VKOR carboxylation activity

Carboxylation activity of VKOR variants by substrate surface expression.

urn:mavedb:00000078-a

Created Oct. 2, 2021
Last updated Oct. 2, 2021
Published Oct. 2, 2021
Member of urn:mavedb:00000078

Score sets

urn:mavedb:00000078-a-1

Abstract

Untitled

This study tested the carboxylation activity change of vitamin K epoxide reductase (VKOR) variants. The functioning VKOR is able to carboxylate Factor IX domain which is secreted and retained on the cell surface. By culturing the cells with fluorophore-labeled carboxylation-specific antibody, the impact of VKOR variants to its carboxylation activity can be determined by FACS.

Method

Untitled

The variant library is generated by mutagenesis primers through PCR which contains 697 missense mutations. The cell line is binded with a fluorophore-labeled carboxylation-specific antibody and sorted into quartile bins according to the APC fluorescent intensity by FACS. Each bin is deeply sequenced and the final abundance scores are calculated.

References

  • Chiasson MA, et al. Multiplexed measurement of variant abundance and activity reveals VKOR topology, active site and human variant impact. Elife. 2020; 9:None. PMID: 32870157

Contributors

Keywords

No keywords are associated with this entry.

Targets

Name: VKOR

Type: Protein coding

Organism: Homo sapiens

Reference genome: hg38

Reference assembly: Other/Synthetic

Reference sequence: MGSTWGSPGWVRLALCLTGLVLSLYALHVKAARARDRDYRALCDVGTAISCSRVFSSRWGRGFGLVEHVLGQDSILNQSNSIFGCIFYTLQLLLGCLRTRWASVLMLLSSLVSLAGSVYLAWILFFVLYDFCIVCITTYAINVSLMWLSFRKVQEPQGKAKRH

External identifiers

DOI: No associated DOIs

Raw reads:

Score sets

  • urn:mavedb:00000078-a-1

    VKOR carboxylation activity

    Carboxylation activity of VKOR variants by substrate surface expression.