leucyl การใช้

• Oxytocin is known to be metabolized by the oxytocinase, leucyl / cystinyl aminopeptidase.
• Tavaborole inhibits an essential fungal enzyme, leucyl-tRNA synthetase, that is required for protein synthesis.
• Tavaborole inhibits an essential fungal enzyme, leucyl-transfer RNA synthetase, or LeuRS, required for protein synthesis.
• The systematic name of this enzyme class is "'L-leucyl-tRNA : protein leucyltransferase " '.
• This gene encodes a G protein-coupled receptor cell surface protein that binds and is activated by N-Formylmethionine-containing oligopeptides, particularly N-Formylmethionine-leucyl-phenylalanine ( FMLP ).
• Many oligopeptides that possess a N-Formylmethionine " N "-terminal residue such as the prototypical tripeptide N-Formylmethionine-leucyl-phenylalanine ( i . e . FMLP ), are products of the protein synthesis conducted by bacteria.
• "' Ubenimex "'( leukotriene A 4 hydrolase ( a zinc metalloprotease that displays both epoxide hydrolase and aminopeptidase activities ), alanyl aminopeptidase ( aminopeptidase M / N ), leucyl / cystinyl aminopeptidase ( oxytocinase / vasopressinase ), and membrane dipeptidase ( leukotriene D 4 hydrolase ).
• The proteins used were the DNA polymerase III beta-subunit, initiation factor IF-2, leucyl-tRNA synthetase, the phenylalanine tRNA ligase beta-subunit, VARS, elongation factor Tu, the RNA polymerase beta-subunit, and the ribosomal proteins L2, S5, and S11.
• The prototypical fMet-containing oligopeptide is N-Formylmethionine-leucyl-phenylalanine ( FMLP ) which activates leukocytes and other cell types by binding with these cells'formyl peptide receptor 1 ( FPR1 ) and formyl peptide receptor 2 ( FPR2 ) G protein coupled receptors ( see also formyl peptide receptor 3 ).
• It specifically inhibits leucyl aminopeptidase, alanyl aminopeptidase ( aminopeptidase M / N ), bacterial leucyl aminopeptidase ( " Aeromonas proteolytica " aminopeptidase ), leucyl / cystinyl aminopeptidase ( oxytocinase / vasopressinase ), and, to a lesser extent, glutamyl aminopeptidase ( aminopeptidase A ), as well as other aminopeptidases.
• It specifically inhibits leucyl aminopeptidase, alanyl aminopeptidase ( aminopeptidase M / N ), bacterial leucyl aminopeptidase ( " Aeromonas proteolytica " aminopeptidase ), leucyl / cystinyl aminopeptidase ( oxytocinase / vasopressinase ), and, to a lesser extent, glutamyl aminopeptidase ( aminopeptidase A ), as well as other aminopeptidases.
• It specifically inhibits leucyl aminopeptidase, alanyl aminopeptidase ( aminopeptidase M / N ), bacterial leucyl aminopeptidase ( " Aeromonas proteolytica " aminopeptidase ), leucyl / cystinyl aminopeptidase ( oxytocinase / vasopressinase ), and, to a lesser extent, glutamyl aminopeptidase ( aminopeptidase A ), as well as other aminopeptidases.
• FPR2, which is now termed the ALX, ALX / FPR, or ALX / FPR2 receptor, is a G protein coupled receptor initially identified as a receptor for the leukocyte chemotactic factor, N-Formylmethionine-leucyl-phenylalanine ( FMLP ), based on its amino acid sequence similarity to the known FMLP receptor, FPR1.
• Some 85 years after this seminal observation, laboratory studies showed that these elements were low molecular weight ( between 150 and 1500 Dalton ( unit ) s ) N-formylated oligopeptides, including the most prominent member of this group, N-Formylmethionine-leucyl-phenylalanine, that are made by a variety of growing gram positive bacteria and gram negative bacteria.
• Studies conducted in the 1970s found that a series of N-formylmethionine-containing oligopeptides, including the most potent and best known member of this series, N-Formylmethionine-leucyl-phenylalanine ( FMLP or fMet-Leu-Phe ), stimulated rabbit and human neutrophils by an apparent receptor-dependent mechanism to migrate in a directional pattern in classical laboratory assays of chemotaxis.
• Studies conducted in the 1970s found that a series of N-Formylmethionine-containing oligopeptides, including the most potent and best known member of this series, N-formyl-methionyl-leucyl-phenylalanine ( FMLP or fMet-Leu-Phe ), stimulated rabbit and human neutrophils by an apparent receptor-dependent mechanism to migrate in a directional pattern in classical laboratory assays of chemotaxis.