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]

Crystallization

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Crystallization on EC 3.2.1.123 - endoglycosylceramidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

hanging drop vapor diffusion method at 20°C, X-ray crystal structures of the enzyme alone and in complex with its substrates monosialodihexosylganglioside and monosialotetrahexosylganglioside determined at 2.11 A resolution. Compared with EGCase II from Rhodococcus sp. M-777, which possesses strict substrate specificity, EGCase I from Rhodococcus hoagii 103S possesses a longer alpha7-helix and a shorter loop 4, which forms a larger substrate-binding pocket that could accommodate more extended oligosaccharides. In addition, loop 2 and loop 8 of the enzyme adopt a more open conformation, which also enlarges the oligosaccharide-binding cavity

Rhodococcus equi

A0A3S5YBC7

751102

by vapor diffusion method, crystals of the native enzyme belong to space group P21 with unit cell dimensions a=53.8 A, b=92.9 Å, c=94.5 A,beta=98.6°, to 1.6 A resolution. Crystal structure of mutant E351S in complex with the ganglioside GM3, crystals belong to space group C2, with unit cell dimensions a = 77.8 A, b = 62.0 A, c = 102.8 A, beta = 112.3°, to 1.1 A resolution. Active site of endo-glycoceramidase is split into a wide, polar cavity to bind the polyhydroxylated oligosaccharide moiety and a narrow, hydrophobic tunnel to bind the ceramide lipid chains

Rhodococcus sp.

-

680770

EGC-inhibitor complexes, to 1.50-1.85 A resolution. Both (3R,4R,5R)-4-(beta-D-glucopyranosyl)oxy-3-hydroxy-5-(hydroxymethyl)piperidine and (5R,6R,7S,8S)-6-(beta-D-glucopyranosyloxy)-5,6,7,8-tetrahydro-5-(hydroxymethyl)imidazo-[1,2-a]pyridine-7,8-diol bind in the -2 and -1 subsites of the enzyme, with the isofagomine and glucoimidazole moieties located in the catalytic -1 subsite. 1-(4-dimethylamino)benzoylamino-1,2,5-trideoxy-2,5-imino-d-mannitol binds in the -1 subsite in an envelope conformation. The ring nitrogen superimposes with the anomeric carbon of the lactosyl-enzyme intermediate and the ring nitrogen of the isofagomine

Rhodococcus sp.

-

677557