amidohydrolases


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am·i·do·hy·dro·las·es

(am'i-dō-hī'drō-lās'ez),
Enzymes that hydrolyze C-N bonds of amides and cyclic amides, for example, asparaginase, barbiturase, urease, amidase.
References in periodicals archive ?
Huang, "Inhibition of a putative dihydropyrimidinase from Pseudomonas aeruginosa PAO1 by flavonoids and substrates of cyclic amidohydrolases," PLoS One, vol.
Sander, "An evolutionary treasure: unification of a broad set of amidohydrolases related to urease," Proteins: Structure, Function, and Genetics, vol.
Huang, "Allantoinase and dihydroorotase binding and inhibition by flavonols and the substrates of cyclic amidohydrolases," Biochimie, vol.
Dobritzsch, "The crystal structures of dihydropyrimidinases reaffirm the close relationship between cyclic amidohydrolases and explain their substrate specificity," Journal of Biological Chemistry, vol.
For example, hydantoinase purified from Agrobacterium species has no 5,6-dihydropyrimidine amidohydrolase activity [13].
Dihydropyrimidinase, hydantoinase, imidase, allantoinase, and dihydroorotase belong to the cyclic amidohydrolase family because of their functional and structural similarities [17].
aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases (Figure 3(a)) and other members of the amidohydrolase family of enzymes, such as hydantoinases, dihydroorotases, and allantoinases (Figure 3(b)).
A hydantoinase with no 5,6-dihydropyrimidine amidohydrolase activity," European Journal of Biochemistry, vol.
Clemente-Jimenez et al., "Structure of dihydropyrimidinase from Sinorhizobium meliloti CECT4114: new features in an amidohydrolase family member," Journal of Structural Biology, vol.