Results 161 to 170 of about 10,073 (196)

Guanine storage vacuoles sequester guanine crystals and serve as nitrogen reserves in <i>Chlamydomonas reinhardtii</i>. [PDF]

Proc Natl Acad Sci U S A
Goodenough U, Roth R, Lee JH.
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Ring A Cleaving Beta-Diketone Hydrolase Is a Key Enzyme of Steroid Degradation in Anaerobic Bacteria. [PDF]

Environ Microbiol
Jacoby C, Peller L, Wenzler J, Luttermann M, Seiche W, Breit B, Boll M.   +6 more
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Studies on Bacterial β-Aspartyl amidohydrolases

Studies on Bacterial β-Aspartyl amidohydrolases
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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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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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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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