| Title : Cloning and tissue distribution of three murine alpha\/beta hydrolase fold protein cDNAs - Edgar_2002_Biochem.Biophys.Res.Commun_292_617 |
| Author(s) : Edgar AJ , Polak JM |
| Ref : Biochemical & Biophysical Research Communications , 292 :617 , 2002 |
| Abstract : 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. |
| ESTHER : Edgar_2002_Biochem.Biophys.Res.Commun_292_617 |
| PubMedSearch : Edgar_2002_Biochem.Biophys.Res.Commun_292_617 |
| PubMedID: 11922611 |
| Gene_locus related to this paper: mouse-abhd1 , mouse-abhd3 , mouse-ABHD2 |
| Gene_locus related to this paper: mouse-abhd1 , mouse-abhd3 , mouse-ABHD2 |
Edgar AJ, Polak JM (2002)
Cloning and tissue distribution of three murine alpha\/beta hydrolase fold protein cDNAs
Biochemical & Biophysical Research Communications
292 :617
Edgar AJ, Polak JM (2002)
Biochemical & Biophysical Research Communications
292 :617