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Information on EC 2.3.2.16 - lipid II:glycine glycyltransferase and Organism(s) Weissella viridescens and UniProt Accession Q9EY50

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.16 lipid II:glycine glycyltransferase
IUBMB Comments
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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This record set is specific for:
Weissella viridescens
UNIPROT: Q9EY50
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The taxonomic range for the selected organisms is: Weissella viridescens
The enzyme appears in selected viruses and cellular organisms
Synonyms
lipid ii:glycine glycyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -
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).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
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
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FEMX_WEIVI
336
0
38284
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39360
1 * 39360, calculated
40000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 39360, calculated
PROTEIN VARIANTS
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hegde, S.S.; Shrader, T.E.
FemABX family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets
J. Biol. Chem.
276
6998-7003
2001
Weissella viridescens (Q9EY50)
Manually annotated by BRENDA team