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TitleMutagenesis and structure-based analysis of the role of Tryptophan525 of gamma-glutamyltranspeptidase from Pseudomonas nitroreducens.
Journal, issue, pagesBiochem. Biophys. Res. Commun., Vol. 534, Page 286-291, Year 2021
Publish dateOct 13, 2020 (structure data deposition date)
AuthorsSano, C. / Itoh, T. / Phumsombat, P. / Hayashi, J. / Wakayama, M. / Hibi, T.
External linksBiochem. Biophys. Res. Commun. / PubMed:33288198
MethodsX-ray diffraction
Resolution1.5 - 1.9 Å
Structure data

PDB-7d9e:
Gamma-glutamyltranspeptidase from Pseudomonas nitroreducens complexed with L-DON
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-7d9w:
Gamma-glutamyltranspeptidase from Pseudomonas nitroreducens complexed with L-DON
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-7d9x:
Highly active mutant W525D of Gamma-glutamyltranspeptidase from Pseudomonas nitroreducens
Method: X-RAY DIFFRACTION / Resolution: 1.74 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-DON:
6-DIAZENYL-5-OXO-L-NORLEUCINE

ChemComp-HOH:
WATER

ChemComp-GLY:
GLYCINE

ChemComp-GBL:
GAMMA-BUTYROLACTONE

Source
  • pseudomonas nitroreducens (bacteria)
KeywordsTRANSFERASE / theanine synthesis / transpeptidation / enzyme / protein engineering / substrate specificity / reaction specificity

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