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- Name help_outline S-methyl-5-thio-D-ribulose 1-phosphate Identifier CHEBI:58548 (Beilstein: 11409869) help_outline Charge -2 Formula C6H11O7PS InChIKeyhelp_outline CNSJRYUMVMWNMC-RITPCOANSA-L SMILEShelp_outline CSC[C@@H](O)[C@@H](O)C(=O)COP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-methyl-1-thiol-D-ribulose 5-phosphate Identifier CHEBI:85606 Charge -2 Formula C6H11O7PS InChIKeyhelp_outline JQZPXWYLEQDBGH-INEUFUBQSA-L SMILEShelp_outline CSCC(=O)[C@H](O)[C@H](O)COP([O-])([O-])=O 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
Cross-references
| RHEA:57580 | RHEA:57581 | RHEA:57582 | RHEA:57583 | |
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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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A RubisCO-like protein links SAM metabolism with isoprenoid biosynthesis.
Erb T.J., Evans B.S., Cho K., Warlick B.P., Sriram J., Wood B.M., Imker H.J., Sweedler J.V., Tabita F.R., Gerlt J.A.
Functional assignment of uncharacterized proteins is a challenge in the era of large-scale genome sequencing. Here, we combine in extracto NMR, proteomics and transcriptomics with a newly developed (knock-out) metabolomics platform to determine a potential physiological role for a ribulose-1,5-bis ... >> More
Functional assignment of uncharacterized proteins is a challenge in the era of large-scale genome sequencing. Here, we combine in extracto NMR, proteomics and transcriptomics with a newly developed (knock-out) metabolomics platform to determine a potential physiological role for a ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein from Rhodospirillum rubrum. Our studies unraveled an unexpected link in bacterial central carbon metabolism between S-adenosylmethionine-dependent polyamine metabolism and isoprenoid biosynthesis and also provide an alternative approach to assign enzyme function at the organismic level. << Less
Nat. Chem. Biol. 8:926-932(2012) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.
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Mechanistic diversity in the RuBisCO superfamily: a novel isomerization reaction catalyzed by the RuBisCO-like protein from Rhodospirillum rubrum.
Imker H.J., Singh J., Warlick B.P., Tabita F.R., Gerlt J.A.
Some homologues of D-ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) do not catalyze carboxylation and are designated RuBisCO-like proteins (RLPs). The RLP from Rhodospirillum rubrum (gi:83593333) catalyzes a novel isomerization reaction (overall 1,3-proton transfer reaction; likely, two ... >> More
Some homologues of D-ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) do not catalyze carboxylation and are designated RuBisCO-like proteins (RLPs). The RLP from Rhodospirillum rubrum (gi:83593333) catalyzes a novel isomerization reaction (overall 1,3-proton transfer reaction; likely, two 1,2-proton transfer reactions) that converts 5-methylthio-D-ribulose 1-phosphate to a 3:1 mixture of 1-methylthioxylulose 5-phosphate and 1-methylthioribulose 5-phosphate. Disruption of the gene encoding the RLP abolishes the ability of R. rubrum to utilize 5'-methylthioadenosine as a sole sulfur source, implicating a new, as-yet-uncharacterized, pathway for sulfur salvage. << Less
Biochemistry 47:11171-11173(2008) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Two Distinct Aerobic Methionine Salvage Pathways Generate Volatile Methanethiol in Rhodopseudomonas palustris.
Miller A.R., North J.A., Wildenthal J.A., Tabita F.R.
5'-Methyl-thioadenosine (MTA) is a dead-end, sulfur-containing metabolite and cellular inhibitor that arises from <i>S-</i>adenosyl-l-methionine-dependent reactions. Recent studies have indicated that there are diverse bacterial <u>m</u>ethionine <u>s</u>alvage <u>p</u>athways (MSPs) for MTA detox ... >> More
5'-Methyl-thioadenosine (MTA) is a dead-end, sulfur-containing metabolite and cellular inhibitor that arises from <i>S-</i>adenosyl-l-methionine-dependent reactions. Recent studies have indicated that there are diverse bacterial <u>m</u>ethionine <u>s</u>alvage <u>p</u>athways (MSPs) for MTA detoxification and sulfur salvage. Here, via a combination of gene deletions and directed metabolite detection studies, we report that under aerobic conditions the facultatively anaerobic bacterium <i>Rhodopseudomonas palustris</i> employs both an MTA-isoprenoid shunt identical to that previously described in <i>Rhodospirillum rubrum</i> and a second novel MSP, both of which generate a methanethiol intermediate. The additional <i>R. palustris</i> aerobic MSP, a dihydroxyacetone phosphate (DHAP)-methanethiol shunt, initially converts MTA to 2-(methylthio)ethanol and DHAP. This is identical to the initial steps of the recently reported anaerobic ethylene-forming MSP, the DHAP-ethylene shunt. The aerobic DHAP-methanethiol shunt then further metabolizes 2-(methylthio)ethanol to methanethiol, which can be directly utilized by O-acetyl-l-homoserine sulfhydrylase to regenerate methionine. This is in contrast to the anaerobic DHAP-ethylene shunt, which metabolizes 2-(methylthio)ethanol to ethylene and an unknown organo-sulfur intermediate, revealing functional diversity in MSPs utilizing a 2-(methylthio)ethanol intermediate. When MTA was fed to aerobically growing cells, the rate of volatile methanethiol release was constant irrespective of the presence of sulfate, suggesting a general housekeeping function for these MSPs up through the methanethiol production step. Methanethiol and dimethyl sulfide (DMS), two of the most important compounds of the global sulfur cycle, appear to arise not only from marine ecosystems but from terrestrial ones as well. These results reveal a possible route by which methanethiol might be biologically produced in soil and freshwater environments.<b>IMPORTANCE</b> Biologically available sulfur is often limiting in the environment. Therefore, many organisms have developed methionine salvage pathways (MSPs) to recycle sulfur-containing by-products back into the amino acid methionine. The metabolically versatile bacterium <i>Rhodopseudomonas palustris</i> is unusual in that it possesses two RuBisCOs and two RuBisCO-like proteins. While RuBisCO primarily serves as the carbon fixation enzyme of the Calvin cycle, RuBisCOs and certain RuBisCO-like proteins have also been shown to function in methionine salvage. This work establishes that only one of the <i>R. palustris</i> RuBisCO-like proteins functions as part of an MSP. Moreover, in the presence of oxygen, to salvage sulfur, <i>R. palustris</i> employs two pathways, both of which result in production of volatile methanethiol, a key compound of the global sulfur cycle. When total available sulfur was plentiful, methanethiol was readily released into the environment. However, when sulfur became limiting, methanethiol release decreased, presumably due to methanethiol utilization to regenerate needed methionine. << Less
mBio 9:e00407-18(2018) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.