Results 141 to 150 of about 3,806 (190)

Evolution of Cyclic Amidohydrolases: A Highly Diversified Superfamily [PDF]

open access: yesJournal 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).
Bernard Labedan   +2 more
exaly   +5 more sources

Amidohydrolases in soils as affected by cropping systems

Applied Soil Ecology, 2003
Cropping 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]

open access: yesBiochemical 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
exaly   +1 more source

Dihydropyrimidine amidohydrolases and dihydroorotases share the same origin and several enzymatic properties [PDF]

open access: yesNucleic 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

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
openaire   +2 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   +2 more
openaire   +2 more sources

Amidohydrolases of the reductive pyrimidine catabolic pathway

Biochimica Et Biophysica Acta - Proteins and Proteomics, 2008
Doreen Dobritzsch, Klaus D Schnackerz
exaly   +2 more sources

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
openaire   +2 more sources

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

Home - About - Disclaimer - Privacy