Literature DB >> 9198223

Characterization of the gamma-glutamyl carboxylase.

S M Wu1, T B Stanley, V P Mutucumarana, D W Stafford.   

Abstract

Studies on the vitamin K-dependent carboxylase are still in their infancy, but the cloning and purification of the enzyme have permitted a number of advances in our understanding of both the molecular biology, and mechanism of the carboxylase. Advances in our knowledge of the molecular biology of the carboxylase include chromosomal location, characterization of messenger RNA transcript(s) and the study of patients with carboxylase mutations. Our understanding of the mechanism of the carboxylase has been enhanced by the expression of peptides in E. coli which contain multiple carboxylation sites and more closely resemble the native carboxylase substrates. These peptides have been utilized to identify elements within the substrates which are critical for carboxylation and to demonstrate that the vitamin K-dependent carboxylase is one of the first examples of a processive post-translational modification enzyme.

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Year:  1997        PMID: 9198223

Source DB:  PubMed          Journal:  Thromb Haemost        ISSN: 0340-6245            Impact factor:   5.249


  1 in total

1.  Vitamin K2 suppresses rotenone-induced microglial activation in vitro.

Authors:  Yan-Xia Yu; Yi-Pei Li; Feng Gao; Qing-Song Hu; Yan Zhang; Dong Chen; Guang-Hui Wang
Journal:  Acta Pharmacol Sin       Date:  2016-08-08       Impact factor: 6.150

  1 in total

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