Literature summary for 3.2.1.108 extracted from

Jacob, R.; Weiner, J.R.; Stadge, S.; Naim, H.Y.
Additional N-glycosylation and its impact on the folding of intestinal lactase-phlorizin hydrolase (2000), J. Biol. Chem., 275, 10630-10637.

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Protein Variants

Protein Variants	Comment	Organism
D1711N	introduction of potential N-glycosilation site, no enzymic activity, probably due to altered protein folding pattern and reduced dimerization efficiency	Homo sapiens
I1697N	introduction of potential N-glycosilation site, no enzymic activity, probably due to altered protein folding pattern and reduced dimerization efficiency	Homo sapiens
P1743S	introduction of potential N-glycosilation site, no enzymic activity, probably due to altered protein folding pattern and reduced dimerization efficiency	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Subunits

Subunits	Comment	Organism
More	region LAC236 between R1647 and T1882 is implicated in the dimerization process of pro-enzyme	Homo sapiens

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Release 2023.1 (January 2023)