![Figure 1 from Propeptide and glutamate-containing substrates bound to the vitamin K-dependent carboxylase convert its vitamin K epoxidase function from an inactive to an active state. | Semantic Scholar Figure 1 from Propeptide and glutamate-containing substrates bound to the vitamin K-dependent carboxylase convert its vitamin K epoxidase function from an inactive to an active state. | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/efde951f4e84d37307f7631384d949d8ec11038b/2-Figure1-1.png)
Figure 1 from Propeptide and glutamate-containing substrates bound to the vitamin K-dependent carboxylase convert its vitamin K epoxidase function from an inactive to an active state. | Semantic Scholar
![In the vitamin K cycle, vitamin K-dependent gamma-carboxyglutamic acid... | Download Scientific Diagram In the vitamin K cycle, vitamin K-dependent gamma-carboxyglutamic acid... | Download Scientific Diagram](https://www.researchgate.net/profile/Michael-Holick/publication/276159848/figure/fig1/AS:616371763281924@1523965888887/In-the-vitamin-K-cycle-vitamin-K-dependent-gamma-carboxyglutamic-acid-Gla-proteins-are_Q640.jpg)
In the vitamin K cycle, vitamin K-dependent gamma-carboxyglutamic acid... | Download Scientific Diagram
Nutriab - The vitamin K cycle. Vitamin K acts as a coenzyme. The enzyme involved in this reaction is Gamma-Glutamyl-CarboXylase (GGCX) (a). The catalyzed reaction is the carboxylation of glutamic acid residues (
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N-Fmoc-γ-carboxyglutamic Acid γ,γ-Di-t-butyl Ester | CAS 308357-14-4 | SCBT - Santa Cruz Biotechnology
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