizations. Significant homology was found with a trypsin inhibitor, peroxidase, mitochondrial uncoupling protein, endomembrane protein, 20S proteasome alpha-subunit, and diaminopimelate decarboxylase. The cellular and temporal expression of each of the six genes was analyzed by mRNA in situ hybridizations.
Mol Plant Microbe Interact 2001 Mar
PMID:Arabidopsis thaliana genes expressed in the early compatible interaction with root-knot nematodes. 1127 26

Arginine decarboxylase (ADC) and ornithine decarboxylase (ODC) are involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria. These pyridoxal-5'-phosphate-dependent decarboxylases belong to the alanine racemase (AR) structural family together with diaminopimelate decarboxylase (DapDC), which catalyzes the final step of lysine biosynthesis in bacteria. We have constructed a multiple-sequence alignment of decarboxylases in the AR structural family and, based on the alignment, inferred phylogenetic trees. The phylogenetic tree consists of 3 distinct clades formed by ADC, DapDC, and ODC that diverged from an ancestral decarboxylase. The ancestral decarboxylase probably was able to recognize several substrates, and in archaea and bacteria, ODC may have retained the ability to bind other amino acids. Previously, a paralogue of ODC has been proposed to account for ADC activity detected in mammalian cells. According to our results, this appears unlikely, emphasizing the need for more caution in functional assignment made using sequence data and illustrating the continuing value of phylogenetic analysis in clarifying relationships and putative functions.
Mol Biol Evol 2007 Jan
PMID:Functional classification of amino acid decarboxylases from the alanine racemase structural family by phylogenetic studies. 1699 6


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