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Lipases Provide a New Mechanistic Model for Polyhydroxybutyrate (PHB) Synthases:  Characterization of the Functional Residues in Chromatiumvinosum PHB Synthase

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Departments of Chemistry and Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139
Cite this: Biochemistry 2000, 39, 14, 3927–3936
Publication Date (Web):March 14, 2000
https://doi.org/10.1021/bi9928086
Copyright © 2000 American Chemical Society

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    Abstract

    Polyhydroxybutyrate (PHB) synthases catalyze the conversion of β-hydroxybutyryl coenzyme A (HBCoA) to PHB. These enzymes require an active site cysteine nucleophile for covalent catalysis. A protein BLASTp search using the Class III Chromatiumvinosum synthase sequence reveals high homology to prokaryotic lipases whose crystal structures are known. The homology is very convincing in the α-β-elbow (with the active site nucleophile)-α-β structure, residues 131−175 of the synthase. A conserved histidine of the Class III PHB synthases aligns with the active site histidine of the lipases using the ClustalW algorithm. This is intriguing as this histidine is approximately 200 amino acids removed in sequence space from the catalytic nucleophile. Different threading algorithms suggest that the Class III synthases belong to the α/β hydrolase superfamily which includes prokaryotic lipases. Mutagenesis studies were carried out on C.vinosum synthase C149, H331, H303, D302, and C130 residues. These studies reveal that H331 is the general base catalyst that activates the nucleophile, C149, for covalent catalysis. The model indicates that C130 is not involved in catalysis as previously proposed [Müh, U., Sinskey, A. J., Kirby, D. P., Lane, W. S., and Stubbe, J. (1999) Biochemistry38, 826−837]. Studies with D302 mutants suggest D302 functions as a general base catalyst in activation of the 3-hydroxyl of HBCoA (or a hydroxybutyrate acyl enzyme) for nucleophilic attack on the covalently linked thiol ester intermediate. The relationship of the lipase model to previous models based on fatty acid synthases is discussed.

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     This work was supported by NIH grant GM49171 to J.S. and A.J.S. T.J.K. was supported by NIH training grant CA09112.

     Department of Chemistry.

    §

     Department of Biology.

    *

     To whom correspondence should be addressed:  telephone (617) 253-1814, fax (617) 258-7247, e-mail [email protected].

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