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Function of your protein
MqnA is a chorismate dehydratase that has been studied in Streptomyces coelicolor. MqnA is important because it catalyzes the initial step in the biosynthesis of menaquinone via the futalosine pathway. MqnA folds like a venus flytrap and binds to called chorismate. Without the venus flytrap folding, the protein would be unable to access the binding site. Products of ScMqnA include 3-EPB and the presumed hydrolysis product, 3,4-dihydroxycyclohexa-1,5-dienoate (3,4-CHD).
dienoate (3,4-CHD),
Biological relevance and broader implications
MqnA is important because it catalyzes the biosynthesis of menaquinone, which is an important player in the electron transport chain. According to Prasad et al. (2022), "Menaquinone serves as an electron carrier in the electron transport chain. Although some prokaryotes utilize ubiquinone solely, mycobacteria and most gram-positive bacteria produce menaquinone exclusively, and many gram-negative bacteria such as Escherichia coli switch from ubiquinone to menaquinone when grown under anaerobic conditions (2). In humans, menaquinone (vitamin K2) acts as a cosubstrate in the carboxylation of glutamic acids that leads to the activation of proteins essential for blood coagulation, control of cell growth, apoptosis, signal transduction, and calcium metabolism."
Important amino acids
Amino acids involved in the catalytic triad for MqnA include N17, S86, and Y242. Other amino acids that are important include
Structural highlights
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