EC Number   |
General Information |
Reference |
|---|
    2.4.1.129 | evolution |
proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs |
-, 735922 |
| 2.4.1.129 | evolution |
proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs. Both forms contain a single transmembrane span at the N-terminus followed by the glycosyltransferase domain. In the class A PBPs, the C-terminus contains the transpeptidase domain. Bacterial species typically have multiple forms of these enzymes. Escherichia coli has 3 class A PBPs (PBP1a, PBP1b, and PBP1c) and 2 MGT proteins |
-, 735922 |
| 2.4.1.129 | evolution |
proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs. Both forms contain a single transmembrane span at the N-terminus followed by the glycosyltransferase domain. In the class A PBPs, the C-terminus contains the transpeptidase domain. Bacterial species typically have multiple forms of these enzymes. Staphylococcus aureus has a single class A PBP (PBP2) and 2 MGT proteins (SgtA, SgtB/MGT) |
-, 735922 |
| 2.4.1.129 | evolution |
Streptococcus pneumoniae contains three class A (PBP1a, PBP2a and PBP1b) and two class B (PBP2x and PBP2b) enzymes. PBP1a and PBP2a are not equivalent |
-, 759785 |
| 2.4.1.129 | evolution |
the enzyme belongs to the glycosyltransferases of family 51 (GT51), the glycosyltransferases of family 51 are essential enzymes found in bacteria with peptidoglycan cell wall. They exist in two forms: as a monofunctional domain or linked to the N-terminal end of penicillin-binding (PB) domain in bifunctional PB proteins. Both forms catalyze the polymerization of lipid II (undecaprenyl pyrophosphate-MurNAc(pentapeptide)-GlcNAc) precursor to form linear glycan chains |
735646 |
| 2.4.1.129 | evolution |
the enzyme belongs to the peptidoglycan glycosyltransferase family 51 |
758865 |
| 2.4.1.129 | malfunction |
an Staphylococcus aureus sgtB transposon mutant, with the monofunctional peptidoglycan glycosyltransferase SgtB inactivated, display a 4fold increase in the MIC of oxacillin, suggesting that alterations in the peptidoglycan structure can help bacteria compensate for the lack of lipoteichoic acid (LTA). Muropeptide analysis of peptidoglycans isolated from a wild-type strain and sgtB mutant strain does not reveal any sizable alterations in the peptidoglycan structure. In contrast, the peptidoglycan isolated from an LTA-negative ltaS mutant strain shows a significant reduction in the fraction of highly cross-linked peptidoglycan, which is partially rescued in the sgtB ltaS double mutant suppressor strain. Introduction of SgtB or MazE in the respective suppressor strain results in growth arrest. Increased resistance of the sgtB mutant to oxacillin. The increase in peptidoglycan cross-linking potentially strengthens the cell wall to better sustain the high internal turgor pressure and might be at least partly responsible for the observed growth improvement |
759431 |
| 2.4.1.129 | malfunction |
DELTAmltG mutants in unencapsulated strains accumulate inactivation mutations of class A PBP1a. The reduction of cell width and size of DELTApbp1a mutants compared to those of wild-type parent cells. Mutations in pbp1a suppress the DELTAmltG mutations |
-, 759785 |
| 2.4.1.129 | malfunction |
inhibition of the enzyme blocks peptidoglycan synthesis and leads to bacterial lysis and death |
735646 |
| 2.4.1.129 | malfunction |
mutations that inactivate the pneumococcal YceG-domain protein, Spd_1346 (renamed MltG), remove the requirement for PBP2b. DELTAmltG mutants in unencapsulated strains accumulate inactivation mutations of class A PBP1a, which possesses TP and transglycosylase (TG) activities |
-, 759785 |
