amidohydrolase

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a·mi·do·hy·dro·lase

(am'i-dō-hī'drō-lās)
[EC class 3.5.1 and 3.5.2] An enzyme hydrolyzing C-N bonds of amides and cyclic amides; e.g., asparaginase, barbiturase, urease, amidase.
Synonym(s): amidases, deamidase, deamidizing enzyme.
References in periodicals archive ?
These enzymes include N-acetylmuramidase, N-acetyl glucosaminidase, N-acetylmuramyl-L-alanine amidase, and endopeptidase [8-11].
A 63.3 kDa N-terminal domain possesses amidase activity while a 53.6 kDa N-terminal domain possesses the glucosaminidase activity [15-18].
The recombinant Atl proteins that possess only the C-terminal glucosaminidase activity domain but truncated amidase domain did not result in any visible autolytic activity in the zymography (Figure 3, lanes 4-9).
No lytic activity was observed with any of the other recombinant His-tagged Atl proteins with larger deletions of the amidase domain (Table 2).
By generating enzymatically inactive point mutations, it has been shown that both the amidase and the glucosaminidase domains of Atl must be catalytically active for 5.
Tomasz, "A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-[beta]-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization," Proceedings of the National Academy of Sciences of the United States of America, vol.
This suggests that any CDEPA or CMEPA produced in this time was either not being metabolized to the corresponding aniline by the aryl amidase or metabolized so slowly as to preclude detection.