BRENDA - Enzyme Database
show all sequences of 3.2.1.123

Hydrophobic interactions contribute to conformational stabilization of endoglycoceramidase II by mechanism-based probes

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.; Biochemistry 55, 4823-4835 (2016)

Data extracted from this reference:

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.
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
beta-glucoside-configured cyclophellitol-type activity-based probes are effective mechanism-based, and irreversible inhibitors
Rhodococcus sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodococcus sp.
O33853
-
-
General Stability (protein specific)
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.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
beta-glucoside-configured cyclophellitol-type activity-based probes are effective mechanism-based, and irreversible inhibitors
Rhodococcus sp.
Other publictions for EC 3.2.1.123
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
750248
Shen
Mass spectrometry-based ident ...
Rhodococcus sp. M-777
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476
53-59
2019
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751102
Han
Structural insights into the ...
Rhodococcus hoagii 103S, Rhodococcus hoagii, Rhodococcus sp. M-777
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292
4789-4800
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1
1
12
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2
749565
Albrecht
Comprehensive profiling of gl ...
Rhodococcus triatomea, Rhodococcus triatomea BKS 15-14
Anal. Chem.
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4795-4802
2016
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2
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749905
Ben Bdira
Hydrophobic interactions cont ...
Rhodococcus sp.
Biochemistry
55
4823-4835
2016
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5
5
732295
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1
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4
4
714723
Rich
Glycosphingolipid synthesis em ...
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Chem. Commun. (Camb. )
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2011
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715127
Karlsson
Differentiation of glycosphing ...
Rhodococcus sp.
Glycobiology
20
1103-1116
2010
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Preparation of homogenous olig ...
Rhodococcus sp., Rhodococcus sp. M-750
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26
929-933
2009
1
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699823
Misonou
Comprehensive clinico-glycomic ...
Rhodococcus sp.
J. Proteome Res.
8
2990-3005
2009
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1
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703891
Xu
A novel fucosyl glycosphingoli ...
Rhodococcus sp.
Glycobiology
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1446-1451
2009
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703903
Ishibashi
Transglycosylation-based fluor ...
Rhodococcus hoagii
Glycobiology
19
797-807
2009
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1
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695545
Hancock
High-throughput screening of c ...
Rhodococcus sp.
Anal. Biochem.
382
48-54
2008
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7
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677532
Korekane
Novel fucogangliosides found i ...
Rhodococcus sp.
Anal. Biochem.
364
37-50
2007
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677557
Caines
The structural basis of glycos ...
Rhodococcus sp.
Angew. Chem. Int. Ed. Engl.
46
4474-4476
2007
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680549
Xu
Fucosyl-GM1a, an endoglycocera ...
Sus scrofa
J. Biochem.
141
1-7
2007
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680753
Ishibashi
A novel endoglycoceramidase hy ...
Rhodococcus hoagii
J. Biol. Chem.
282
11386-11396
2007
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680770
Caines
Structural and mechanistic ana ...
Rhodococcus sp.
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282
14300-14308
2007
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2
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665547
Horibata
Unique catabolic pathway of gl ...
Aiptasia sp., Bacillus sp. (in: Bacteria), Cellana sp., Cyanea nozakii, Entacmaea sp., Hydra vulgaris 105, Hydra vulgaris, Marphysa sp., Meretrix sp., Ruditapes sp.
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2004
2
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3
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18
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12
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9
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646694
Horibata
Transglycosylation and reverse ...
Cyanea nozakii
J. Biochem.
130
263-268
2001
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646695
Horibata
Purification, characterization ...
Cyanea nozakii
J. Biol. Chem.
275
31297-31304
2000
3
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646702
Sakaguchi
Cloning and expression of gene ...
Rhodococcus sp., Rhodococcus sp. C9
J. Biochem.
128
145-152
2000
2
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1
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4
3
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19
1
1
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646700
Miura
Requirement for a different hy ...
Corynebacterium sp., Rhodococcus sp.
Glycobiology
9
957-960
1999
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646701
Sakaguchi
The Glu residue in the conserv ...
Rhodococcus sp., Rhodococcus sp. C9
Biochem. Biophys. Res. Commun.
260
89-93
1999
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1
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4
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646697
Ji
Effects of endoglycoceramidase ...
Rhodococcus sp.
Arch. Biochem. Biophys.
359
107-114
1998
1
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646699
Mitsutake
Enzymatic synthesis of 14C-gly ...
Condylactis sp., Rhodococcus sp.
J. Biochem.
123
859-863
1998
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11
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Ji
The hydrolysis of cell surface ...
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Transglycosylation activity of ...
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646693
Ito
Kinetics of endoglycoceramidas ...
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Ashida
Purification and characterizat ...
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1
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1
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Ito
Activator proteins for glycosp ...
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5
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Ito
Conversion of endoglycoceramid ...
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Ito
Purification and characterizat ...
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20
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20
1
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1
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646687
Ito
A novel glycosphingolipid-degr ...
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1
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25
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25
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