EC Number   |
Natural Substrates |
|---|
   5.3.2.5 | 2,3-diketo-1-phosphohexane |
an alternate substrate for the methionine salvage pathway |
| 5.3.2.5 | 5-(methylthio)-2,3-dioxopentyl phosphate |
- |
| 5.3.2.5 | 5-(methylthio)-2,3-dioxopentyl phosphate |
Rhodospirillum rubrum Form II RubisCO |
| 5.3.2.5 | 5-methylthio-2,3-dioxo-pentyl phosphate |
purified recombinant rubisco-like protein RbcLIV, overexpressed in Escherichia coli cells, does not display CO2 fixation activity but catalyzes enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate |
| 5.3.2.5 | 5-methylthioribulose 1-phosphate |
Rhodospirillum rubrum RLP |
| 5.3.2.5 | more |
RLP has no RuBP-carboxylating activity, RLP catalyzes the DK-MTP-1-P enolase reaction and not the enolase/phosphatase reaction |
| 5.3.2.5 | more |
the enzyme catalyzes the tautomerization of 2,3-diketo-5-methylthiopentane 1-phosphate in the methionine salvage pathway in which 5-methylthio-D-ribose derived from 5'-methylthioadenosine is converted to methionine. The reaction is accomplished by abstraction of the 1-proS proton from C1 of the DK-MTP 1-P substrate to form the tautomerized product, a conjugated enol. Stabilization of an enolate anion intermediate by coordination to an active site Mg2+. Structure-function relationships, overview. The enolase from Geobacillus kaustophilus catalyzes stereospecific abstraction of the 1-proS proton of the DK-MTP 1-P substrate |
| 5.3.2.5 | more |
the form II RubisCO enzyme from the nonsulfur purple bacterium Rhodospirillum rubrum is also able to function as an enolase in vivo as part of an methionine salvage pathway, but only under anaerobic conditions |
