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2.4.1.129: peptidoglycan glycosyltransferase

This is an abbreviated version!
For detailed information about peptidoglycan glycosyltransferase, go to the full flat file.

Word Map on EC 2.4.1.129

Reaction

[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol
+
GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
=
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol
+
undecaprenyl diphosphate

Synonyms

bacterial cell wall glycosyltransferase, bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase, bifunctional penicillin-binding protein, class A penicillin-binding protein, class B penicillin-binding protein, DD-transpeptidase, ftsI, glycosyltransferase, peptidoglycan, glycosyltransferase/acyltransferase penicillin-binding protein 4, GTase, MGT, monofunctional glycosyltransferase, mrcB, MtgA, murein synthase, PBP, PBP 1a, PBP 2b, PBP 2x, PBP 3, PBP-1A, PBP-1B, PBP-1C, PBP-2, PBP1, PBP1a, PBP1b, PBP1c, PBP2, PBP2A, PBP2b, PBP2c, PBP2d, PBP3, PBP4, PBP7, PBP8, PBPA, PenA, penicillin binding protein, penicillin binding protein 1b, penicillin-binding protein, penicillin-binding protein 1a, penicillin-binding protein 1B, penicillin-binding protein 2, penicillin-binding protein 3, peptidoglycan glycosyltransferase, peptidoglycan transglycosylase, PG-II, PGT, SgtB, SpoIID

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.129 peptidoglycan glycosyltransferase

Cloned

Cloned on EC 2.4.1.129 - peptidoglycan glycosyltransferase

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a soluble form of Staphylococcus aureus MGT devoid of its membrane anchor, called SauH6-MGT (D68-R268), is expressed in the cytoplasm of Escherichia coli C41 (DE3) strain
-
activity of PBP1a or PBP1b can be measured in membranes by cloning the PBP into an Escherichia coli ponB::Spcr strain
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construction of expression plasmids allowing the production of native PBP1B or PBP1B variants with an inactive transpeptidase or transglycosylase domain or both. Overproduction of the inactive PBP1B variants, but not of the active proteins, causes lysis of wild-type cells. Cells became tolerant to lysis by inactive PBP1B at a pH of 5.0
-
enzyme overexpression in Escherichia coli imp mutant strain
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Escherichia coli structural gene mrcB, recloned from plasmid pLC19-19 to high copy number plasmid pBr322, yielding plasmid pTM13
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(lambdaDE3)-RIL cells
expressed in Escherichia coli Rosetta lambdaDE3 cells
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expressed in Escherichia coli Top10 cells
-
expression in Escherichia coli
gene mrcB, recombinant expression of His6-tagged PBP1b (residues 58-604) in Escherichia coli
gene mtgA, recombinant expression of wild-type and mutant enzymes
-
gene pbp2A, recombinant expression of FLAG-tagged wild-type and mutant enzymes in Streptococcus pneumoniae strain D39 DELTAcps/DELTAmltG obtained from strain IU7260
gene penA or pbp2B, genotyping, recombinant expression in Streptococcus pneumoniae strain IU1824, i.e. D39 DELTAcps
overexpression and characterization of the glycosyltransferase module of PBP1b. The isolated module can be overexpressed at significantly higher levels than the full-length protein
-
overexpression of His-tagged enzyme in Escherichia coli strain BL21 pDML924
PBP4 was not functional in Escherichia coli
-
recombinant expression of His-tagged wild-type MtgA and point mutants as well as MtgA (D68-R269) mutant lacking the transmembrane segment in Escherichia coli
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wild type and mutant enzymes are expressed in Escherichia coli BL21(DE3) cells
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