Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle.

Journal of theoretical biology - 21 Jun 2011

Wu Sangwook, Liu Shubin, Davis Charles H, Stafford Darrel W, Kulman John D, Pedersen Lee G

Abstract excerpt

Vitamin K carboxylase (VKC) is believed to convert vitamin K, in the vitamin K cycle, to an alkoxide-epoxide form which then reacts with CO(2) and glutamate to generate γ-carboxyglutamic acid (Gla). Subsequently, vitamin K epoxide reductase (VKOR) is thought to convert the alkoxide-epoxide to a hydroquinone form. By recycling vitamin K, the two integral-membrane proteins, VKC and VKOR, maintain vitamin K levels...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Carbon-Carbon Ligases
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to NAD(P)H Dehydrogenase (Quinone)

Share to Protein Multimerization

Share to Protein Structure, Secondary

Share to Quantum Theory

Share to Vitamin K

Share to Warfarin

Source

Open in PubMed Open full text

Identifiers

PMID: 21453708
DOI: 10.1016/j.jtbi.2011.03.030
PMCID: PMC3108363

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle.PMID 21453708Read ↗

Structural and functional insights into enzymes of the vitamin K cycle.Semantic proximity Read ↗

The vitamin K cycle.Semantic proximity Read ↗

VKORC1 and the vitamin K cycle.Semantic proximity Read ↗

Key Pathways and Regulators of Vitamin K Function and Intermediary Metabolism.Semantic proximity Read ↗

The catalytic mechanism of vitamin K epoxide reduction in a cellular environment.Semantic proximity Read ↗

Insight into the coupling mechanism of the vitamin K-dependent carboxylase: mutation of histidine 160 disrupts glutamic acid carbanion formation and efficient coupling of vitamin K epoxidation to glutamic acid carboxylation.Semantic proximity Read ↗

Structural and Functional Insights into GGCX-FIX Interaction: Implications for Vitamin K-Dependent Bleeding DisordersSemantic proximity Read ↗

Cellular and biochemical approaches to define GGCX carboxylation of vitamin K-dependent proteins.Semantic proximity Read ↗

The vitamin K oxidoreductase VKORC1L1 prevents oxidative stress in hepatocytes and protects from MASLD and hepatocellular carcinomaSemantic proximity Read ↗

Molecular basis of vitamin K-dependent protein γ-glutamyl carboxylationSemantic proximity Read ↗

Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer.Semantic proximity Read ↗

Engineering of a recombinant vitamin K-dependent gamma-carboxylation system with enhanced gamma-carboxyglutamic acid forming capacity: evidence for a functional CXXC redox center in the system.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.