Literature summary for 3.2.1.123 extracted from

Ben Bdira, F.; Jiang, J.; Kallemeijn, W.; de Haan, A.; Florea, B.I.; Bleijlevens, B.; Boot, R.; Overkleeft, H.S.; Aerts, J.M.; Ubbink, M.
Hydrophobic interactions contribute to conformational stabilization of endoglycoceramidase II by mechanism-based probes (2016), Biochemistry, 55, 4823-4835 .

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General Stability

General Stability	Organism
the stability of EGCII is markedly enhanced by formation of covalent complexes with cyclophellitol activity-based probes substituted with hydrophobic moieties, as evidenced by an increased melting temperature, resistance against tryptic digestion, changes in 15N-1H transverse relaxation optimized spectroscopy spectra of the [15N]Leu-labeled enzyme, and relative hydrophobicity as determined by 8-anilino-1-naphthalenesulfonic acid fluorescence. The stabilization of EGCII conformation correlates with the shape and hydrophobicity of the substituents of the activity-based probes	Rhodococcus sp.

Organism

the stability of EGCII is markedly enhanced by formation of covalent complexes with cyclophellitol activity-based probes substituted with hydrophobic moieties, as evidenced by an increased melting temperature, resistance against tryptic digestion, changes in 15N-1H transverse relaxation optimized spectroscopy spectra of the [15N]Leu-labeled enzyme, and relative hydrophobicity as determined by 8-anilino-1-naphthalenesulfonic acid fluorescence. The stabilization of EGCII conformation correlates with the shape and hydrophobicity of the substituents of the activity-based probes

Rhodococcus sp.

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	beta-glucoside-configured cyclophellitol-type activity-based probes are effective mechanism-based, and irreversible inhibitors	Rhodococcus sp.

Organism

Organism	UniProt	Comment	Textmining
Rhodococcus sp.	O33853	-	-

Synonyms

Synonyms	Comment	Organism
EGCII	-	Rhodococcus sp.
endoglycoceramidase II	-	Rhodococcus sp.

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Release 2023.1 (January 2023)