Prephenate decarboxylase
Definition:
EC Tree > 4 Lyases > 4.1 Carbon-carbon lyases > 4.1.1 Carboxy-lyases > 4.1.1.100 prephenate decarboxylase
Prephenate decarboxylase is characterized from Bacillus subtilis and participates in biosynthesis of bacilysin, the nonribosomal dipeptide antibiotic composed of L-alanine and L-anticapsin; it isomerizes only the pro-R double bond of prephenate. It decarboxylates prephenate into 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate and CO2. In bacilysin biosynthesis it feeds anticapsin. It features a prephenate decarboxylase fold.
Prephenate decarboxylase is characterized from Bacillus subtilis and participates in biosynthesis of bacilysin, the nonribosomal dipeptide antibiotic composed of L-alanine and L-anticapsin; it isomerizes only the pro-R double bond of prephenate. It decarboxylates prephenate into 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate and CO2. In bacilysin biosynthesis it feeds anticapsin. It features a prephenate decarboxylase fold.
References:
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