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Structure and catalytic mechanism of LigI: insight into the amidohydrolase enzymes of cog3618 and lignin degradation.
TLDR
LigI from Sphingomonas paucimobilis catalyzes the reversible hydrolysis of 2-pyrone-4,6-dicarboxylate (PDC) to 4-oxalomesaconate and 4-carboxy-2-hydroxymuconate in the degradation of lignin, the first enzyme from the amidohydrolase superfamily that does not require a divalent metal ion for catalytic activity.
Discovery of an L-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily.
TLDR
BmulJ_04915 is the first enzyme that has been shown to catalyze the hydrolysis of either L-fucono-1,4-lactone or L-fucose dehydrogenase, and is the second enzyme from cog3618 of the amidohydrolase superfamily that does not require a divalent metal for catalytic activity.
l-Galactose Metabolism in Bacteroides vulgatus from the Human Gut Microbiota
TLDR
A previously unknown metabolic pathway for the utilization of l-galactose was discovered in a prevalent gut bacterium, Bacteroides vulgatus, and is estimated to be hydrolyzed 300-fold faster than its thermodynamically more stable counterpart, l-Galactono-1,4-lactone.
Galactose Metabolism in Bacteroides vulgatus from the Human Gut Microbiota
A previously unknown metabolic pathway for the utilization of L-galactose was discovered in a prevalent gut bacterium, Bacteroides vulgatus. The new pathway consists of three previously
The Discovery of New Enzymes in the Human Gut Microbiome
TLDR
A previously unknown metabolic pathway for the utilization of L-galactose was discovered in a prevalent human gut bacterium, Bacteroides vulgatus, and it is unclear whether this pathway is related to human gut infection or not.