Results 201 to 210 of about 5,211 (236)

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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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 (fatty acid amide hydrolase)

Prostaglandins & Other Lipid Mediators, 2000
Anandamide (N-arachidonoylethanolamine) loses its cannabimimetic activity when it is hydrolyzed to arachidonic acid and ethanolamine by the catalysis of an enzyme referred to as anandamide amidohydrolase or fatty acid amide hydrolase. Cravatt's group and our group cloned cDNA of the enzyme from rat, human, mouse and pig, and the primary structures ...
N, Ueda, S, Yamamoto
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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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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
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Novel Inhibitors of Brain, Neuronal, and Basophilic Anandamide Amidohydrolase

Biochemical and Biophysical Research Communications, 1997
Mammalian brain as well as mouse neuroblastoma (N18TG2) and rat basophilic leukaemia (RBL) cells were previously shown to contain "anandamide amidohydrolase', a membrane-bound enzyme sensitive to serine and cysteine protease inhibitors and catalyzing the hydrolysis of the endogenous cannabimimetic metabolite, anandamide (arachidonoyl-ethanolamide ...
De Petrocellis L, Melck D, Ueda N, Maurelli S, Kurahashi Y, Yamamoto S, Marino G, Di Marzo V   +7 more
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Inhibition of Serine Amidohydrolases by Complexes of Vanadate with Hydroxamic Acids

Biochemical and Biophysical Research Communications, 2000
Serine beta-lactamases are inhibited by phosphonate monoester monoanions. These compounds phosphonylate the active site serine hydroxyl group to form inert, covalent complexes. Since spontaneous hydrolysis of these phosphonates is generally quite slow, the beta-lactamase active site must have considerable affinity for the (presumably) pentacoordinated ...
J H, Bell, K, Curley, R F, Pratt
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Evolutionary relationship and application of a superfamily of cyclic amidohydrolase enzymes

The Chemical Record, 2005
AbstractCyclic amidohydrolases belong to a superfamily of enzymes that catalyze the hydrolysis of cyclic CN bonds. They are commonly found in nucleotide metabolism of purine and pyrimidine. These enzymes share similar catalytic mechanisms and show considerable structural homologies, suggesting that they might have evolved from a common ancestral ...
Nam, SH Nam, Sung-Hun, Park, HS Park, Hee-Sung, Kim, HS Kim, Hak-Sung   +2 more
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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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Identification of Caerulomycin A Gene Cluster Implicates a Tailoring Amidohydrolase

Organic Letters, 2012
The biosynthetic gene cluster for caerulomycin A (1) was cloned and characterized from the marine actinomycete Actinoalloteichus cyanogriseus WH1-2216-6, which revealed an unusual hybrid polyketide synthase (PKS)/nonribosomal peptide synthetase (NRPS) system.
Yiguang, Zhu, Peng, Fu, Qinheng, Lin, Guangtao, Zhang, Haibo, Zhang, Sumei, Li, Jianhua, Ju, Weiming, Zhu, Changsheng, Zhang   +8 more
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