ArticleThe Journal of biological chemistry2010
Effect of vitamin K-dependent protein precursor propeptide, vitamin K hydroquinone, and glutamate substrate binding on the structure and function of {gamma}-glutamyl carboxylase.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 16 citations in OpenAlex.
- Structural and functional insights into γ-glutamyl carboxylase-factor IX interaction: implications for vitamin K-dependent bleeding disorders.Haematologica · 2026Article
- Molecular insights into the comorbidity of vitamin K-dependent clotting factor deficiency and chondrodysplasia punctata.Journal of thrombosis and haemostasis : JTH · 2025Article
- Structural insight into bicarbonate-mediated carboxylation by human vitamin K-dependent carboxylase.Nature communications · 2025Article
- Molecular basis of vitamin K-dependent protein γ-glutamyl carboxylation.Cell research · 2025Article
- Structural insights into the vitamin K-dependent γ-carboxylation of osteocalcin.Cell research · 2025Article
- Sustained high expression of human FVII following AAV8-mediated gene delivery in mice.Molecular therapy. Methods & clinical development · 2025Article
- Article
- The Molecular Basis of FIX Deficiency in Hemophilia B.International journal of molecular sciences · 2022Review
- Characterization of missense mutations in the signal peptide and propeptide of FIX in hemophilia B by a cell-based assay.Blood advances · 2020Article
- Insights into vitamin K-dependent carboxylation: home field advantage.Haematologica · 2020Article
- Vitamin K-dependent carboxylation of coagulation factors: insights from a cell-based functional study.Haematologica · 2020Article
- The WAGR syndrome gene PRRG4 is a functional homologue of the commissureless axon guidance gene.PLoS genetics · 2017Article
- Functional Study of the Vitamin K Cycle Enzymes in Live Cells.Methods in enzymology · 2017Article
- Characterization of vitamin K-dependent carboxylase mutations that cause bleeding and nonbleeding disorders.Blood · 2016Article
- Structural and functional insights into enzymes of the vitamin K cycle.Journal of thrombosis and haemostasis : JTH · 2016Review
- A conformational investigation of propeptide binding to the integral membrane protein γ-glutamyl carboxylase using nanodisc hydrogen exchange mass spectrometry.Biochemistry · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The γ-glutamyl carboxylase utilizes four substrates to catalyze carboxylation of certain glutamic acid residues in vitamin K-dependent proteins. How the enzyme brings the substrates together to promote catalysis is an important question in understanding the structure and function of this enzyme. The propeptide is the primary binding site of the vitamin K-dependent proteins to carboxylase. It is also an effector of carboxylase activity. We tested the hypothesis that binding of substrates causes changes to the carboxylase and in turn to the substrate-enzyme interactions. In addition we investigated how the sequences of the propeptides affected the substrate-enzyme interaction. To study these questions we employed fluorescently labeled propeptides to measure affinity for the carboxylase. We also measured the ability of several propeptides to increase carboxylase catalytic activity. Finally we determined the effect of substrates: vitamin K hydroquinone, the pentapeptide FLEEL, and NaHCO(3), on the stability of the propeptide-carboxylase complexes. We found a wide variation in the propeptide affinities for carboxylase. In contrast, the propeptides tested had similar effects on carboxylase catalytic activity. FLEEL and vitamin K hydroquinone both stabilized the propeptide-carboxylase complex. The two together had a greater effect than either alone. We conclude that the effect of propeptide and substrates on carboxylase controls the order of substrate binding in such a way as to ensure efficient, specific carboxylation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.