the Oenococcus oeni lysine racemase has a specific activity towards basic amino acids, residues Thr224 and Trp355 are important for enzyme substrate specificity
the Oenococcus oeni lysine racemase has a specific activity towards basic amino acids, residues Thr224 and Trp355 are important for enzyme substrate specificity
enzyme residue S394 residue plays a crucial role in determining the preference of Lyr to lysine and arginine. No activity by wild-type and mutant enzyme with alanine, methionine, histidine, tryptophan, leucine, glutamine, asparagine and serine
enzyme residue S394 residue plays a crucial role in determining the preference of Lyr to lysine and arginine. No activity by wild-type and mutant enzyme with alanine, methionine, histidine, tryptophan, leucine, glutamine, asparagine and serine
lysine racemase, although functionally inactive for growth purposes, may still have regulatory significance in permitting cross-induction of D-lysine-related enzymes by L-lysine, and vice versa
L-Lys gives rise to L-pipecolate that is utilized in the biosynthesis of the piperidine alkaloids 1-acetoxy-6-aminooctahydroindolizine and 3,4,5-trihydroxyoctahydro-1-pyridine. D-Lys is converted to D-N6-acetyllysine prior to further catabolism
the Oenococcus oeni lysine racemase has a specific activity towards basic amino acids, residues Thr224 and Trp355 are important for enzyme substrate specificity
the Oenococcus oeni lysine racemase has a specific activity towards basic amino acids, residues Thr224 and Trp355 are important for enzyme substrate specificity
lysine racemase, although functionally inactive for growth purposes, may still have regulatory significance in permitting cross-induction of D-lysine-related enzymes by L-lysine, and vice versa
L-Lys gives rise to L-pipecolate that is utilized in the biosynthesis of the piperidine alkaloids 1-acetoxy-6-aminooctahydroindolizine and 3,4,5-trihydroxyoctahydro-1-pyridine. D-Lys is converted to D-N6-acetyllysine prior to further catabolism
analyzing of bound metal ions in purified Lyr with an inductively coupled plasma spectrometer shows that dialyzed Lyr contains 0.77 mol of Zn2+ per mol of the dimeric enzyme, while cobalt, magnesium, manganese, nickel, or copper ions are absent
enzyme is incubated in 1 ml of reaction mixture containing 50 mM Tris-HCl (pH 8.0), 2 mM cobalt chloride and 10 mM L- or D-lysine at 30°C, Lyr activities in 4 week old wild type and transgenic tobacco plants are determined, the specific activity of Lyr in the transgenic T2 plants selected on L-lysine ranges from 0.77 to 1.06 mU/mg protein, although transgenic plants exhibit considerable variation in enzyme activities, no phenotypic dissimilarities associated with L-lysine selection are found, suggesting that the Lyr gene as a selectable marker could be effective over a range of expression levels
from garden soil, the lyr gene may have only recently evolved from Escherichia coli N-acetyl-gamma-glutamyl-phosphate reductase and Deinococcus radiodurans N-acyl amino acid racemase, the partial regions of both enzymes might have been combined to evolve a novel enzyme, in which the new catalytic sites are created for catalyzing the racemization of lysine
from soil, the lyr gene may have recently evolved from Escherichia coli N-acetyl-gamma-glutamyl-phosphate reductase and Deinococcus radiodurans N-acyl amino acid racemase, the partial regions of both enzymes might have been combined to evolve a novel enzyme, in which the new catalytic sites are created for catalyzing the racemization of lysine
enzyme Lyr catalyzes the conversion of D-lysine into L-lysine. Proteus mirabilis Lyr activity is independent of its putative signal peptide and can function in the eukaryotic endoplasmic reticulum
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, sitting drop vapor diffusion method, mixing of 2.5 mg/ml protein with 0.1 M sodium acetate, pH 4.6, 0.05 M lithium chloride, and 29% w/v PEG 8000, 20°C, X-ray diffraction structure determination and analysis at 1.74 A resolution
for D-lysine production, a two-step process for D-lysine production from L-lysine by the successive microbial racemization and asymmetric degradation with lysine racemase and decarboxylase is developed. L-lysine is rapidly racemized to give DL-lysine, and L-lysine is selectively catabolized to generate cadaverine by lysine decarboxylase. In order to obtain enantiopure D-lysine, chiral selective degradation of L-lysine from the reaction mixture of DL-lysine is necessary. Under optimal conditions, 750.7 mmol/l D-lysine is finally obtained from 1710 mmol/l L-lysine after 1 h of racemization reaction and 0.5 h of decarboxylation reaction. D-lysine yield can reach 48.8% with enantiomeric excess of 99% or more
in an attempt to limit extracellular Lyr (while retaining the catalytic activity), amino acids 1-36 are removed from the enzyme (LyrM37) and a C-terminal KDEL ER retention motif (LyrM37-KDEL) is added
for D-lysine production, a two-step process for D-lysine production from L-lysine by the successive microbial racemization and asymmetric degradation with lysine racemase and decarboxylase is developed. L-lysine is rapidly racemized to give DL-lysine, and L-lysine is selectively catabolized to generate cadaverine by lysine decarboxylase. In order to obtain enantiopure D-lysine, chiral selective degradation of L-lysine from the reaction mixture of DL-lysine is necessary. Under optimal conditions, 750.7 mmol/l D-lysine is finally obtained from 1710 mmol/l L-lysine after 1 h of racemization reaction and 0.5 h of decarboxylation reaction. D-lysine yield can reach 48.8% with enantiomeric excess of 99% or more
gene LYR, functional recombinant expression in Escherichia coli strain BL21(DE3), showing high lysine racemase activity. L-Lysine is rapidly racemized to give DL-lysine, and the D-lysine yield is approximately 48% after 0.5 h
recombinant expression of C-terminally HA-tagged wild-type enzyme and mutant enzyme LyrM37-KDEL, codon optimized for mouse expression, in C3H10T1/2 cells or MDA-MB-231 cells. MDA-MB-231 cells are infected with pGIPZ lentivirus for GFP expression, and C3H10T1/2 cells are infected with pMSCV-pBabeMCS-IRES-RFP retrovirus for RFP expression, identification of proteotypic Lyr peptides suitable for relative isotopic quantification. Wild-type Proteus mirabilis Lyr is prolifically secreted from eukaryotic cells in contrast to mutant enzyme LyrM37-KDEL. Extracellular Lyr converts labeled D-lysine to labeled L-lysine in conditioned media and severely compromises coculture labeling efficiency. Cells stably transfected with LyrM37-KDEL achieve proliferation comparable to that with L-lysine when grown on concentrations of D-lysine greater than 1 mM
transformation of the lyr gene in Nicotiana benthamiana and Arabidopsis thaliana plants by means of Agrobacterium tumefaciens strains LBA4404 and GV3101, transgenic plants produce normal roots that penetrate into the selection medium and are healthy, the Lyr gene is found to be expressed as a protein in all the transgenic lines
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
to investigate the effect of Lyr expression on the amino acid profile of the host cells, the composition of free amino acids in the leaves of wild-type and transgenic tobacco plants is determined, the results reveal a substantial 40fold and a marginal 4fold increase of free L-aspartate content in the wild-type and transgenic plants, respectively, grown on L-lysine medium as compared to plants grown on medium containing D-lysine or without lysine supplement
Biosynthesis of slaframine, (1S,6S,8aS)-1-acetoxy-6-aminooctahydroindolizine, a parasympathomimetic alkaloid of fungal origin. II. The origin of pipecolic acid