| First Author | Flick MJ | Year | 2002 |
| Journal | Biochem Biophys Res Commun | Volume | 295 |
| Issue | 4 | Pages | 910-6 |
| PubMed ID | 12127981 | Mgi Jnum | J:113942 |
| Mgi Id | MGI:3687894 | Doi | 10.1016/s0006-291x(02)00768-4 |
| Citation | Flick MJ, et al. (2002) Identification of putative mammalian D-lactate dehydrogenase enzymes. Biochem Biophys Res Commun 295(4):910-6 |
| abstractText | Mammalian L-isomer dehydrogenases represent an expansive and well characterized class of metabolic enzymes. Surprisingly, little is known regarding their evolutionarily distinct counterparts, D-isomer dehydrogenases, since few mammalian D-isomer 2-hydroxy acid enzymes have been isolated. Here we present the identification and initial characterization of putative human and murine D-lactate dehydrogenases (DLD) that can interact with the muscle-specific cysteine-rich protein CRP3/MLP. Sequence analysis reveals that the human and mouse transcripts encode novel proteins that display strong similarities to the yeast D-lactate dehydrogenase proteins DLD1, AIP2, and YEL071W. Expression analysis of the mammalian proteins indicates widespread distribution with transcripts present in striated muscle tissues and a variety of other tissue types. Immunofluorescence subcellular localization of the mouse DLD protein indicates that it resides within mitochondria, a feature shared by many dehydrogenases. The identification of the human and mouse DLD clones provides new insight regarding the activity of D-isomer-specific enzymes in mammalian cells. |
