Results 111 to 120 of about 3,541 (141)

Glutaminase activity of L-asparagine amidohydrolase

Biochemical Pharmacology, 1969
Relatively high concentrations of 6-diazo-5-oxo-norleucine (DON) and azaserine, potent specific inhibitors of many enzymes using glutamine as substrate, do not have an appreciable effect on the activity of Escherechia coliL-asparagine amido-hydrolase (EC 3.5.1.1) when either asparagine or glutamine is used as substrate.
H K, Miller, M E, Balis
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Dihydropyrimidine amidohydrolase is a zinc metalloenzyme

Biochimica et Biophysica Acta (BBA) - Enzymology, 1979
Bovine liver dihydropyrimidine amidohydrolase (EC 3.5.2.2) has been subjected to atomic absorption analysis. Three different preparations of homogeneous enzyme indicated that the enzyme contains 4.3 +/- 0.3 g atoms of Zn2+ per mol of enzyme or 1.1 g atoms of Zn2+ per subunit. No Co2+, Mn2+, Mg2+ or Cd2+ was detected.
K P, Brooks, B D, Kim, E G, Sander
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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
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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
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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
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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
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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
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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
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Evolution of Cyclic Amidohydrolases: A Highly Diversified Superfamily

Journal of Molecular Evolution, 2013
Dihydroorotases are universal proteins catalyzing the third step of pyrimidine biosynthesis. These zinc metalloenzymes belong to the superfamily of cyclic amidohydrolases, comprising also other enzymes that are involved in degradation of either purines (allantoinases), pyrimidines (dihydropyrimidinases) or hydantoins (hydantoinases).
Barba, Matthieu, Labedan, Bernard, Glansdorff, Nicolas   +2 more
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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
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