1 hosphonoacetaldehyde hydrolase (trivial name phosphonatase).

2 The similarity of backbone folds observed in phosphonatase and the 2-haloacid dehalogenase of the HAD

3 between the open and closed conformations of phosphonatase and the hypothesis that ligand binding sta

4 llus cereus phosphonoacetaldehyde hydrolase (phosphonatase) as an experimental model for metal-activa

5                                We found that phosphonatase belongs to a novel family of hydrolases wh

6 nding and the known stereochemical course of phosphonatase-catalyzed hydrolysis at phosphorus (retent

7             Phosphonoacetaldehyde hydrolase (phosphonatase) catalyzes the hydrolysis of phosphonoacet

8             Phosphonoacetaldehyde hydrolase (phosphonatase) catalyzes the hydrolysis of phosphonoacet

9             Phosphonoacetaldehyde hydrolase (phosphonatase) catalyzes the hydrolytic P-C bond cleavag

10 he x-ray crystal structures of the wild-type phosphonatase complexed with Mg(II) alone or with Mg(II)

11      Homologous genes for both C-P lyase and phosphonatase degradative pathways are distributed in di

12 erfamily includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases

13             Phosphonoacetaldehyde hydrolase (phosphonatase) from Bacillus cereus catalyzes hydrolytic

14 used along with that from the S. typhimurium phosphonatase gene sequence to search the primary sequen

15 protein sequence inferred from the B. cereus phosphonatase gene was determined, and this sequence was

16 ray crystal structure of the Bacillus cereus phosphonatase homodimer complexed with the phosphate (pr

17            In this study, the genes encoding phosphonatase in Bacillus cereus and in Salmonella typhi

18 vel of catalytic activity in the G185D/D190G phosphonatase mutant demonstrated the plasticity of the

19 dues at these stations by the dehalogenases, phosphonatases, phosphatases, and phosphomutases of the

20                                   Within the phosphonatase subfamily, Asp186 is stringently conserved

21 etic properties of the purified, recombinant phosphonatases were determined.