Enzymes
| UniProtKB help_outline | 2 proteins |
| Enzyme class help_outline |
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- Name help_outline all-trans-zeaxanthin Identifier CHEBI:27547 (Beilstein: 2068416; CAS: 144-68-3) help_outline Charge 0 Formula C40H56O2 InChIKeyhelp_outline JKQXZKUSFCKOGQ-QAYBQHTQSA-N SMILEShelp_outline CC(\C=C\C=C(C)\C=C\C1=C(C)C[C@@H](O)CC1(C)C)=C/C=C/C=C(C)/C=C/C=C(C)/C=C/C1=C(C)C[C@@H](O)CC1(C)C 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP-α-D-glucose Identifier CHEBI:58885 (Beilstein: 3827329) help_outline Charge -2 Formula C15H22N2O17P2 InChIKeyhelp_outline HSCJRCZFDFQWRP-JZMIEXBBSA-L SMILEShelp_outline OC[C@H]1O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2ccc(=O)[nH]c2=O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 231 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline zeaxanthin bis(β-D-glucoside) Identifier CHEBI:63067 Charge 0 Formula C52H76O12 InChIKeyhelp_outline DHNSFMNURMJEQV-OIBMWOCGSA-N SMILEShelp_outline CC(\C=C\C=C(C)\C=C\C1=C(C)C[C@H](CC1(C)C)O[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O)=C/C=C/C=C(C)/C=C/C=C(C)/C=C/C1=C(C)C[C@H](CC1(C)C)O[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O 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 UDP Identifier CHEBI:58223 Charge -3 Formula C9H11N2O12P2 InChIKeyhelp_outline XCCTYIAWTASOJW-XVFCMESISA-K SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 577 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:31543 | RHEA:31544 | RHEA:31545 | RHEA:31546 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Functional expression of zeaxanthin glucosyltransferase from Erwinia herbicola and a proposed uridine diphosphate binding site.
Hundle B.S., O'Brien D.A., Alberti M., Beyer P., Hearst J.E.
Erwinia herbicola, a nonphotosynthetic bacterium, is yellow colored due to the accumulation of unusually polar carotenoids, primarily mono- and diglucosides of zeaxanthin. We have cloned and expressed the gene for the enzyme that catalyzes the glucosylation of zeaxanthin. The enzyme has an apparen ... >> More
Erwinia herbicola, a nonphotosynthetic bacterium, is yellow colored due to the accumulation of unusually polar carotenoids, primarily mono- and diglucosides of zeaxanthin. We have cloned and expressed the gene for the enzyme that catalyzes the glucosylation of zeaxanthin. The enzyme has an apparent molecular mass of 45 kDa on an SDS/polyacrylamide gel, which is consistent with its calculated molecular mass. In vitro enzymatic activity was demonstrated using UDP-[14C]glucose and zeaxanthin as substrates. The product zeaxanthin diglucoside and its intermediate monoglucoside were identified by thin layer chromatography. The optimum pH and temperature ranges of the enzyme are 7.0-7.5 and 32-37 degrees C, respectively. A hydropathy plot indicates no apparent membrane-spanning regions, and biochemical experiments suggest that the enzyme is weakly membrane-associated. The amino acid sequence derived from the zeaxanthin glucosyltransferase gene shows a small region of high similarity with other glucuronosyl- and glucosyltransferases that use either UDP-activated glucuronic acid or a sugar as one of their substrates. Based on these similarities, we propose that this conserved sequence is part of the UDP binding site. << Less
Proc. Natl. Acad. Sci. U.S.A. 89:9321-9325(1992) [PubMed] [EuropePMC]