Information on EC 2.3.2.16 - lipid II:glycine glycyltransferase

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The expected taxonomic range for this enzyme is: Bacilli

EC NUMBER
COMMENTARY
2.3.2.16
-
RECOMMENDED NAME
GeneOntology No.
lipid II:glycine glycyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + glycyl-tRNAGly = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + tRNAGly
show the reaction diagram
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-
-
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PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Peptidoglycan biosynthesis
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peptidoglycan cross-bridge biosynthesis I (S. aureus)
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peptidoglycan cross-bridge biosynthesis III (Enterococcus faecalis)
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SYSTEMATIC NAME
IUBMB Comments
alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine N6-glycyltransferase
The enzyme from Staphylococcus aureus catalyses the transfer of glycine from a charged tRNA to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphosphoundecaprenyl-GlcNAc (lipid II), attaching it to the N6 of the L-Lys at position 3 of the pentapeptide. This is the first step in the synthesis of the pentaglycine interpeptide bridge that is used in S. aureus for the crosslinking of different glycan strands to each other. Four additional Gly residues are subsequently attached by EC 2.3.2.17 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase) and EC 2.3.2.18 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
surface protein is linked to tri- and monoglycyl cross-bridges of peptidoglycan isolated from femB and femA mutant staphylococci, respectively. No surface protein is found linked directly to the epsilon-amino group of lysyl within the cell wall of a femAX strain
physiological function
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FemX catalyzes the first step in the synthesis of the pentaglycine interpeptide bridge crosslinking different glycan strands in Staphylococcus aureus. FemX uses MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala-diphosphoundecaprenyl-M-acetylglucosamine, i.e. lipid II, exclusively as acceptor for the first glycine residue. Addition of glycine residues 2, 3 and glycine residues 4, 5 is catalyzed by enzymes FemA and FemB, respectively. None of the FemABX enzymes requires the presence of one or two of the other Fem proteins for activity, rather, bridge formation is delayed in an in vitro system when all 3 enzymes are present
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycyl-tRNA(E.coli) + UDP-MurNAc-Ala-D-Glu-Lys-D-Ala-D-Ala
tRNA(E.coli) + UDP-MurNAc-Ala-D-Glu-(N6-Gly)Lys-D-Ala-D-Ala
show the reaction diagram
Q9EY50
addition of serine and alanine is preferred over glycine
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-
?
glycyl-tRNAGly + N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine
tRNAGly + N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine
show the reaction diagram
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i.e. lipid II. Enzyme uses lipid II exclusively as acceptor
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-
?
L-alanyl-tRNA(E.coli) + UDP-MurNAc-Ala-D-Glu-Lys-D-Ala-D-Ala
tRNA(E.coli) + UDP-MurNAc-Ala-D-Glu-(N6-L-Ala)Lys-D-Ala-D-Ala
show the reaction diagram
Q9EY50
addition of serine and alanine is preferred over glycine
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-
?
L-seryl-tRNA(E.coli) + UDP-MurNAc-Ala-D-Glu-Lys-D-Ala-D-Ala
tRNA(E.coli) + UDP-MurNAc-Ala-D-Glu-(N6-L-Ser)Lys-D-Ala-D-Ala
show the reaction diagram
Q9EY50
addition of serine and alanine is preferred over glycine
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-
?
additional information
?
-
Q9EY50
Assays with mixtures of alanyl-, seryl-, and glycyl-tRNAs result in mixtures of the expected UDP-MurNAc hexapeptides, but no larger species. FemX adds only the first residue of the interchain peptide
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MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
Q9EY50
gel filtration
50000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
Q9EY50
1 * 39360, calculated
monomer
-
1 * 48500, calculated
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression as His-tagged protein in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
F196L
Q9EY50
26% of wild-type activity
F196Y
Q9EY50
87% of wild-type activity
F305L
Q9EY50
16% of wild-type activity
F305Y
Q9EY50
98% of wild-type activity
G292V
Q9EY50
inactive
G319S
Q9EY50
13% of wild-type activity
G319V
Q9EY50
5% of wild-type activity
K306A
Q9EY50
8% of wild-type activity
K306C
Q9EY50
38% of wild-type activity
K306N
Q9EY50
9% of wild-type activity
K306R
Q9EY50
25% of wild-type activity
P110F
Q9EY50
inactive
P110H
Q9EY50
inactive
Q144E
Q9EY50
11% of wild-type activity
Q144T
Q9EY50
79% of wild-type activity
Q29E
Q9EY50
inactive
Q29T
Q9EY50
inactive
Y216F
Q9EY50
41% of wild-type activity
Y216L
Q9EY50
inactive
Y73F
Q9EY50
40% of wild-type activity
Y73L
Q9EY50
40% of wild-type activity
additional information
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in strains carrying mutations of FemA, femAB, or the femAX genes, the sorting reaction of surface proteins is significantly slowed. Strains carrying mutations in the fem genes display a decreased rate of surface protein precursor cleavage as compared with the wild-type strains, suggesting that the altered cross-bridges slow the anchoring of surface proteins