Identity of heart and liver L-3-hydroxyacyl coenzyme A dehydrogenase

Rat heart and liver cDNAs for precursor of L-3-hydroxyacyl-CoA dehydrogenas e have been cloned and sequenced. The results indicate that these different rat organs express identical dehydrogonases. Furthermore, pig heart mRNA f or L-3-hydroxyacyl-CoA dehydrogenase precursor was amplified by reverse tra nscription-polymerase chain reaction, and all the cDNA clones were found to encode a precursor of liver L-3-hydroxyacyl-CoA dehydrogenase (X.-Y. He, S .-Y. Yang, Biochim. Biophys, Acta 1392 (1998) 119-126) but not the well-doc umented heart form of the dehydrogenase (K.G. Bitar et al., FEES Lett. 116( 1980) 196-198). Sequencing data and other evidence establish that the pig, like the rat, has the same dehydrogenase in heart and liver. Since the size and structure of pig heart L-3-hydroxyacyl-CoA dehydrogenase are identical to the pie liver dehydrogenase, reports that relied on the published seque nce of the pig heart dehydrogenase need to be reevaluated. For example, the signature pattern of the L-3-hydroxyacyl-CoA dehydrogenase family is HXFXP X3MXLXE. Furthermore, the published crystal structure of the pig heart dehy drogenase that substantiated each subunit comprising 307 residues with a me rcury-binding residue at position 204 (J.J. Birktoft et al., Proc. Natl. Ac ad. Sci. U.S.A. 84 (1987) 8262-8266) must be re-examined in accordance with this revelation. (C) 1999 Elsevier Science B.V. All rights reserved.