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Regulation of Petal Coloration by the Auxin Amide Hydrolase Gene <i>RhILL1</i> in Rose (<i>Rosa hybrida</i>). [PDF]
Genes (Basel)Wang D +10 more
europepmc +1 more source
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).
Nicolas Glansdorff +2 more
exaly +5 more sources
FEBS Letters, 2014 NMN deamidase (PncC) is a bacterial enzyme involved in NAD biosynthesis. We have previously demonstrated that PncC is structurally distinct from other known amidohydrolases.
Leonardo Sorci +2 more
exaly +3 more sources
Penicillin Amidohydrolases in Fungal Autolysis [PDF]
Microbiology and Immunology, 1989 AbstractThe production of penicillin G and penicillin V amidohydrolases or acylases (E.C.3.5.1.11) was studied during the autolysis of filamentous fungi in a mineral medium, and in the same medium with phenoxyacetic acid as inducer. In all the studied fungi, enzymes showing penicillin G and penicillin V amidohydrolase activities were found.
CARLOS Alfonso +2 more
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Biochemical Journal, 1998 The functionally related amidohydrolases, including D-hydantoinases, dihydropyrimidinases, allantoinases and dihydro-orotases, share a similar catalytic function of acting on the cyclic amide ring.
G J Kim
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Nucleic Acids Research, 2003 Slime mold, plant and insect dihydropyrimidine amidohydrolases (DHPases, EC 3.5.2.2), which catalyze the second step of pyrimidine and several anti-cancer drug degradations, were cloned and shown to functionally replace a defective DHPase enzyme in the ...
Birgit Andersen +2 more
exaly +1 more source
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Dihydropyrimidine amidohydrolase is a zinc metalloenzyme
Biochimica et Biophysica Acta (BBA) - Enzymology, 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.
K P, Brooks, B D, Kim, E G, Sander
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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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Aminolytic reaction catalyzed by d-stereospecific amidohydrolases from Streptomyces spp
Biochimie, 2011 Tadashi Hatanaka, Nobuhiro Mori
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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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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
openaire +2 more sources