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Literature summary extracted from

  • Tape, C.J.; Norrie, I.C.; Worboys, J.D.; Lim, L.; Lauffenburger, D.A.; Joergensen, C.
    Cell-specific labeling enzymes for analysis of cell-cell communication in continuous co-culture (2014), Mol. Cell. Proteomics, 13, 1866-1876 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
5.1.1.5 additional information the enzyme is used for isotopic labeling of cells Proteus mirabilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.5 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 Proteus mirabilis

Protein Variants

EC Number Protein Variants Comment Organism
5.1.1.5 additional information 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 Proteus mirabilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.1.5 L-lysine Proteus mirabilis
-
D-lysine
-
r

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.5 Proteus mirabilis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.5 L-lysine
-
Proteus mirabilis D-lysine
-
r

Subunits

EC Number Subunits Comment Organism
5.1.1.5 More Lyr contains a globular catalytic core (amino acids 37-407) distinct from the putative signal peptide Proteus mirabilis

Synonyms

EC Number Synonyms Comment Organism
5.1.1.5 lyr
-
Proteus mirabilis

General Information

EC Number General Information Comment Organism
5.1.1.5 additional information unlike wild-type enzyme LyrWT, enzyme mutant LyrM37-KDEL is a truly intracellular D-lysine conversion enzyme Proteus mirabilis
5.1.1.5 physiological function 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 Proteus mirabilis