Dienelactone hydrolase

Briickmann M, R Blasco, KH Timmis, DH Pieper (1998) Detoxification of protoanemonin by dienelactone hydrolase. Appl Environ Microbiol 64 400-402. 

Schldmann M, E Schmidt, H-J Knackmuss (1990a) Different types of dienelactone hydrolase in 4-fluoro-benzoate-utilizing bacteria. J Bacterial 172 5112-5118. 

It is well established that the same three-dimensional scaffolding in proteins often carries constellations of amino acids with diverse enzymatic functions. A classic example is the large family of a/jS, or TIM, barrel enzymes (Farber and Petsko, 1990 Lesk et ai, 1989). It appears that lipases are no exception to date five other hydrolases with similar overall tertiary folds have been identified. They are AChE from Torpedo calif arnica (Sussman et al., 1991) dienelactone hydrolase, a thiol hydrolase, from Pseudomonas sp. B13 (Pathak and Ollis, 1990 Pathak et al, 1991) haloalkane dehalogenase, with a hitherto unknown catalytic mechanism, from Xanthobacter autotrophicus (Franken et al, 1991) wheat serine carboxypeptidase II (Liao et al, 1992) and a cutinase from Fusa-rium solani (Martinez et al, 1992). Table I gives some selected physical and crystallographic data for these proteins. They all share a similar overall topology, described by Ollis et al (1992) as the a/jS hydrolase... 

Fig. 13. The alp hydrolase fold and it variations. (A) cudnase, (B) dienelactone hydrolase and haloalkane dehalogenase, (C) wheat carboxypepddase, (D) RmL, (E) hPL, (F) GcL and AChE the three catalytic residues, always in the order Ser, Asp/Glu, and His, appear as dark dots. The folds are aligned in such a way as to show the structural homologies within the hydrolytic domains, somewhat divorced from the N-terminal part of the sheet. The hPL is a two-domain protein, and the location of the additional C-terminal domain is indicated.

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