Results 211 to 220 of about 6,806 (259)

Efficient Secretory Expression and Purification on Three Insoluble Amidohydrolases for Ochratoxin A Hydrolysis by Pichia pastoris.

Journal of Agricultural and Food Chemistry
As a highly toxic mycotoxin, ochratoxin A (OTA) is widely contaminating agricultural products and has various toxicological effects. Bioenzymes for OTA degradation have shown promising potential for detoxification. Other than the efficient amidohydrolase
Xuanjun Zhang, Xue Ma, Guangqing Dai, Xiaojie Fu, Yu Zhou   +4 more
semanticscholar   +1 more source

Catalytic Properties of Purified Recombinant Anandamide Amidohydrolase

Prostaglandins & Other Lipid Mediators, 1999
The major degradative pathway of anandamide, an endogenous ligand for cannabinoid receptors, is its enzymatic hydrolysis to arachidonic acid and ethanolamine.1The enzyme responsible for this reaction has been referred to as anandamide amidohydrolase23or fatty acid amide hydrolase.4‘N-Acylethanolamine amidohydrolase’ reported much earlier by Schmid and ...
Natsuo, Ueda, Kazuhisa, Katayama, Sravan Kumar, Goparaju, Yuko, Kurahashi, Kenji, Yamanaka, Hiroshi, Suzuki, Shozo, Yamamoto   +6 more
openaire   +2 more sources

Amidohydrolases of the reductive pyrimidine catabolic pathway purification, characterization, structure, reaction mechanisms and enzyme deficiency.

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2008
K. Schnackerz, D. Dobritzsch
semanticscholar   +2 more sources

Characterization of unexplored amidohydrolase enzyme—pterin deaminase

Applied Microbiology and Biotechnology, 2016
Pterin deaminase is an amidohydrolase enzyme hydrolyzing pteridines to form lumazine derivatives and ammonia. The enzyme captured the attention of scientists as early as 1959 and had been patented for its application as an anticancer agent. It is ubiquitously present in prokaryotes and has been reported in some eukaryotes such as honey bee, silkworm ...
Angayarkanni, Jayaraman, Murugesan, Thandeeswaran, Ulaganathan, Priyadarsini, Shanmugam, Sabarathinam, K A Ayub, Nawaz, Muthusamy, Palaniswamy   +5 more
openaire   +2 more sources

Structural Insights into the Substrate Specificity of (S)-Ureidoglycolate Amidohydrolase and Its Comparison with Allantoate Amidohydrolase

Journal of Molecular Biology, 2014
In plants, the ureide pathway is a metabolic route that converts the ring nitrogen atoms of purine into ammonia via sequential enzymatic reactions, playing an important role in nitrogen recovery. In the final step of the pathway, (S)-ureidoglycolate amidohydrolase (UAH) catalyzes the conversion of (S)-ureidoglycolate into glyoxylate and releases two ...
Inchul Shin, Kitae Han, Sangkee Rhee
openaire   +2 more sources

Penicillin amidohydrolase productivity of locally isolated bacterial species

Folia Microbiologica, 1991
Penicillin amidohydrolase productivity of four locally isolated bacterial species is described. Organisms were identified as Escherichia coli, Pseudomonas aeruginosa, Sarcina lutea and Bacillus megaterium. Highest enzyme productivity of 3.2 U/mL with a corresponding dry cell mass of 4.5 g/L was recorded from S. lutea.
Z A, Mahmood, D, Shaikh, S M, Zoha
openaire   +2 more sources

Enzymological and Molecular Biological Studies on Anandamide Amidohydrolase

1999
Previously we suggested that anandamide amidohydrolase partially purified from porcine brain catalyzed the anandamide synthesis. The reversibility of the anandamide hydrolytic reaction was confirmed with a recombinant enzyme of rat liver. We also showed that the recombinant enzyme had a wide substrate specificity hydrolyzing primary amides and esters ...
Ueda N, Katayama K, Kurahashi Y, Suzuki M, Suzuki H, Yamamoto S, Katoh I, Di Marzo V, De Petrocellis L   +8 more
openaire   +4 more sources

Anandamide Amidohydrolase from Porcine Brain

1997
Ethanolamide of arachidonic acid was isolated from porcine brain as an endogenous ligand for cannabinoid receptors, and referred to as anandamide.1 In consideration of various biological activities of anandamide,2 it is very important to elucidate how the production and degradation of this new compound are regulated by enzymes within the cells.
Natsuo Ueda, Yuko Kurahashi, Kei Yamamoto, Shozo Yamamoto   +3 more
openaire   +1 more source

Structural and Catalytic Diversity within the Amidohydrolase Superfamily

Biochemistry, 2005
The amidohydrolase superfamily comprises a remarkable set of enzymes that catalyze the hydrolysis of a wide range of substrates bearing amide or ester functional groups at carbon and phosphorus centers. The most salient structural landmark for this family of hydrolytic enzymes is a mononuclear or binuclear metal center embedded within the confines of a
Clara M, Seibert, Frank M, Raushel
openaire   +2 more sources

Purification and Characterization of Allantoate Amidohydrolase fromBacillus fastidiosus

Archives of Biochemistry and Biophysics, 1995
Allantoate amidohydrolase from Bacillus fastidiosus was purified 170-fold to homogeneity as judged by isoelectric focusing and nondenaturing and sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular mass was estimated to be 128 kDa. The enzyme appeared to be a homodimer with a subunit molecular mass of 66 kDa.
Xu, Z.W., Windt, F.E. de, Drift, C. van der   +2 more
openaire   +3 more sources