3.2.1.123: endoglycosylceramidase

This is an abbreviated version!
For detailed information about endoglycosylceramidase, go to the full flat file.

Reaction

Synonyms

ceramidase, endoglycosyl-, ceramide glycanase, EGALC, EGC, EGCase, EGCase I, EGCase II, EGCase III, EGCII, EGCrP1, EGCrP2, endo-glycoceramidase II, endogalactosylceramidase, endoglycoceramidase, endoglycoceramidase I, endoglycoceramidase II, endoglycoceramidase-related protein, glycosyl-N-acetyl-sphingosine 1,1-beta-D-glucanohydrolase, oligogalactosyl-N-acylsphingosine 1,1'-beta-galactohydrolase

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.123 endoglycosylceramidase

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Results	in table
28	Activating Compound
62	AA Sequence
6	Application
1	CAS Registry Number
14	Cloned(Commentary)
3	Crystallization (Commentary)
5	General Stability
32	Inhibitors
11	kcat/KM [mM/s]
3	Ki Value [mM]
27	KM Value [mM]
6	Localization
5	Metals/Ions
16	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
66	Organism
1	Oxidation Stability
11	PDB ID
25	pH Optimum
3	pH Range
4	pH Stability
6	pI Value
1	Posttranslational Modification
39	Protein Variants
16	Purification (Commentary)
1	Reaction
3	Reaction Type
56	Reference
13	Source Tissue
24	Specific Activity [micromol/min/mg]
3	Storage Stability
239	Substrates and Products (Substrate)
12	Subunits
75	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
1	Temperature Range [°C]
4	Temperature Stability [°C]
14	Turnover Number [1/s]

General Stability

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General Stability on EC 3.2.1.123 - endoglycosylceramidase

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

highly purified ECGase II loses activity due to instability following purification

Rhodococcus sp.

-

646690

stable to repeated freezing and thawing

Corynebacterium sp.

-

646688

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.

O33853

749905

unstable at protein concentration below 0.2 mg/ml or without Triton X-100

Rhodococcus sp.

-

646691

unstable to repeated freezing and thawing

Rhodococcus sp.

-

646691