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Structural and Catalytic Diversity within the Amidohydrolase Superfamily
Biochemistry, 2005The 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, 1995Allantoate 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. +2 more
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Novel Inhibitors of Brain, Neuronal, and Basophilic Anandamide Amidohydrolase
Biochemical and Biophysical Research Communications, 1997Mammalian 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 +7 more
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Inhibition of Serine Amidohydrolases by Complexes of Vanadate with Hydroxamic Acids
Biochemical and Biophysical Research Communications, 2000Serine 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, 2005AbstractCyclic amidohydrolases belong to a superfamily of enzymes that catalyze the hydrolysis of cyclic CN 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 +2 more
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Penicillin amidohydrolase productivity of locally isolated bacterial species
Folia Microbiologica, 1991Penicillin 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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Anandamide Amidohydrolase from Porcine Brain
1997Ethanolamide 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 +3 more
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Arylamidase and amidohydrolases in soils as affected by liming and tillage systems
Soil and Tillage Research, 2004M A Tabatabai
exaly