| First Author | Edgar AJ | Year | 2002 |
| Journal | Biochem Biophys Res Commun | Volume | 292 |
| Issue | 3 | Pages | 617-25 |
| PubMed ID | 11922611 | Mgi Jnum | J:75883 |
| Mgi Id | MGI:2177994 | Doi | 10.1006/bbrc.2002.6692 |
| Citation | Edgar AJ, et al. (2002) Cloning and Tissue Distribution of Three Murine alpha/beta Hydrolase Fold Protein cDNAs. Biochem Biophys Res Commun 292(3):617-25 |
| abstractText | We have cloned 3 novel murine cDNAs encoding proteins containing an alpha/beta hydrolase fold; a catalytic domain found in a very wide range of enzymes. These proteins belong to the prosite UPF0017 uncharacterized protein family and we have named them lung alpha/beta hydrolase 1, 2, and 3 (LABH) since they were cloned from lung cDNA. All have 9 coding exons, encoding 412, 425, and 411 residue proteins respectively (46-48 kDa); LABH1 being closely related to LABH3 having 45% identity. All 3 proteins have a single predicted amino-terminus transmembrane domain. An alignment of family members from different phyla enabled the identification of the LABH1 catalytic triad as Ser211, Asp337, and His366. mRNA expression levels of LABH1 and 3 were highest in liver and LABH2 highest in testis. These findings suggest that the LABH proteins consist of a novel family of membrane bound enzymes whose function has yet to be determined. (c)2002 Elsevier Science (USA). |
