Literature DB >> 2354204

Vitamin K-dependent carboxylase: structural requirements for propeptide activation.

A Cheung1, J W Suttie, M Bernatowicz.   

Abstract

The activity of the rat liver vitamin K-dependent gamma-glutamyl carboxylase has been shown to be stimulated by the presence of the free amino terminal 'propeptide' region of the primary gene product of its normal protein substrates. A series of analogs of the human factor X propeptide have been utilized to demonstrate the structure/function relationships important in these interactions.

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Year:  1990        PMID： 2354204     DOI： 10.1016/0167-4838(90)90230-d

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  3 in total

1.  Substrate recognition by the vitamin K-dependent gamma-glutamyl carboxylase: identification of a sequence homology between the carboxylase and the carboxylase recognition site in the substrate.

Authors:  P A Price; M K Williamson
Journal:  Protein Sci       Date:  1993-11       Impact factor: 6.725

2.  Effect of vitamin K-dependent protein precursor propeptide, vitamin K hydroquinone, and glutamate substrate binding on the structure and function of {gamma}-glutamyl carboxylase.

Authors:  Shannon L Higgins-Gruber; Vasantha P Mutucumarana; Pen-Jen Lin; James W Jorgenson; Darrel W Stafford; David L Straight
Journal:  J Biol Chem       Date:  2010-08-17       Impact factor: 5.157

3.  A mutation in the propeptide of Factor IX leads to warfarin sensitivity by a novel mechanism.

Authors:  K Chu; S M Wu; T Stanley; D W Stafford; K A High
Journal:  J Clin Invest       Date:  1996-10-01       Impact factor: 14.808
  3 in total

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