Information on EC 2.3.2.16 - lipid II:glycine glycyltransferase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
2.3.2.16
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RECOMMENDED NAME
GeneOntology No.
lipid II:glycine glycyltransferase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
peptidoglycan cross-bridge biosynthesis I (S. aureus)
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peptidoglycan cross-bridge biosynthesis III (Enterococcus faecalis)
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peptidoglycan biosynthesis
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Peptidoglycan biosynthesis
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Metabolic pathways
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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).
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
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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
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
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
addition of serine and alanine is preferred over glycine
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additional information
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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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39360
1 * 39360, calculated
40000
gel filtration
48500
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1 * 48500, calculated
50000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression as His-tagged protein in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F196L
26% of wild-type activity
F196Y
87% of wild-type activity
F305L
16% of wild-type activity
F305Y
98% of wild-type activity
G319S
13% of wild-type activity
G319V
5% of wild-type activity
K306A
8% of wild-type activity
K306C
38% of wild-type activity
K306N
9% of wild-type activity
K306R
25% of wild-type activity
Q144E
11% of wild-type activity
Q144T
79% of wild-type activity
Y216F
41% of wild-type activity
Y73F
40% of wild-type activity
Y73L
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
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Show AA Sequence (304 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.2.16)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)