Detail of GM0110


Summary

The genetically modified enzybiotic, named Q199A , constructed by Mutagenesis strategy, decrease the binding activity.
With  Q199A
  Sequence Length:  78 AA.
  Mass:  8639.7 Da.
  Isoelectric Point:  6.67
  Function:  decrease the binding activity

Construction

GM0110, constructed by Mutagenesis strategy.
    No schema construted on GM0110
Details:
GM0110[1-78]: derive from protein Q8LTE6 sequence 156-233

Q8LTE6, 233 AA., the N-acetylmuramoyl-L-alanine amidase from Bacillus phage Gamma

Source: Bacillus phage Gamma

Domains and repeats

3 - 156:  IPR002502, the N-acetylmuramoyl-L-alanine amidase domain
189 - 232:  IPR021976, the N-acetylmuramoyl-l-alanine amidase

GO term prediction

Biological Process:  0009253, the peptidoglycan catabolic process
Molecular Function:  0008745, the N-acetylmuramoyl-L-alanine amidase activity


Linking to UniprotKB
Linging to InterPro

Annotation

1-78

1-78
: CBD, Cell wall-targeting domain, derived from B. anthracis ??Phage lysin PlyG (PlyGB (PlyG binding domain; residues 156?C233));
199
: MUT, mutation with Q199A ;
Domain and repeats:
1-78
: IPR002502,N-acetylmuramoyl-L-alanine amidase domain;
1-78
: IPR021976,N-acetylmuramoyl-l-alanine amidase;
GO term prediction:
0008745, the N-acetylmuramoyl-L-alanine amidase activity
0009253, the peptidoglycan catabolic process
NGNVATTSPTKQNIIQSGAFSPYETPDVMGALTSLKMTADFILASDGLTYFISKPTSDAQLKAMKEYLDRKGWWYEVK
  BlastP to GMEnzy

Production

  1.  Expressed by pGEX-6P-2 in E. coli (pG-KJE8/BL21),  Purified by Glutathione-Sepharose 4B columns

Activity

    No activity data found on GM0110

Reference

  1. Kikkawa, H.Fujinami, Y.Suzuki, S.Yasuda, J.. (2007) Identification of the amino acid residues critical for specific binding of the bacteriolytic enzyme of gamma-phage, PlyG, to Bacillus anthracis. Biochemical and biophysical research communication. 03:531-535. [doi:10.1016/j.bbrc.2007.09.002] [PMID:17888883]

Comments

    No comments found on GM0110


CAPTCHA Image   Reload Image
Enter Code*: