Results 181 to 190 of about 6,120 (217)

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, Shozo Yamamoto, Kenji Yamanaka, Yuko Kurahashi, Sravan Kumar Goparaju, Kazuhisa Katayama, Hiroshi Suzuki   +6 more
openaire   +4 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 ...
Shanmugam Sabarathinam, K. A. Ayub Nawaz, Murugesan Thandeeswaran, Ulaganathan Priyadarsini, Muthusamy Palaniswamy, Angayarkanni Jayaraman   +5 more
openaire   +3 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   +5 more sources

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 ...
Shozo Yamamoto, Natsuo Ueda
openaire   +3 more sources

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   +3 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   +4 more sources

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
openaire   +3 more sources

Resolution of S-benzyl-DL-penicillamine with penicillin amidohydrolase [PDF]

Collection of Czechoslovak Chemical Communications, 1981
Racemic m-phenylacetyl-S-benzylpenicillamine was resolved into otical isomers by action of penicillin amidohydrolase (E.C.3.5.1.11) in high yield and optical purity.
Petr Šimek, Karel Jošt, Vladimír Vojtíšek, Miroslav Bárta, Tomislav Barth   +4 more
openaire   +1 more source

Protonic reorganization and substrate structure in catalysis by amidohydrolases

Journal of the American Chemical Society, 1980
D. Quinn, K. S. Venkatasubban, M. Kise, R. Schowen   +3 more
semanticscholar   +3 more sources

Purification of Penicillin Amidohydrolase, an Enzyme for Semisynthetic Procedures

Collection of Czechoslovak Chemical Communications, 1992
Penicillin amidohydrolase (EC 3.5.1.11.) is one of the few enzymes used successfully for deprotection of primary amino groups of semisynthetic peptides. The available material is usually contamined by endo- and exopeptidases. We managed to prepare the enzyme devoid of trypsin- and chymotrypsin-like activities using affinity chromatography with specific
Ivo Bláha, Ivan Svoboda, Tomislav Barth, Jiří Jiráček, Jiří Velek, Jan Pospíšek   +5 more
openaire   +2 more sources