The Discovery of <i>N</i> <sup>2</sup>,<i>N</i> <sup>2</sup>‑Dimethylguanine Hydrolases Unravels General Molecular Principles of Enzyme Evolvability and Promiscuity. [PDF]
ACS CatalDrexler L, Duran C, Osuna S, Sterner R.
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The Urea Cycle in Connection to Polyamine Metabolism in Higher Plants: New Perspectives on a Central Pathway. [PDF]
Physiol PlantBuezo J +5 more
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Protein carbamylation and proteomics: from artifacts to elucidation of biological functions. [PDF]
Front Anal SciYou Y, Many G, Nakayasu ES.
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Biodegradation of S-Triazine Herbicides Under Saline Conditions by <i>Paenarthrobacter ureafaciens</i> PC, a New Halotolerant Bacterial Isolate: Insights into Both the Degradative Pathway and Mechanisms of Tolerance to High Salt Concentrations. [PDF]
MicroorganismsFu C, Jiang Y, Xu B, Fu X, Tan L, Jin M.
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Studies on Bacterial β-Aspartyl amidohydrolases
Studies on Bacterial β-Aspartyl amidohydrolasesopenaire
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Dihydropyrimidine amidohydrolase is a zinc metalloenzyme
Biochimica Et Biophysica Acta - Biomembranes, 1979Bovine 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.
Eugene G Sander
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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 ...
Kitae Han, Sangkee Rhee
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Crystal structure of N-carbamyl-d-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases [PDF]
Structure, 2000 N-carbamyl-D-amino acid amidohydrolase (DCase) catalyzes the hydrolysis of N-carbamyl-D-amino acids to the corresponding D-amino acids, which are useful intermediates in the preparation of beta-lactam antibiotics. To understand the catalytic mechanism of N-carbamyl-D-amino acid hydrolysis, the substrate specificity and thermostability of the enzyme, we
Takahisa Nakai +2 more
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Allantoate hydrolysis by allantoate amidohydrolase
Archives of Biochemistry and Biophysics, 1970Abstract 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 +2 more
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