| A conserved motif within the vitamin K-dependent carboxylase gene is widely distributed across animal phyla. | |
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MedLine Citation:
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PMID: 10893417 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The vitamin K-dependent gamma-glutamyl carboxylase catalyzes the posttranslational conversion of glutamic acid to gamma-carboxyglutamic acid, an amino acid critical to the function of the vitamin K-dependent blood coagulation proteins. Given the functional similarity of mammalian vitamin K-dependent carboxylases and the vitamin K-dependent carboxylase from Conus textile, a marine invertebrate, we hypothesized that structurally conserved regions would identify sequences critical to this common functionality. Furthermore, we examined the diversity of animal species that maintain vitamin K-dependent carboxylation to generate gamma-carboxyglutamic acid. We have cloned carboxylase homologs in full-length or partial form from the beluga whale (Delphinapterus leucas), toadfish (Opsanus tau), chicken (Gallus gallus), hagfish (Myxine glutinosa), horseshoe crab (Limulus polyphemus), and cone snail (Conus textile) to compare these structures to the known bovine, human, rat, and mouse cDNA sequences. Comparison of the predicted amino acid sequences identified a nearly perfectly conserved 38-amino acid residue region in all of these putative carboxylases. In addition, this amino acid motif is also present in the Drosophila genome and identified a Drosophila homolog of the gamma-carboxylase. Assay of hagfish liver demonstrated vitamin K-dependent carboxylase activity in this hemichordate. These results demonstrate the broad distribution of the vitamin K-dependent carboxylase gene, including a highly conserved motif that is likely critical for enzyme function. The vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid appears to be a highly conserved function in the animal kingdom. |
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Authors:
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G S Begley; B C Furie; E Czerwiec; K L Taylor; G L Furie; L Bronstein; J Stenflo; B Furie |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 275 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2000 Nov |
Date Detail:
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Created Date: 2000-12-29 Completed Date: 2000-12-29 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 36245-9 Citation Subset: IM |
Affiliation:
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Marine Biological Laboratory, Woods Hole, Massachusetts 02543, USA. |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/AF278713; AF278714 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Motifs Amino Acid Sequence Animals Carbon-Carbon Ligases / chemistry*, genetics* Chickens Cloning, Molecular Conserved Sequence* Fishes* / genetics Hagfishes / genetics Humans Invertebrates / chemistry, genetics Molecular Sequence Data Sequence Alignment Sequence Homology, Amino Acid Vitamin K / metabolism* Whales* / genetics |
| Grant Support | |
ID/Acronym/Agency:
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HL38216/HL/NHLBI NIH HHS; HL42443/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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12001-79-5/Vitamin K; EC 6.4.-/Carbon-Carbon Ligases; EC 6.4.-/glutamyl carboxylase |
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