Results 121 to 130 of about 4,894 (170)

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
exaly   +3 more sources

Allantoate hydrolysis by allantoate amidohydrolase

Archives of Biochemistry and Biophysics, 1970
Abstract The degradation of allantoate by allantoate amidohydrolase from Streptococcus allantoicus resulted in the production of 1 mole of carbon dioxide, 2 moles of NH 3 , and probably 1 mole of (−)-ureidoglycolate per mole of allantoate. Ureidoglycine was an intermediate and presumably also a substrate for allantoate amidohydrolase.
C, van der Drift, F E, de Windt, G D, Vogels   +2 more
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The characterization of amidohydrolases in a freshwater lake sediment

Microbial Ecology, 1989
The properties of three amidohydrolases, i.e., urease (I) EC 3.5.1.5, L-asparaginase (II) EC 3.5.1.1, and L-glutaminase (III) EC 3.5.1.2, were studied in sediment samples taken from a shallow eutrophic freshwater lake.Sediment samples were air dried (ADS) and stored for at least 3 months before being enzymically characterized.
Sallis, P J, Burns, Richard G
openaire   +4 more sources

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
openaire   +2 more sources

The Purification and Properties of an Amidohydrolase from Soybean

Canadian Journal of Biochemistry, 1974
An amidohydrolase (EC 3.5.1.13) was isolated from the roots of soybean (Glycine max Merril, var. Hawkeye) seedlings and purified 130-fold over the crude extract with 30% recovery. The purification steps entailed ammonium sulfate precipitation, gel filtration, cellulose ion-exchange chromatography, and polyacrylamide gel electrophoresis.
R E, Hoagland, G, Graf
openaire   +2 more sources

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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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

Mechanism and thermodynamics of ligand binding to auxin amidohydrolase

Journal of Molecular Recognition, 2011
AbstractBrILL2 is catalytically the most efficient auxin amidohydrolase from Brassica rapa, playing a key role in auxin metabolism by catalyzing its release from amino acid conjugates. Auxins, with the most abundant representative indole‐acetic acid ([1H‐indol‐3‐yl]‐acetic acid, IAA), are a group of plant hormones that in very small concentrations ...
Simunovic, Mijo, Zagrovic, Bojan, Tomic, Sanja   +2 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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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