Related Research Articles
DD-transpeptidase is a bacterial enzyme that catalyzes the transfer of the R-L-αα-D-alanyl moiety of R-L-αα-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.
Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics bind to PBPs, which are essential for bacterial cell wall synthesis. PBPs are members of a subgroup of enzymes called transpeptidases. Specifically, PBPs are DD-transpeptidases.
A carboxypeptidase is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases, which cleave peptide bonds at the N-terminus of proteins. Humans, animals, bacteria and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation. At least two mechanisms have been discussed.
In enzymology, an alanine—tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a D-alanine—D-alanine ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase (EC 2.3.2.10) is an enzyme that catalyzes the chemical reaction
Peptidoglycan binding domains have a general peptidoglycan binding function and a common core structure consisting of a closed, three-helical bundle with a left-handed twist. It is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. Examples are:
In molecular biology, VanY are protein domains found in enzymes named metallopeptidases. They are vital to bacterial cell wall synthesis and antibiotic resistance.
Lipid II:glycine glycyltransferase (EC 2.3.2.16, N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:N6-glycine transferase, femX (gene)) is an enzyme with systematic name alanyl-D-alanine-diphospho-ditrans, octacis-undecaprenyl-N-acetylglucosamine:glycine N6-glycyltransferase. This enzyme catalyses the following chemical reaction
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase (EC 2.3.2.17, femA (gene)) is an enzyme with systematic name N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase. This enzyme catalyses the following chemical reaction
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase (EC 2.3.2.18, femB (gene)) is an enzyme with systematic name N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase. This enzyme catalyses the following chemical reaction
D-Ala-D-Ala dipeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Lysine carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction:
Alanine carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Muramoylpentapeptide carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction.
Muramoyltetrapeptide carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Gamma-D-glutamyl-meso-diaminopimelate peptidase is an enzyme. This enzyme catalyses the following chemical reaction
Sortases are membrane anchored enzyme that sort these surface proteins onto the bacterial cell surface and anchor them to the peptidoglycan. There are different types of sortases and each catalyse the anchoring of different proteins to cell walls.
D-Alanine—D-serine ligase is an enzyme with systematic name D-alanine:D-serine ligase (ADP-forming). This enzyme catalyses the following chemical reaction
References
- ↑ Dideberg O, Charlier P, Dive G, Joris B, Frère JM, Ghuysen JM (September 1982). "Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution". Nature. 299 (5882): 469–70. doi:10.1038/299469a0. PMID 7121588.
- ↑ Joris B, Van Beeumen J, Casagrande F, Gerday C, Frère JM, Ghuysen JM (January 1983). "The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of streptomyces albus G". European Journal of Biochemistry. 130 (1): 53–69. doi: 10.1111/j.1432-1033.1983.tb07116.x . PMID 6825689.
- ↑ Ghuysen JM, Frère JM, Leyh-Bouille M, Nguyen-Distèche M, Coyette J, Dusart J, Joris B, Duez C, Dideberg O, Charlier P (1984). "Bacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics". Scandinavian Journal of Infectious Diseases. Supplementum. 42: 17–37. PMID 6597561.
