Evaluation of substrate promiscuity of an L-carbamoyl amino acid amidohydrolase fromGeobacillus stearothermophilusCECT43

2010 ◽  
pp. NA-NA
Author(s):  
Joaquín Pozo-Dengra ◽  
Ana Isabel Martínez-Gómez ◽  
Sergio Martínez-Rodríguez ◽  
Josefa María Clemente-Jiménez ◽  
Felipe Rodríguez-Vico ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Promiscuity ◽  
Acid Amidohydrolase

Structure–Stability–Activity Relationship in Covalently Cross-linked N-Carbamoyl d-Amino acid Amidohydrolase and N-Acylamino acid Racemase

2006 ◽  
Vol 359 (3) ◽  
pp. 741-753 ◽  
Author(s):  
Wei-Chun Chiu ◽  
Ji-Yu You ◽  
Jai-Shin Liu ◽  
Shih-Kuang Hsu ◽  
Wen-Hwei Hsu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Activity Relationship ◽  
Structure Stability ◽  
Acid Amidohydrolase

scholarly journals Heterologous Expression and Characterization of A Novel Ochratoxin A Degrading Enzyme, N-acyl-L-amino Acid Amidohydrolase, from Alcaligenes faecalis

Toxins ◽  
2019 ◽  
Vol 11 (9) ◽  
pp. 518
Author(s):  
Honghai Zhang ◽  
Yunpeng Zhang ◽  
Tie Yin ◽  
Jing Wang ◽  
Xiaolin Zhang
Keyword(s):  
Amino Acid ◽  
Ochratoxin A ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Alcaligenes Faecalis ◽  
Degrading Enzyme ◽  
Sds Page ◽  
Ochratoxin Α ◽  
Acid Amidohydrolase

Ochratoxin A (OTA) is a well-known, natural contaminant in foods and feeds because of its toxic effects, such as nephrotoxicity in various animals. Recent studies have revealed that Alcaligenes faecalis could generate enzymes to efficiently degrade OTA to ochratoxin α (OTα) in vitro. In an effort to obtain the OTA degrading mechanism, we purified and identified a novel degrading enzyme, N-acyl-L-amino acid amidohydrolase (AfOTase), from A. faecalis DSM 16503 via mass spectrometry. The same gene of the enzyme was also encountered in other A. faecalis strains. AfOTase belongs to peptidase family M20 and contains metal ions at the active site. In this study, recombination AfOTase was expressed and characterized in Escherichia coli. The molecular mass of recombinant rAfOTase was approximately 47.0 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme exhibited a wide temperature range (30–70 °C) and pH adaptation (4.5–9.0) and the optimal temperature and pH were 50 °C and 6.5, respectively.

Production of D-P-HYDROXYPHENYLGLYCINE BY N-CARBAMOYL-D-amino Acid Amidohydrolase-Overproducing Escherichia coli Strains

1999 ◽  
Vol 15 (4) ◽  
pp. 603-607 ◽  
Author(s):  
Y.-P. Chao ◽  
T.-Y. Juang ◽  
J.-T. Chern ◽  
C.-K. Lee
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Acid Amidohydrolase

Expression, crystallization and preliminary X-ray diffraction studies ofN-carbamyl-D-amino-acid amidohydrolase fromAgrobacterium radiobacter

1999 ◽  
Vol 55 (3) ◽  
pp. 694-695 ◽  
Author(s):  
Wen-Hwei Hsu ◽  
Fan-Tso Chien ◽  
Chuan-Long Hsu ◽  
Tse-Chi Wang ◽  
Hanna S. Yuan ◽  
...  
Keyword(s):  
Amino Acid ◽  
X Ray Diffraction ◽  
X Ray ◽  
Acid Amidohydrolase

scholarly journals Thermostability Reinforcement through a Combination of Thermostability-related Mutations ofN-Carbamyl-D-Amino Acid Amidohydrolase

1999 ◽  
Vol 63 (1) ◽  
pp. 91-95 ◽  
Author(s):  
Yasuhiro IKENAKA ◽  
Hirokazu NANBA ◽  
Kazuyoshi YAJIMA ◽  
Yukio YAMADA ◽  
Masayuki TAKANO ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Amidohydrolase

scholarly journals Crystal structure of N-carbamyl-d-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases

Structure ◽  
2000 ◽  
Vol 8 (7) ◽  
pp. 729-738 ◽  
Author(s):  
Takahisa Nakai ◽  
Tomokazu Hasegawa ◽  
Eiki Yamashita ◽  
Masaki Yamamoto ◽  
Takashi Kumasaka ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Acid Amidohydrolase
Sign in / Sign up

Export Citation Format

Share Document