Transpeptidation

	Transpeptidation Transpeptidase may refer to: * DD-transpeptidase, a bacterial enzyme that cross-links the peptidoglycan chains to form rigid cell walls * Gamma-glutamyl transpeptidase, a liver enzyme * D-glutamyl transpeptidase * A protein-sorting transpeptidase (e.g. sortase Sortase refers to a group of prokaryote, prokaryotic enzymes that modify surface proteins by recognizing and cleaving a carboxyl-terminal protein targeting, sorting signal. For most substrates of sortase enzymes, the recognition signal consists o ... ), that cleaves a C-terminal sorting signal from its target protein(s) and then covalently attaches the remainder to the cell surface. {{disambiguation ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu]
picture info	DD-transpeptidase DD-transpeptidase (, ''DD-peptidase'', ''DD-transpeptidase'', ''DD-carboxypeptidase'', ''D-alanyl-D-alanine carboxypeptidase'', ''D-alanyl-D-alanine-cleaving-peptidase'', ''D-alanine carboxypeptidase'', ''D-alanyl carboxypeptidase'', and ''serine-type D-Ala-D-Ala carboxypeptidase''.) is a bacterial enzyme that catalyzes the transfer of the R-L-aca-D-alanyl moiety of R-L-aca-D-alanyl-D-alanine carbonyl donors to the γ-OH of their active-site serine and from this to a final acceptor. It is involved in bacterial cell wall biosynthesis, namely, the transpeptidation that crosslinks the peptide side chains of peptidoglycan strands. The antibiotic penicillin irreversibly binds to and inhibits the activity of the transpeptidase enzyme by forming a highly stable penicilloyl-enzyme intermediate. Because of the interaction between penicillin and transpeptidase, this enzyme is also known as penicillin-binding protein (PBP). Mechanism DD-transpeptidase is mechanistically similar to the prote ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu]
	Gamma-glutamyl Transpeptidase Gamma-glutamyltransferase (also γ-glutamyltransferase, GGT, gamma-GT, gamma-glutamyl transpeptidase; ) is a transferase (a type of enzyme) that catalyzes the transfer of gamma- glutamyl functional groups from molecules such as glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione as well as drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a pro-oxidant role, with regulatory effects at various levels in cellular signal transduction and cellular pathophysiology. This transferase is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. Nomenclature The name γ-glutamyltransferase is preferred by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. The Expert Panel on Enzymes of the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu]
	D-glutamyl Transpeptidase In enzymology, a D-glutamyltransferase () is an enzyme that catalyzes the chemical reaction :L(or D)-glutamine + D-glutamyl-peptide \rightleftharpoons NH3 + 5-glutamyl-D-glutamyl-peptide The 3 substrates of this enzyme are L-glutamine, D-glutamine, and D-glutamyl-peptide, whereas its two products are NH3 and 5-glutamyl-D-glutamyl-peptide. This enzyme belongs to the family of transferases, specifically the aminoacyltransferase Aminoacyltransferases () are acyltransferase enzymes which act upon an amino group. For instance, aminoacyl tRNA synthetases attach an aminoacid through esterification to the corresponding tRNA. The activation of amino acids it aminoacyl-tRNA synt ...s. The systematic name of this enzyme class is glutamine:D-glutamyl-peptide 5-glutamyltransferase. Other names in common use include D-glutamyl transpeptidase, and D-gamma-glutamyl transpeptidase. This enzyme participates in d-glutamine and d-glutamate metabolism. References * EC 2.3.2 En ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu]
	Protein-sorting Transpeptidase A protein-sorting transpeptidase is an enzyme, such as the sortase SrtA of Staphylococcus aureus, that cleaves one or more target proteins produced by the same cell, as part of a specialized pathway of protein targeting. The typical prokaryotic protein-sorting transpeptidase is characterized as a protease, but does not simply hydrolyze a peptide bond. Instead, the larger, N-terminal portion of the cleaved polypeptide is transferred onto another molecule, such as a precursor of the peptidoglycan cell wall in Gram-positive bacteria. The term sortase is properly reserved for the set of cysteine protease enzymes sortase A, sortase B, and members of additional classes, all of which share homology. However, a growing number of additional protein sorting systems has been described in prokaryotes, involving sorting enzymes that lack any homology to sortase and that appear to have arisen separately by convergent evolution Convergent evolution is the independent evolution of similar ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu]