Results 141 to 150 of about 3,806 (190)
Evolution of Cyclic Amidohydrolases: A Highly Diversified Superfamily [PDF]
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).
Bernard Labedan +2 more
exaly +5 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Amidohydrolases in soils as affected by cropping systems
Applied Soil Ecology, 2003Cropping systems influence the ecology of agricultural soils. The effects of crop rotation and N fertilization on the activities of four amidohydrolases (amidase, l-asparaginase, l-aspartase, and l-glutaminase) were studied in soils of two long-term cropping systems in Iowa: the Northeast Research Center (NERC) and the Clarion–Webster Research Center ...
M A Tabatabai
exaly +2 more sources
Identification of the structural similarity in the functionally related amidohydrolases acting on the cyclic amide ring [PDF]
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
exaly +1 more source
Dihydropyrimidine amidohydrolases and dihydroorotases share the same origin and several enzymatic properties [PDF]
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
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
openaire +2 more sources
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
openaire +2 more sources
Aminolytic reaction catalyzed by d-stereospecific amidohydrolases from Streptomyces spp [PDF]
Tadashi Hatanaka
exaly +2 more sources
Amidohydrolases of the reductive pyrimidine catabolic pathway
Biochimica Et Biophysica Acta - Proteins and Proteomics, 2008Doreen Dobritzsch, Klaus D Schnackerz
exaly +2 more sources
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
openaire +2 more sources
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
The characterization of amidohydrolases in a freshwater lake sediment
Microbial Ecology, 1989The 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

