l-tryptophan-histidine synthesis by Pseudomonas serine peptidase, an amino acid ester hydrolase of the peptidase family S9

2021 ◽  
Vol 147 ◽  
pp. 109785
Author(s):  
Keiko Maki ◽  
Md Saddam Hossain ◽  
Takahiro Tanaka ◽  
Yoichi Takeda ◽  
Kazuyoshi Takagi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Ester ◽  
Amino Acid Ester ◽  
Serine Peptidase ◽  
Ester Hydrolase

Substrate Specificity of α-Amino Acid Ester Hydrolase fromXanthomonas citri

1980 ◽  
Vol 44 (5) ◽  
pp. 1075-1081
Author(s):  
Koichi Kato ◽  
Kenji Kawahara ◽  
Takeshi Takahashi ◽  
Atsushi Kakinuma
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Acid Ester ◽  
Amino Acid Ester ◽  
Ester Hydrolase

Stabilization of a tetrameric enzyme (α-amino acid ester hydrolase from Acetobacter turbidans) enables a very improved performance of ampicillin synthesis

2001 ◽  
Vol 11 (4-6) ◽  
pp. 633-638 ◽  
Author(s):  
Roberto Fernandez-Lafuente ◽  
Odette Hernández-Jústiz ◽  
Cesar Mateo ◽  
Marco Terreni ◽  
Jorge Alonso ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Ester ◽  
Amino Acid Ester ◽  
Ester Hydrolase ◽  
Improved Performance

scholarly journals Molecular Basis of Prodrug Activation by Human Valacyclovirase, an α-Amino Acid Ester Hydrolase

2008 ◽  
Vol 283 (14) ◽  
pp. 9318-9327 ◽  
Author(s):  
Longsheng Lai ◽  
Zhaohui Xu ◽  
Jiahai Zhou ◽  
Kyung-Dall Lee ◽  
Gordon L. Amidon
Keyword(s):  
Amino Acid ◽  
Acid Ester ◽  
Molecular Basis ◽  
Amino Acid Ester ◽  
Prodrug Activation ◽  
Ester Hydrolase

scholarly journals 3D Structure Modeling of Alpha-Amino Acid Ester Hydrolase from Xanthomonas rubrilineans

Acta Naturae ◽  
2013 ◽  
Vol 5 (4) ◽  
pp. 62-70 ◽  
Author(s):  
S. A. Zarubina ◽  
I. V. Uporov ◽  
E. A. Fedorchuk ◽  
V. V. Fedorchuk ◽  
A. V. Sklyarenko ◽  
...  
Keyword(s):  
Amino Acid ◽  
Active Site ◽  
Acid Ester ◽  
Rational Design ◽  
3D Structure ◽  
Catalytic Triad ◽  
Amino Acid Ester ◽  
Dimensional Structure ◽  
Ester Hydrolase ◽  
Alpha Amino Acid

Alpha-amino acid ester hydrolase (EC 3.1.1.43, AEH) is a promising biocatalyst for the production of semi-synthetic -lactam antibiotics, penicillins and cephalosporins. The AEH gene from Xanthomonas rubrilineans (XrAEH) was recently cloned in this laboratory. The three-dimensional structure of XrAEH was simulated using the homology modeling method for rational design experiments. The analysis of the active site was performed, and its structure was specified. The key amino acid residues in the active site - the catalytic triad (Ser175, His341 and Asp308), oxyanion hole (Tyr83 and Tyr176), and carboxylate cluster (carboxylate groups of Asp209, Glu310 and Asp311) - were identified. It was shown that the optimal configuration of residues in the active site occurs with a negative net charge -1 in the carboxylate cluster. Docking of different substrates in the AEH active site was carried out, which allowed us to obtain structures of XrAEH complexes with the ampicillin, amoxicillin, cephalexin, D-phenylglycine, and 4-hydroxy-D-phenylglycine methyl ester. Modeling of XrAEH enzyme complexes with various substrates was used to show the structures for whose synthesis this enzyme will show the highest efficiency.

Sign in / Sign up

Export Citation Format

Share Document