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EC Tree
The taxonomic range for the selected organisms is: Weissella viridescens The enzyme appears in selected viruses and cellular organisms
Synonyms
femxwv, alanyltransferase,
more
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alanyl-transfer ribonucleate-uridine diphosphoacetylmuramoylpentapeptide transferase
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alanyltransferase, uridine diphosphoacetylmuramoylpentapeptide lysine N6-
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UDP-N-acetylmuramoylpentapeptide lysine N6-alanyltransferase
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uridine diphosphoacetylmuramoylpentapeptide lysine N6-alanyltransferase
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L-alanyl-tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
L-alanyl-tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
transfer of L-Ala to epsilon-amino group of L-lysine of UDP-UDP-acetylmuramoylpentapeptide in an ordered sequential mechanism
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L-alanyl-tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
catalysis via a ternary complex
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aminoacyl group transfer
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aminoacyl group transfer
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L-alanyl-tRNAAla:UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine N6-alanyltransferase
Also acts on L-seryl-tRNASer.
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L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
glycyl-tRNAGly + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAGly + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(glycyl)-L-lysyl-D-alanyl-D-alanine
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poor substrate
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ir
L-alanyl-tRNA(Ala) + UDP-N-acetylmuramoyl-pentapeptide containing L-lysine
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r
L-alanyl-tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
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?
L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
L-alanyl-tRNASer + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNASer + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
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?
L-cysteinyl-tRNACys + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNACys + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-cysteinyl)-L-lysyl-D-alanyl-D-alanine
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ir
L-seryl-tRNASer + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNASer + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-seryl)-L-lysyl-D-alanyl-D-alanine
additional information
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L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
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L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
production of precursors for branched chain peptidoglycans, involved in the synthesis of bacterial cell walls
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L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
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L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
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L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
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poor or no acceptors are acetylmuramoyl- and phosphoacetylmuramoyl-L-Ala-L-Glu-L-Lys-D-Ala-D-Ala or UDP-acetylmuramoyl-L-Ala-L-Glu-L-Lys
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ir
L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
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no strict specificity for tRNA-carrier: tRNACys can replace tRNAAla, tRNA from other species can substitute to some extent for the homologous tRNA from Lactobacillus viridescens, higher specificity for transferred amino acid: amino acids with larger substituents are no substrates, UDP-acetylmuramyl-L-Ala-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala can replace UDP-acetylmuramyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala at 15% the transfer rate
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ir
L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
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involved in peptidoglucan metabolism, responsible for interpeptide bridges
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ir
L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
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production of precursors for branched chain peptidoglycans
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L-seryl-tRNASer + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNASer + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-seryl)-L-lysyl-D-alanyl-D-alanine
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L-seryl-tRNASer + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNASer + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-seryl)-L-lysyl-D-alanyl-D-alanine
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about half as effective as L-alanyl-tRNA
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ir
additional information
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also utilizes UDP-N-acetylmuramoylpentapeptide containing L-ornithine as substrate
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additional information
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enzyme highly specific for UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, only traces of activity with UDP-N-acetylmuramoyl-tripeptide or UDP-N-acetylmuramoyl-tetrapeptide or derivatives of UDP-N-acetylmuramoyl-pentapeptide
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additional information
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catalyses the transfer of L-Ala from Ala-tRNAAla to the peptidoglycan precursor UDP-MurNAc-pentapeptide in order to introduce the first residue of an L-Ala-L-Ser-L-Ala side chain
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additional information
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FemXWv transferase adds the first residue of the L-Ala-L-Ser-L-Ala side chain onto the nucleotide precursor UDP-MurNAc-pentadepsipeptide
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
production of precursors for branched chain peptidoglycans, involved in the synthesis of bacterial cell walls
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L-alanyl-tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
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L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
additional information
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L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
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involved in peptidoglucan metabolism, responsible for interpeptide bridges
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ir
L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
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production of precursors for branched chain peptidoglycans
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additional information
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catalyses the transfer of L-Ala from Ala-tRNAAla to the peptidoglycan precursor UDP-MurNAc-pentapeptide in order to introduce the first residue of an L-Ala-L-Ser-L-Ala side chain
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additional information
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FemXWv transferase adds the first residue of the L-Ala-L-Ser-L-Ala side chain onto the nucleotide precursor UDP-MurNAc-pentadepsipeptide
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additional information
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no activation by EDTA or metal ions
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aminoacyl-tRNA analogue C
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aminoacyl-tRNA analogue C'
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Ser-tRNA
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versus UDP-acetylmuramoylpentapeptide
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
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product inhibition
additional information
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no inhibition by EDTA or metal ions
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0.0017
L-alanyl-tRNA
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pH 7.5, 30°C
0.015 - 0.061
L-alanyl-tRNA(Ala)
0.0002 - 0.165
UDP-acetylmuramoylpentapeptide
0.079
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
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pH 7.5, 30°C
0.015
L-alanyl-tRNA(Ala)
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Ala-tRNAAla from E. coli, recombinant wild-type
0.054
L-alanyl-tRNA(Ala)
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Ala-tRNAAla from E. coli, recombinant mutant E320Q
0.061
L-alanyl-tRNA(Ala)
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Ala-tRNAAla from E. coli, recombinant mutant D109N
0.0002
UDP-acetylmuramoylpentapeptide
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0.042
UDP-acetylmuramoylpentapeptide
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recombinant wild-type
0.067
UDP-acetylmuramoylpentapeptide
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recombinant mutant E320Q
0.165
UDP-acetylmuramoylpentapeptide
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recombinant mutant D109N
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26.7
L-alanyl-tRNA
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pH 7.5, 30°C
0.183 - 11
L-alanyl-tRNAAla
0.183
L-alanyl-tRNAAla
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recombinant mutant D109N
0.917
L-alanyl-tRNAAla
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recombinant mutant E320Q
11
L-alanyl-tRNAAla
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recombinant wild-type
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0.248
Ser-tRNA
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versus UDP-acetylmuramoylpentapeptide
0.048
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
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product inhibition
additional information
additional information
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0.0024
aminoacyl-tRNA analogue C
Weissella viridescens
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0.0041
aminoacyl-tRNA analogue C'
Weissella viridescens
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0.0014
oxa-helixAla
Weissella viridescens
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0.067
oxa-helixGly
Weissella viridescens
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0.015
oxa-helixSer
Weissella viridescens
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additional information
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relative activity of FemXWv for the transfer of L-Ala from helixAla to UDP-MurNAc-pentapeptide 100%
additional information
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relative activity of FemXWv for the transfer of L-Ala from helixGly to UDP-MurNAc-pentapeptide 2.9%
additional information
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relative activity of FemXWv for the transfer of L-Ala from helixSer to UDP-MurNAc-pentapeptide 31%
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6.8 - 7.2
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L-alanyl-tRNA
additional information
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broad maximum
7.5
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inhibition assay
7.5
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radioactive coupled FemX assay
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5.2 - 8.6
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L-alanyl-tRNA, about 80% of maximal activity at pH 5.2 and pH 8.6
6.1 - 8.6
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L-seryl-tRNA, about half-maximal activity at pH 6.1 and about 90% of maximal activity at pH 8.6
additional information
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pK values of 5.5 and 9.3
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30
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assay at
30
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radioactive coupled FemX assay
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SwissProt
brenda
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brenda
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FEMX_WEIVI
336
0
38284
Swiss-Prot
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38000
crystal structure analysis
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monomer
1 * 38000, crystal structure analysis
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crystallized by vapor diffusion method
crystallized in the presence of UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine by vapor diffusion method
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D109N
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site-directed mutagenesis, loss of 99% activity compared to the wild-type
E205Q
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site-directed mutagenesis, unaltered activity compared to the wild-type
E215Q
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site-directed mutagenesis, loss of 15% activity compared to the wild-type
E316Q
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site-directed mutagenesis, loss of 60% activity compared to the wild-type
E320Q
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site-directed mutagenesis, loss of 96% activity compared to the wild-type
F70L
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35% loss of activity
K36M
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activity complete abolished
K36R
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160-fold reduction of activity, 5.4-fold increased Km for UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
R211K
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17000-fold reduction of activity, no effect on Km for Ala-tRNA, Km for UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine higher than the highest sample concentration
Y103F
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no effect on activity
Y215F
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25-fold decrease of activity, increased Km for UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
Y215L
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insoluble protein
Y256F
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2.6-fold reduction of activity
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recombinant His-tagged wild-type and mutants from E. coli
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recombinant proteins using His-tag
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expressed as intein-tagged fusion protein
expression of wild-type and mutants as His-tagged proteins in Escherichia coli, in vitro transcription of tRNAs
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wild type and mutant enzymes expressed as His-tag fusion proteins in Escherichia coli TOP10
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medicine
potential target for antimicrobial drugs
medicine
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Fem transferases are considered as attractive targets for the development of novel antibiotics active against multi-resistant bacteria
medicine
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Fem transferases are considered attractive targets for the development of novel antibiotics active against multiply resistant bacteria
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Plapp, R.; Strominger, J.L.
Biosynthesis of the peptidoglycan of bacterial cell walls
J. Biol. Chem.
245
3673-3682
1970
Weissella viridescens
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brenda
Hegde, S.S.; Blanchard, J.S.
Kinetic and mechanistic characterization of recombinant Lactobacillus viridescens FemX (UDP-N-acetylmuramoyl pentapeptide-lysine N6-alanyltransferase)
J. Biol. Chem.
278
22861-22867
2003
Weissella viridescens
brenda
Maillard, A.P.; Biarrotte-Sorin, S.; Villet, R.; Mesnage, S.; Bouhss, A.; Sougakoff, W.; Mayer, C.; Arthur, M.
Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens
J. Bacteriol.
187
3833-3838
2005
Weissella viridescens, Weissella viridescens CIP 102810 / ATCC 12706
brenda
Biarrotte-Sorin, S.; Maillard, A.P.; Delettre, J.; Sougakoff, W.; Arthur, M.; Mayer, C.
Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: Insights into FemABX family substrates recognition
Structure
12
257-267
2004
Weissella viridescens (Q9EY50)
brenda
Chemama, M.; Fonvielle, M.; Arthur, M.; Valery, J.M.; Etheve-Quelquejeu, M.
Synthesis of stable aminoacyl-tRNA analogues containing triazole as a bioisoster of esters
Chemistry
15
1929-1938
2009
Weissella viridescens
brenda
Fonvielle, M.; Chemama, M.; Villet, R.; Lecerf, M.; Bouhss, A.; Valery, J.M.; Etheve-Quelquejeu, M.; Arthur, M.
Aminoacyl-tRNA recognition by the FemXWv transferase for bacterial cell wall synthesis
Nucleic Acids Res.
37
1589-1601
2009
Weissella viridescens
brenda
Mellal, D.; Fonvielle, M.; Santarem, M.; Chemama, M.; Schneider, Y.; Iannazzo, L.; Braud, E.; Arthur, M.; Etheve-Quelquejeu, M.
Synthesis and biological evaluation of non-isomerizable analogues of Ala-tRNAAla
Org. Biomol. Chem.
11
6161-6169
2013
Weissella viridescens
brenda