Enzymes
| UniProtKB help_outline | 3 proteins |
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- 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 octyl β-D-glucose Identifier CHEBI:41128 (CAS: 29836-26-8) help_outline Charge 0 Formula C14H28O6 InChIKeyhelp_outline HEGSGKPQLMEBJL-RKQHYHRCSA-N SMILEShelp_outline O1[C@@H]([C@H]([C@@H]([C@H]([C@@H]1OCCCCCCCC)O)O)O)CO 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- 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 octan-1-ol Identifier CHEBI:16188 (Beilstein: 1697461; CAS: 111-87-5) help_outline Charge 0 Formula C8H18O InChIKeyhelp_outline KBPLFHHGFOOTCA-UHFFFAOYSA-N SMILEShelp_outline CCCCCCCCO 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:59108 | RHEA:59109 | RHEA:59110 | RHEA:59111 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Formation of bile acid glucosides by a sugar nucleotide-independent glucosyltransferase isolated from human liver microsomes.
Matern H., Matern S., Gerok W.
A heat-labile protein has been detected in microsomes from human liver which catalyzes the formation of glucosides of the bile acids chenodeoxycholic, deoxycholic, and ursodeoxycholic acids. This glucosyltransferase activity has been purified about 900-fold from human liver microsomes, resulting i ... >> More
A heat-labile protein has been detected in microsomes from human liver which catalyzes the formation of glucosides of the bile acids chenodeoxycholic, deoxycholic, and ursodeoxycholic acids. This glucosyltransferase activity has been purified about 900-fold from human liver microsomes, resulting in homogeneity as determined by sodium dodecyl sulfate gel electrophoresis. The subunit molecular weight was calculated to be about 56,000. The enzyme was separated from bile acid UDP-glucuronosyltransferase [UDP-glucuronate beta-D-glucuronosyltransferase (acceptor-unspecific), EC 2.4.1.17] during purification and does not catalyze the formation of bile acid glucuronides. The purified glucosyltransferase utilizes lipophilic alkyl beta-D-glucopyranosides as artificial donor substrates and dolichyl phosphoglucose as natural donor for the transfer of glucose to bile acids and does not exhibit bile acid conjugating activity in the presence of sugar nucleotides such as UDP-glucose. The apparent Km values estimated for various alkyl beta-D-glucopyranosides decreased with increasing alkyl chain length from 680 X 10(-6) M for hexyl beta-D-glucopyranoside to 20 X 10(-6) M as estimated for decyl and dodecyl beta-D-glucopyranoside. The results suggest that a glucoside-conjugation pathway of bile acids exists in humans. This conjugation is catalyzed by a sugar nucleotide-independent glucosyltransferase and is therefore distinct from the known mechanisms of glycoside conjugation. << Less
Proc Natl Acad Sci U S A 81:7036-7040(1984) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Mutation of beta-glucosidase 2 causes glycolipid storage disease and impaired male fertility.
Yildiz Y., Matern H., Thompson B., Allegood J.C., Warren R.L., Ramirez D.M.O., Hammer R.E., Hamra F.K., Matern S., Russell D.W.
beta-Glucosidase 2 (GBA2) is a resident enzyme of the endoplasmic reticulum thought to play a role in the metabolism of bile acid-glucose conjugates. To gain insight into the biological function of this enzyme and its substrates, we generated mice deficient in GBA2 and found that these animals had ... >> More
beta-Glucosidase 2 (GBA2) is a resident enzyme of the endoplasmic reticulum thought to play a role in the metabolism of bile acid-glucose conjugates. To gain insight into the biological function of this enzyme and its substrates, we generated mice deficient in GBA2 and found that these animals had normal bile acid metabolism. Knockout males exhibited impaired fertility. Microscopic examination of sperm revealed large round heads (globozoospermia), abnormal acrosomes, and defective mobility. Glycolipids, identified as glucosylceramides by mass spectrometry, accumulated in the testes, brains, and livers of the knockout mice but did not cause obvious neurological symptoms, organomegaly, or a reduction in lifespan. Recombinant GBA2 hydrolyzed glucosylceramide to glucose and ceramide; the same reaction catalyzed by the beta-glucosidase acid 1 (GBA1) defective in subjects with the Gaucher's form of lysosomal storage disease. We conclude that GBA2 is a glucosylceramidase whose loss causes accumulation of glycolipids and an endoplasmic reticulum storage disease. << Less
J. Clin. Invest. 116:2985-2994(2006) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.