Enzymes
UniProtKB help_outline | 3 proteins |
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- Name help_outline β-D-glucosyl-(1→3)-O-chenodeoxycholate Identifier CHEBI:142610 Charge -1 Formula C30H49O9 InChIKeyhelp_outline QRLIJDGVRXVHQD-UVMPBBQUSA-M SMILEShelp_outline C1[C@@]2([C@]3(CC[C@]4([C@]([C@@]3([C@@H](C[C@@]2(C[C@@H](C1)O[C@H]5[C@@H]([C@H]([C@@H]([C@H](O5)CO)O)O)O)[H])O)[H])(CC[C@@]4([C@@H](CCC([O-])=O)C)[H])[H])C)[H])C 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline chenodeoxycholate Identifier CHEBI:36234 (Beilstein: 3703074) help_outline Charge -1 Formula C24H39O4 InChIKeyhelp_outline RUDATBOHQWOJDD-BSWAIDMHSA-M SMILEShelp_outline [H][C@@]12C[C@H](O)CC[C@]1(C)[C@@]1([H])CC[C@]3(C)[C@]([H])(CC[C@@]3([H])[C@]1([H])[C@H](O)C2)[C@H](C)CCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-glucose Identifier CHEBI:4167 (Beilstein: 1281604; CAS: 2280-44-6) help_outline Charge 0 Formula C6H12O6 InChIKeyhelp_outline WQZGKKKJIJFFOK-GASJEMHNSA-N SMILEShelp_outline OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 152 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:58340 | RHEA:58341 | RHEA:58342 | RHEA:58343 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
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Publications
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Purification and characterization of a microsomal bile acid beta-glucosidase from human liver.
Matern H., Heinemann H., Legler G., Matern S.
A human liver microsomal beta-glucosidase has been purified to apparent homogeneity in sodium dodecyl sulfate-polyacrylamide gel electrophoresis where a single protein band of Mr 100,000 was obtained under reducing conditions. The enzyme was enriched about 73, 000-fold over starting microsomal mem ... >> More
A human liver microsomal beta-glucosidase has been purified to apparent homogeneity in sodium dodecyl sulfate-polyacrylamide gel electrophoresis where a single protein band of Mr 100,000 was obtained under reducing conditions. The enzyme was enriched about 73, 000-fold over starting microsomal membranes by polyethylene glycol fractionation, anion exchange chromatographies on DEAE-Trisacryl, and Mono Q followed by affinity chromatography on N-(9-carboxynonyl)-1-deoxynojirimycin-AH-Sepharose 4B. The purified enzyme had a pH optimum between 5.0 and 6.4, was activated by divalent metal ions, and required phospholipids for exhibition of activity. The enzyme catalyzed the hydrolysis of 3beta-D-glucosido-lithocholic and 3beta-D-glucosido-chenodeoxycholic acids with high affinity (Km, 1.7 and 6.2 microM, respectively) and of the beta-D-glucoside (Km, 210 microM) and the beta-D-galactoside of 4-methylumbelliferone. The ratio of relative reaction rates for these substrates was about 6:3:11:1. No activity was detectable toward 6beta-D-glucosido-hyodeoxycholic acid, glucocerebroside, and the following glycosides of 4-methylumbelliferone: alpha-D-glucoside, alpha-L-arabinoside, beta-D-fucoside or beta-D-xyloside. Immunoinhibition and immunoprecipitation studies using antibodies prepared against lysosomal glucocerebrosidase showed no cross-reactivity with microsomal beta-glucosidase suggesting that these two enzymes are antigenically unrelated. << Less
J. Biol. Chem. 272:11261-11267(1997) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.