Enzymes
UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
- Name help_outline (2E)-geranyl diphosphate Identifier CHEBI:58057 (Beilstein: 4549979) help_outline Charge -3 Formula C10H17O7P2 InChIKeyhelp_outline GVVPGTZRZFNKDS-JXMROGBWSA-K SMILEShelp_outline CC(C)=CCC\C(C)=C\COP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 59 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
-
Namehelp_outline
L-tryptophyl-[protein]
Identifier
RHEA-COMP:15365
Reactive part
help_outline
- Name help_outline L-tryptophan residue Identifier CHEBI:29954 Charge 0 Formula C11H10N2O SMILEShelp_outline C1(=CNC2=C1C=CC=C2)C[C@@H](C(=O)*)N* 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
-
Namehelp_outline
(2S,3R)-3-geranyl-2,3-dihydro-2,Nα-cyclo-L-tryptophyl-[protein]
Identifier
RHEA-COMP:15366
Reactive part
help_outline
- Name help_outline (2S,3R)-3-geranyl-2,3-dihydro-2,Nα-cyclo-L-tryptophan residue Identifier CHEBI:141127 Charge 0 Formula C21H26N2O SMILEShelp_outline C1=2N[C@]3([C@@](C1=CC=CC2)(C[C@@H](C(=O)*)N3*)C/C=C(/CCC=C(C)C)\C)[H] 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 diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,085 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:59492 | RHEA:59493 | RHEA:59494 | RHEA:59495 | |
---|---|---|---|---|
Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
|
Publications
-
Geranyl modification on the tryptophan residue of ComXRO-E-2 pheromone by a cell-free system.
Tsuji F., Ishihara A., Kurata K., Nakagawa A., Okada M., Kitamura S., Kanamaru K., Masuda Y., Murakami K., Irie K., Sakagami Y.
ComX pheromone is an isoprenoidal oligopeptide containing a modified tryptophan residue, which stimulates natural genetic competence in the gram-positive bacterium Bacillus. Since posttranslational prenylation on the tryptophan residue has not been reported except in ComX pheromone, the universali ... >> More
ComX pheromone is an isoprenoidal oligopeptide containing a modified tryptophan residue, which stimulates natural genetic competence in the gram-positive bacterium Bacillus. Since posttranslational prenylation on the tryptophan residue has not been reported except in ComX pheromone, the universality of this modification has not yet been elucidated. In this paper, we established a cell-free system, whereby the tryptophan residue in peptides is modified with a geranyl group by modifying enzyme ComQ. In addition, we investigated enzymatic reaction conditions using an in vitro enzyme reaction system. This is the first report of in vitro geranylation on the tryptophan residue. This system is potentially a useful tool for elucidating the universality of prenylation on the tryptophan residue. << Less
-
Identification of critical residues for the catalytic activity of ComQ, a Bacillus prenylation enzyme for quorum sensing, by using a simple bioassay system.
Hirooka K., Shioda S., Okada M.
<i>Bacillus</i> ComQ participates in the biosynthesis of a quorum-sensing signaling molecule (ComX pheromone) through catalyzing the prenylation at a Trp residue of the precursor peptide (pre-ComX) with geranyl diphosphate (C<sub>10</sub> type) or farnesyl diphosphate (C<sub>15</sub> type). We hyp ... >> More
<i>Bacillus</i> ComQ participates in the biosynthesis of a quorum-sensing signaling molecule (ComX pheromone) through catalyzing the prenylation at a Trp residue of the precursor peptide (pre-ComX) with geranyl diphosphate (C<sub>10</sub> type) or farnesyl diphosphate (C<sub>15</sub> type). We hypothesized that several residues specifically conserved among either type of ComQs are important for their substrate specificities. Using a simple bioassay, we revealed that Phe63, Asn186, and Gly190 in ComQ<sub>RO-E-2</sub> (C<sub>10</sub> type) were nondisplaceable to Ser63, Gly186, and Val190, the corresponding residues in the C<sub>15</sub>-type ComQ, respectively. A three-dimensional model suggested that the 186th and 190th residues are involved in the pre-ComX binding. <i>In vitro</i> analysis showed that substitution of Phe63 with Ser in ComQ<sub>RO-E-2</sub> significantly reduced the geranylation activity but substantially enhanced the farnesylation activity, whereas substitution of Ser63 with Phe in ComQ<sub>168</sub> (C<sub>15</sub> type) reduced the farnesylation activity. Therefore, the 63rd residue was found to be significant for the prenyl-substrate preference.<b>Abbreviations:</b> GPP: geranyl diphosphate; FPP: farnesyl diphosphate; IPP: isopentenyl diphosphate; GGPP: geranylgeranyl diphosphate; FARM: first aspartate-rich motif; SARM: second aspartate-rich motif; β-Gal: β-galactosidase; TBABG: tryptose blood agar base supplemented with glucose; X-gal: 5-bromo-4-chloro-3-indolyl-β-D-galactoside. << Less
Biosci. Biotechnol. Biochem. 84:347-357(2020) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.