Information on EC 2.3.2.17 - N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase

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The expected taxonomic range for this enzyme is: Staphylococcus

EC NUMBER
COMMENTARY hide
2.3.2.17
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RECOMMENDED NAME
GeneOntology No.
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 glycyl-tRNAGly = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 tRNAGly
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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peptidoglycan biosynthesis
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Peptidoglycan biosynthesis
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peptidoglycan cross-bridge biosynthesis I (S. aureus)
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SYSTEMATIC NAME
IUBMB Comments
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
This enzyme catalyses the successive transfer of two Gly moieties from charged tRNAs to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc, attaching them to a Gly residue previously attached by EC 2.3.2.16 (lipid II:glycine glycyltransferase) to the N6 of the L-Lys at position 3 of the pentapeptide. This is the second step in the synthesis of the pentaglycine interpeptide bridge that is used by Staphylococcus aureus for the crosslinking of different glycan strands to each other. The next step is catalysed by EC 2.3.2.18 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase). This enzyme is essential for methicillin resistance [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
decreased expression of the femA gene leads to reduced methicillin resistance
metabolism
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all investigated strains, either methicillin-resistant or susceptible, express FemA during the exponential growth phase in varying amounts. In the stationary phase, the FemA content is diminished. Strains in which FemA is inactivated by insertion of Tn551 into the control region of the FemAB operon still express about 10% of the protein compared to their parent strains. Tn551 insertion in the middle of the femB gene does not affect the FemA expression
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 glycyl-tRNA
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-triglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 tRNA
show the reaction diagram
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i.e. lipid II-Gly. Enzyme is specific for lipid II-Gly as acceptor
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?
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
89300
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 49400, SDS-PAGE
additional information
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proteins FemA and FemB form homo- and heterodimers in vitro
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.1 A resolution. The FemA structure reveals a unique organization of several known protein folds involved in peptide and tRNA binding. The surface of the protein reveals an L-shaped channel suitable for a peptidoglycan substrate
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression as His-tagged protein in Escherichia coli
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expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
femA gene expression is not upregulated in oxacillin susceptible methicillin-resistant OS-MRSA strains compared to low- and high-level methicillin-resistant MRSA control strains
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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definition of a consensus sequence of the femA gene and analysis of interspecies variations for staphylococci species-specific identification
medicine
Show AA Sequence (106 entries)
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