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J. Biol. Chem., Vol. 276, Issue 39, 36215-36224, September 28, 2001
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,,
From the A novel type of hydrolase was purified from
culture fluid of Paucimonas (formerly
Pseudomonas) lemoignei. Biochemical
characterization revealed an unusual substrate specificity of the
purified enzyme for amorphous
poly((R)-3-hydroxyalkanoates) (PHA) such as
native granules of natural poly((R)-3-hydroxybutyrate)
(PHB) or poly((R)-3-hydroxyvalerate) (PHV),
artificial cholate-coated granules of natural PHB or PHV, atactic
poly((R,S)-3-hydroxybutyrate), and oligomers of
(R)-3-hydroxybutyrate (3HB) with six or more 3HB units. The
enzyme has the unique property to recognize the physical state of the
polymeric substrate by discrimination between amorphous PHA (good
substrate) and denatured, partially crystalline PHA (no substrate). The
pentamers of 3HB or 3HV were identified as the main products of
enzymatic hydrolysis of native PHB or PHV, respectively. No activity
was found with any denatured PHA, oligomers of (R)-3HB with
five or less 3HB units, poly(6-hydroxyhexanoate), substrates of lipases
such as tributyrin or triolein, substrates for amidases/nitrilases,
DNA, RNA, casein,
N- Institut für Mikrobiologie,
Universität Stuttgart, Allmandring 31, 70569 Stuttgart, Germany,
the § Department of Chemistry "G. Ciamician" and Centro
di Studio per la Fisica delle Macromolecole del Consiglio Nazionale
delle Ricerche, University of Bologna, 40126 Bologna, Italy; and the
¶ Polish Academy of Sciences, Centre of Polymer Chemistry, 41-800, Zabrze, Poland
-benzoyl-L-arginine-4-nitranilide, or
starch. The purified enzyme (Mr 36,209)
was remarkably stable and active at high temperature (60 °C), high
pH (up to 12.0), low ionic strength (distilled water), and in solvents
(e.g. n-propyl alcohol). The depolymerase contained no essential SH groups or essential disulfide bridges and was insensitive to high concentrations of ionic (SDS) and
nonionic (Triton and Tween) detergents. Characterization of the cloned
structural gene (phaZ7) and the DNA-deduced amino
acid sequence revealed no homologies to any PHB depolymerase or any other sequence of data banks except for a short sequence related to the
active site serine of serine hydrolases. A classification of the enzyme
into a new family (family 9) of carboxyesterases (Arpigny, J. L.,
and Jaeger, K.-E. (1999) Biochem. J. 343, 177-183) is suggested.
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