Menaquinone Biosynthesis: Biochemical and Structural Studies of Chorismate Dehydratase. Academic Article

abstract

• Menaquinone (MK, vitamin K) is a lipid-soluble quinone that participates in the bacterial electron transport chain. In mammalian cells, vitamin K functions as an essential vitamin for the activation of several proteins involved in blood clotting and bone metabolism. MqnA is the first enzyme on the futalosine-dependent pathway to menaquinone and catalyzes the aromatization of chorismate by water loss. Here we report biochemical and structural studies of MqnA. These studies suggest that the dehydration reaction proceeds by a variant of the E1cb mechanism in which deprotonation is slower than water loss and that the enol carboxylate of the substrate is serving as the base.

authors

• Begley, Tadhg

published proceedings

• Biochemistry

altmetric score

• 0.5

author list (cited authors)

• Mahanta, N., Hicks, K. A., Naseem, S., Zhang, Y., Fedoseyenko, D., Ealick, S. E., & Begley, T. P.

citation count

• 4

complete list of authors

• Mahanta, Nilkamal||Hicks, Katherine A||Naseem, Saad||Zhang, Yang||Fedoseyenko, Dmytro||Ealick, Steven E||Begley, Tadhg P

publication date

• April 2019

publisher

• American Chemical Society (ACS)  Publisher

published in

• Biochemistry  Journal

keywords

• Bacterial Proteins
• Biosynthetic Pathways
• Deinococcus
• Hydrogen-Ion Concentration
• Models, Chemical
• Molecular Structure
• Molecular Weight
• Oxo-acid-lyases
• Protons
• Vitamin K 2
• Water

PubMed Central ID

• 30855131

Digital Object Identifier (DOI)

• 10.1021/acs.biochem.9b00105

start page

• 1837

end page

• 1840

volume

• 58

issue

• 14

URL

• http://dx.doi.org/10.1021/acs.biochem.9b00105