Enzymes
| UniProtKB help_outline | 3 proteins |
| Enzyme class help_outline |
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- 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 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline presqualene diphosphate Identifier CHEBI:57310 Charge -3 Formula C30H49O7P2 InChIKeyhelp_outline ATZKAUGGNMSCCY-VYCBRMPGSA-K SMILEShelp_outline CC(C)=CCC\C(C)=C\CC\C(C)=C\[C@H]1[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@]1(C)CC\C=C(/C)CCC=C(C)C 2D coordinates Mol file for the small molecule Search links Involved in 7 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 1,129 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline hydroxysqualene Identifier CHEBI:88123 Charge 0 Formula C30H50O InChIKeyhelp_outline IBTBZLYRNUPSAW-HWKIJRFISA-N SMILEShelp_outline C(/C=C(/CC/C=C(/CCC=C(C)C)\C)\C)[C@H](/C=C(/CC/C=C(/CCC=C(C)C)\C)\C)O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:47984 | RHEA:47985 | RHEA:47986 | RHEA:47987 | |
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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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Biosynthesis of squalene from farnesyl diphosphate in bacteria: three steps catalyzed by three enzymes.
Pan J.J., Solbiati J.O., Ramamoorthy G., Hillerich B.S., Seidel R.D., Cronan J.E., Almo S.C., Poulter C.D.
Squalene (SQ) is an intermediate in the biosynthesis of sterols in eukaryotes and a few bacteria and of hopanoids in bacteria where they promote membrane stability and the formation of lipid rafts in their hosts. The genes for hopanoid biosynthesis are typically located on clusters that consist of ... >> More
Squalene (SQ) is an intermediate in the biosynthesis of sterols in eukaryotes and a few bacteria and of hopanoids in bacteria where they promote membrane stability and the formation of lipid rafts in their hosts. The genes for hopanoid biosynthesis are typically located on clusters that consist of four highly conserved genes-<i>hpnC</i>, <i>hpnD</i>, <i>hpnE</i>, and <i>hpnF</i>-for conversion of farnesyl diphosphate (FPP) to hopene or related pentacyclic metabolites. While <i>hpnF</i> is known to encode a squalene cyclase, the functions for <i>hpnC</i>, <i>hpnD</i>, and <i>hpnE</i> are not rigorously established. The <i>hpnC</i>, <i>hpnD</i>, and <i>hpnE</i> genes from <i>Zymomonas mobilis</i> and <i>Rhodopseudomonas palustris</i> were cloned into <i>Escherichia coli</i>, a bacterium that does not contain genes homologous to <i>hpnC</i>, <i>hpnD</i>, and <i>hpnE</i>, and their functions were established <i>in vitro</i> and <i>in vivo</i>. HpnD catalyzes formation of presqualene diphosphate (PSPP) from two molecules of FPP; HpnC converts PSPP to hydroxysqualene (HSQ); and HpnE, a member of the amine oxidoreductase family, reduces HSQ to SQ. Collectively the reactions catalyzed by these three enzymes constitute a new pathway for biosynthesis of SQ in bacteria. << Less
ACS Cent. Sci. 1:77-82(2015) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.