Unknown

Dataset Information

0

Conserved family of glycerol kinase loci in Drosophila melanogaster.


ABSTRACT: Glycerol kinase (GK) is an enzyme that catalyzes the formation of glycerol 3-phosphate from ATP and glycerol, the rate-limiting step in glycerol utilization. We analyzed the genome of the model organism Drosophila melanogaster and identified five GK orthologs, including two loci with sequence homology to the mammalian Xp21 GK protein. Using a combination of sequence analysis and evolutionary comparisons of orthologs between species, we characterized functional domains in the protein required for GK activity. Our findings include additional conserved domains that suggest novel nuclear and mitochondrial functions for glycerol kinase in apoptosis and transcriptional regulation. Investigation of GK function in Drosophila will inform us about the role of this enzyme in development and will provide us with a tool to examine genetic modifiers of human metabolic disorders.

SUBMITTER: Martinez Agosto JA 

PROVIDER: S-EPMC2807631 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Conserved family of glycerol kinase loci in Drosophila melanogaster.

Martinez Agosto Julian A JA   McCabe Edward R B ER  

Molecular genetics and metabolism 20060320 4


Glycerol kinase (GK) is an enzyme that catalyzes the formation of glycerol 3-phosphate from ATP and glycerol, the rate-limiting step in glycerol utilization. We analyzed the genome of the model organism Drosophila melanogaster and identified five GK orthologs, including two loci with sequence homology to the mammalian Xp21 GK protein. Using a combination of sequence analysis and evolutionary comparisons of orthologs between species, we characterized functional domains in the protein required for  ...[more]

Similar Datasets

| S-EPMC2734154 | biostudies-literature
| S-EPMC2704441 | biostudies-literature
| S-EPMC2246290 | biostudies-literature
| S-EPMC2556263 | biostudies-literature
| S-EPMC3610688 | biostudies-literature
| S-EPMC133815 | biostudies-literature
| S-EPMC1975812 | biostudies-literature
| S-EPMC3302884 | biostudies-literature
| S-EPMC6718298 | biostudies-literature
| S-EPMC301008 | biostudies-other