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Information on EC 5.3.2.5 - 2,3-diketo-5-methylthiopentyl-1-phosphate enolase
for references in articles please use BRENDA:EC5.3.2.5
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EC Tree 5 Isomerases
5.3 Intramolecular oxidoreductases
5.3.2 Interconverting keto- and enol-groups
5.3.2.5 2,3-diketo-5-methylthiopentyl-1-phosphate enolase
IUBMB Comments
The enzyme participates in the methionine salvage pathway in Bacillus subtilis .In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 3.1.3.87, 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase .
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
showSynonyms
dk-mtp-1-p enolase, 2,3-diketo-5-methylthiopentyl-1-phosphate enolase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3-diketo-5-methylthiopentane 1-phosphate enolase
DK-MTP 1-P enolase
DK-MTP-1-P enolase
MtnW
RLP
RuBisCO-like protein
YkrW
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DK-MTP-1-P enolase
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MtnW
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RLP
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ambiguous
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RuBisCO-like protein
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate
5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate
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5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate
reaction mechanism, overview
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5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate
reaction mechanism, overview
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5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate
reaction mechanism, overview
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5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate
reaction mechanism, overview
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5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate
reaction mechanism, overview
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5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate
structure-function relationship and reaction mechanism, overview
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5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate
structure-function relationship and reaction mechanism, overview
5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate
structure-function relationship and reaction mechanism, overview
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PATHWAY SOURCE
PATHWAYS
MetaCyc
S-methyl-5-thio-alpha-D-ribose 1-phosphate degradation I
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SYSTEMATIC NAME
IUBMB Comments
2,3-diketo-5-methylthiopentyl-1-phosphate keto-enol-isomerase
The enzyme participates in the methionine salvage pathway in Bacillus subtilis [2].In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 3.1.3.87, 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase [1].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-diketo-l-phospho-5-thiomethylpentane
?
-
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl 1-phosphate
2-hydroxy-3-oxo-5-methylthiopentenyl 1-phosphate
-
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
5-methylthio-2,3-dioxo-pentyl phosphate
2-hydroxy-5-methylthio-3-oxopentenyl phosphate
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Substrates: 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
Products: -
Products: -
?
5-methylthioribulose 1-phosphate
1-thiomethyl-D-xylulose 5-phosphate + 1-thiomethyl-D-ribulose 5-phosphate
2,3-diketo-1-phosphohexane
2-hydroxy-3-keto-l-phospho-l-hexene
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Substrates: an alternate substrate for the methionine salvage pathway
Products: -
Products: -
?
2,3-diketo-1-phosphohexane
2-hydroxy-3-keto-l-phospho-l-hexene
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Substrates: an analogue to 2,3-diketo-5-methylthio-1-phosphopentane
Products: a chromophoric intermediate compound, product determination by NMR analysis
Products: a chromophoric intermediate compound, product determination by NMR analysis
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
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Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
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Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
r
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
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Substrates: Rhodospirillum rubrum Form II RubisCO
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
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Substrates: Rhodospirillum rubrum Form II RubisCO
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
?
5-methylthioribulose 1-phosphate
1-thiomethyl-D-xylulose 5-phosphate + 1-thiomethyl-D-ribulose 5-phosphate
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Substrates: Rhodospirillum rubrum RLP
Products: -
Products: -
ir
5-methylthioribulose 1-phosphate
1-thiomethyl-D-xylulose 5-phosphate + 1-thiomethyl-D-ribulose 5-phosphate
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Substrates: Rhodospirillum rubrum RLP
Products: -
Products: -
ir
additional information
?
-
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Substrates: RLP has no RuBP-carboxylating activity, RLP catalyzes the DK-MTP-1-P enolase reaction and not the enolase/phosphatase reaction
Products: -
Products: -
?
additional information
?
-
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Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-diketo-1-phosphohexane
2-hydroxy-3-keto-l-phospho-l-hexene
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Substrates: an alternate substrate for the methionine salvage pathway
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
5-methylthio-2,3-dioxo-pentyl phosphate
2-hydroxy-5-methylthio-3-oxopentenyl phosphate
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Substrates: 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
Products: -
Products: -
?
5-methylthioribulose 1-phosphate
1-thiomethyl-D-xylulose 5-phosphate + 1-thiomethyl-D-ribulose 5-phosphate
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
r
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: Rhodospirillum rubrum Form II RubisCO
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: Rhodospirillum rubrum Form II RubisCO
Products: -
Products: -
?
5-(methylthio)-2,3-dioxopentyl phosphate
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
Substrates: -
Products: -
Products: -
?
5-methylthioribulose 1-phosphate
1-thiomethyl-D-xylulose 5-phosphate + 1-thiomethyl-D-ribulose 5-phosphate
-
Substrates: Rhodospirillum rubrum RLP
Products: -
Products: -
ir
5-methylthioribulose 1-phosphate
1-thiomethyl-D-xylulose 5-phosphate + 1-thiomethyl-D-ribulose 5-phosphate
-
Substrates: Rhodospirillum rubrum RLP
Products: -
Products: -
ir
additional information
?
-
-
Substrates: RLP has no RuBP-carboxylating activity, RLP catalyzes the DK-MTP-1-P enolase reaction and not the enolase/phosphatase reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
5-(methylthio)-2,3-dioxopentyl 1-phosphate
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C
0.013
5-(methylthio)-2,3-dioxopentyl 1-phosphate
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mutant enzyme K122R, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
56
5-(methylthio)-2,3-dioxopentyl 1-phosphate
-
mutant enzyme K122R, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C
83
5-(methylthio)-2,3-dioxopentyl 1-phosphate
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4400
5-(methylthio)-2,3-dioxopentyl 1-phosphate
-
mutant enzyme K122R, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C
7100
5-(methylthio)-2,3-dioxopentyl 1-phosphate
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
overall pathway activity, purified enzyme, pH 7.5, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a spontaneous streptomycin-resistant derivative of strain S1, gene rlpA
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brenda
a spontaneous streptomycin-resistant derivative of strain S1, gene rlpA
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brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
functional and evolutionary links between Bacillus subtilis RLP and photosynthetic RuBisCO, photosynthetic RuBisCOs evolved from RLPs, phylogenetic tree, Bacillus subtilis RLP belongs to form IV, overview
evolution
-
members of the form IV subfamily, Rubisco-like proteins or RLPs, do not display Rubisco activity, but the two eubacterial members of this family play a role in sulfur metabolism. Discovery of the coexistence of RbcLI and RbcLIV in cyanobacteria, the ancestors of chloroplasts, enlightens episodes of the chaotic evolutionary history of the Rubiscos, a protein family of major importance for life on earth
evolution
-
phylogenetic tree of RuBisCO and RLPs, overview. The RLP of Bacillus subtilis includes both those amino acid residues of RuBisCO that are responsible for binding the phosphate on C1 of RuBP and those required for activation by CO2. However, the residues of RuBisCO that are responsible for binding the other phosphate group of RuBP and the residues of loop 6, which are essential for RuBisCO activity are replaced by different amino acids in RLP
evolution
-
the Bacillus subtilis enzyme belongs to the RLPalpha-1 enzyme group, functional and evolutionary relationships between Bacillus subtilis RLP of the methionine salvage pathway, other RLPs, and photosynthetic RuBisCO, overview
evolution
-
the enzyme belongs to the RuBisCO superfamily. The functionally divergent Geobacillus kaustophilus member of the RuBisCO superfamily uses the same structural strategy as RuBisCO for stabilizing the enolate anion intermediate, i.e., coordination to an essential Mg2+, but the proton abstraction is catalyzed by a different general base
evolution
the enzyme belongs to the RuBisCO superfamily. The functionally divergent Geobacillus kaustophilus member of the RuBisCO superfamily uses the same structural strategy as RuBisCO for stabilizing the enolate anion intermediate, i.e., coordination to an essential Mg2+, but the proton abstraction is catalyzed by a different general base
evolution
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the enzyme belongs to the RubisCO-like protein, RLP, family of proteins. Unlike Bacillus subtilis RLP, Rodospirillum rubrum RLP does not catalyze the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate. Instead, under aerobic growth conditions, R. rubrum RLP employs another intermediate of the MSP, 5-methylthioribulose-1-phosphate, as a substrate, resulting in the formation of different products
evolution
-
the Geobacillus kaustophilis enzyme belongs to the RLPalpha-1 enzyme group, functional and evolutionary relationships between Bacillus subtilis RLP of the methionine salvage pathway, other RLPs, and photosynthetic RuBisCO, overview
evolution
-
the Microcystis aeruginosa enzyme belongs to the RLPalpha-1 enzyme group, functional and evolutionary relationships between Bacillus subtilis RLP of the methionine salvage pathway, other RLPs, and photosynthetic RuBisCO, overview
evolution
-
the Rhodopseudomonas palustris enzyme belongs to the RLPalpha-1 enzyme group, functional and evolutionary relationships between Bacillus subtilis RLP of the methionine salvage pathway, other RLPs, and photosynthetic RuBisCO, overview
evolution
-
the Rhodospirillum rubrum enzyme belongs to the RLPalpha-1 enzyme group, functional and evolutionary relationships between Bacillus subtilis RLP of the methionine salvage pathway, other RLPs, and photosynthetic RuBisCO, overview
evolution
-
the enzyme belongs to the RuBisCO superfamily. The functionally divergent Geobacillus kaustophilus member of the RuBisCO superfamily uses the same structural strategy as RuBisCO for stabilizing the enolate anion intermediate, i.e., coordination to an essential Mg2+, but the proton abstraction is catalyzed by a different general base
-
malfunction
-
the rlpA disruption strain of Rhodospirillum rubrum was incapable of using 5-methylthioadenosine as the sole sulfur source under aerobic growth conditions
malfunction
-
a growth-defective mutant, in which the gene for this RLP is disrupted, is rescued by the gene for RuBisCO from the photosynthetic bacterium Rhodospirillum rubrum, the photosynthetic RuBisCO from Rhodospirillum rubrum retains the ability to function in the methionine salvage pathway in Bacillus subtilis
malfunction
-
the RLP disruption strain of Rhodospirillum rubrum is incapable of 5-methylthioadenosine-dependent growth under aerobic growth conditions. The rlpA disruption strain of Rhodospirillum rubrum is incapable of using 5-methylthioadenosine as the sole sulfur source under aerobic growth conditions
malfunction
-
the rlpA disruption strain of Rhodospirillum rubrum was incapable of using 5-methylthioadenosine as the sole sulfur source under aerobic growth conditions
-
metabolism
-
Bacillus subtilis RLP is involved in the methionine salvage pathway, overview
metabolism
-
Geobacillus kaustophilis RLP is involved in the methionine salvage pathway, overview
metabolism
-
Klebsiella pneumoniae converts 2,3-diketo-5-methylthio-l-phosphopentane to formate, 2-keto-4-methylthiobutyrate, and 3-methylthiopropionate. 2,3-diketo-1-phosphohexane, the desthio analogue of the naturally occurring diketone, can serve as alternate substrate in the methionine salvage pathway
metabolism
-
Microcystis aeruginosa RLP is involved in the methionine salvage pathway, overview
metabolism
-
Rhodopseudomonas palustris RLP is involved in the methionine salvage pathway, it utilizes the methionine salvage pathway because it can grow using 5-methyladenosine as the sole source of sulfur, although the reaction step of DK-MTP-1-P enolase may be catalysed by a photosynthetic form II RuBisCO and not by RLPs, overview
metabolism
-
Rhodospirillum rubrum RLP is involved in the methionine salvage pathway, it utilizes the methionine salvage pathway because it can grow using 5-methyladenosine as the sole source of sulfur, although the reaction step of DK-MTP-1-P enolase may be catalysed by a photosynthetic form II RuBisCO and not by RLPs, overview
metabolism
-
the enzyme is involved in the methionine salvage pathway. It is a heterofunctional homologue of RuBisCO catalyzing 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
metabolism
the enzyme is involved in the methionine salvage pathway. It is a heterofunctional homologue of RuBisCO catalyzing 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
metabolism
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the RLP of Bacillus subtilis is the 2,3-diketo-5-methylthiopentyl-1-phosphate enolase in the methionine salvage pathway, overview
metabolism
-
the RuBisCO-like protein catalyzes the 2,3-diketo-5-methylthiopentyl-1-phosphate enolase reaction in the methionine salvage pathway
metabolism
-
the enzyme is involved in the methionine salvage pathway. It is a heterofunctional homologue of RuBisCO catalyzing 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
-
metabolism
-
Klebsiella pneumoniae converts 2,3-diketo-5-methylthio-l-phosphopentane to formate, 2-keto-4-methylthiobutyrate, and 3-methylthiopropionate. 2,3-diketo-1-phosphohexane, the desthio analogue of the naturally occurring diketone, can serve as alternate substrate in the methionine salvage pathway
-
physiological function
-
RLP is required for metabolizing 5-methylthioadenosine
physiological function
-
2,3-diketo-5-methylthiopentyl-1-phosphate enolase is a RuBisCO-like protein, that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate
physiological function
-
Bacillus subtilis RLP catalyses an analogous reaction to photosynthetic RuBisCO since its substrate resembles the structure of RuBP, rationalizing the tight linkage between RLPs and RuBisCO. But Bacillus subtilis RLP functions as an enzyme in a different metabolic pathway from that of RuBisCO, overview
physiological function
-
functional and evolutionary links between Bacillus subtilis RLP and photosynthetic RuBisCO, overview
physiological function
-
RubisCO-like protein, RLP, is required for metabolizing 5-methylthioadenosine.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
physiological function
-
RLP is required for metabolizing 5-methylthioadenosine
-
physiological function
-
RubisCO-like protein, RLP, is required for metabolizing 5-methylthioadenosine.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
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additional information
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conserved residues Asn123, Lys175, Lys201, Asp203, and His204 are essential for the enolization reaction of DK-MTP-1-P enolase
additional information
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conserved residues Asn123, Lys175, Lys201, Asp203, and His204 are essential for the enolization reaction of DK-MTP-1-P enolase
additional information
-
conserved residues Lys123, Lys175, Lys201, Asp203, and Glu204 that are essential for the enolization reaction of DK-MTP-1-P enolase
additional information
-
conserved residues Lys123, Lys175, Lys201, Asp203, and Glu204 that are essential for the enolization reaction of DK-MTP-1-P enolase
additional information
-
conserved residues Lys123, Lys175, Lys201, Asp203, and Glu204 that are essential for the enolization reaction of DK-MTP-1-P enolase
additional information
-
structure-function relationship, the active site KDDE motif with the carboxylated Lys173 as well as two carboxylate ligands Asp175 and Glu176 are essential for Mg2+ stabilization and also for stabilizing the enediolate intermediate, the carbamate group of the carboxylated Lys173 is the third ligand for the essential Mg2+ as well as the general base Lys98 that initiates the reaction by abstraction of the proton from the substrate
additional information
structure-function relationship, the active site KDDE motif with the carboxylated Lys173 as well as two carboxylate ligands Asp175 and Glu176 are essential for Mg2+ stabilization and also for stabilizing the enediolate intermediate, the carbamate group of the carboxylated Lys173 is the third ligand for the essential Mg2+ as well as the general base Lys98 that initiates the reaction by abstraction of the proton from the substrate
additional information
-
the rbcLIV gene rescues a Bacillus subtilis MtnW-deficient mutant
additional information
-
structure-function relationship, the active site KDDE motif with the carboxylated Lys173 as well as two carboxylate ligands Asp175 and Glu176 are essential for Mg2+ stabilization and also for stabilizing the enediolate intermediate, the carbamate group of the carboxylated Lys173 is the third ligand for the essential Mg2+ as well as the general base Lys98 that initiates the reaction by abstraction of the proton from the substrate
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Show AA Sequence and Transmembrane Helices (1038 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
-
structure of the apo decarbamylated enzyme E form, computational structure analysis and modeling, structure comparison, overview. In the E form of DK-MTP-1P enolase the loop at 299-311, equivalent to loop-6 in RuBisCO, is in a closed conformation and the loop at 37-46, equivalent to the 60s loop, is positioned about 15 A away from the active site
dimer
-
the active site is located at the open end of a C-terminal (beta/alpha)8-barrel, induced fit of Lys150 to the active site upon substrate binding
dimer
-
RbcLIV secondary structure analysis, spectroscopic analysis, and three-dimensional structure modeling, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
activated wild-type enolase, carboxylated on Lys173, with Mg2+ alone, or Mg2+, and HCO3-, or Mg2+ and substrate 2,3-diketohexane 1-phosphate, and of the selenomethionine-substituted enzyme variant, hanging drop method, 10-15 mg/ml protein in 20 mM Tris-HCl, pH 7.9, 100 mM NaCl, and 5-10 mM MgCl2, 100 mM NaCl, and 1-5 mM NaHCO3, mixed with 24% PEG 3350, 0.1 M Tris-HCl, pH 8.5, and 0.2 M ammonium acetate as precipitant for the crystals of wild-type enzyme with Mg2+, or 25% PEG 3350, 0.1 M HEPES, pH 7.5, and 0.2 M ammonium acetate as precipitant for the other crystal variants, room temperature, 6 days, X-ray diffraction structure determination and analysis at 1.7 A resolution, molecular replacement
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K122E
-
the mutant fails to form a catalytic dimer and does not show any DK-MTP-1-P enolase activity
K122M
-
the mutant fails to form a catalytic dimer and does not show any DK-MTP-1-P enolase activity
K122R
-
the mutant has specific activity of 32% less than that of the wild type enzyme and a lower thermal stability than the wild type enzyme
K147A
site-directed mutagenesis, the mutant requires a 10fold greater concentration of protein for enolization of the natural substrate, reduced activity compared to the wild-type enzyme
K173A
site-directed mutagenesis, the mutant is able to catalyze enolization at approximately the same rate as the wild-type enzyme
K98A
site-directed mutagenesis, the mutant is unable to catalyze the enolase reaction
I19A
additional information
-
a growth-defective mutant, in which the gene for the RLP is disrupted, is rescued by the gene for RuBisCO from the photosynthetic bacterium Rhodospirillum rubrum
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
the wild type enzyme shows no decline in activity after incubation at 40°C, and retains about 80% of its original activity after incubation at 45°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by fractionation with help of protamine suzlfate, ammonium sulfate, and P-60, followed by anion exchange and hydrophobic interaction chromatography
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by two different steps of anion exchange chromatography and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Bacillus subtilis RLPalpha-1 sequence determination and analysis, and phylogenetic analysis
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene rbcLIV, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, cloning in Escherichia coli strain JM109, expression in Escherichia coli strain BL21
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gene rlpA, form II RubisCO-like protein, cloning and expression in Escherichia coli strain DH5alpha
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Geobacillus kaustophilis RLPalpha-1 sequence determination and analysis, and phylogenetic analysis
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Microcystis aeruginosa RLPalpha-1 sequence determination and analysis, and phylogenetic analysis
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overexpression in Klebsiella pneumoniae strain CG253 leading to 5-6fold increased activity compared to the parent strain
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Rhodopseudomonas palustris RLPalpha-1 sequence determination and analysis, and phylogenetic analysis
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Rhodospirillum rubrum RLPalpha-1 sequence determination and analysis, and phylogenetic analysis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Myers, R.W.; Wray, J.W.; Fish, S.; Abeles, R.H.
Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae
J. Biol. Chem.
268
24785-24791
1993
Klebsiella pneumoniae, Klebsiella pneumoniae CG253
brenda
Imker, H.J.; Fedorov, A.A.; Fedorov, E.V.; Almo, S.C.; Gerlt, J.A.
Mechanistic diversity in the RuBisCO superfamily: the enolase in the methionine salvage pathway in Geobacillus kaustophilus
Biochemistry
46
4077-4089
2007
Bacillus subtilis, Bacillus subtilis 168, Geobacillus kaustophilus (Q5L1E2)
brenda
Ashida, H.; Saito, Y.; Nakano, T.; Tandeau de Marsac, N.; Sekowska, A.; Danchin, A.; Yokota, A.
RuBisCO-like proteins as the enolase enzyme in the methionine salvage pathway: functional and evolutionary relationships between RuBisCO-like proteins and photosynthetic RuBisCO
J. Exp. Bot.
59
1543-1554
2008
Bacillus subtilis, Geobacillus kaustophilus, Microcystis aeruginosa, Rhodopseudomonas palustris, Rhodospirillum rubrum
brenda
Tamura, H.; Saito, Y.; Ashida, H.; Kai, Y.; Inoue, T.; Yokota, A.; Matsumura, H.
Structure of the apo decarbamylated form of 2,3-diketo-5-methylthiopentyl-1-phosphate enolase from Bacillus subtilis
Acta Crystallogr. Sect. D
65
942-951
2009
Bacillus subtilis
brenda
Ashida, H.; Saito, Y.; Kojima, C.; Ogasawara, N.; Yokota, A.
A functional link between RuBisCo-like protein of Bacillus and photosynthetic RuBisCo
Science
302
286-290
2003
Bacillus subtilis
brenda
Nakano, T.; Ashida, H.; Mizohata, E.; Matsumura, H.; Yokota, A.
An evolutionally conserved Lys122 is essential for function in Rhodospirillum rubrum bona fide RuBisCO and Bacillus subtilis RuBisCO-like protein
Biochem. Biophys. Res. Commun.
392
212-216
2010
Bacillus subtilis
brenda
Singh, J.; Tabita, F.
Roles of RubisCO and the RubisCO-like protein in 5-methylthioadenosine metabolism in the nonsulfur purple bacterium Rhodospirillum rubrum
J. Bacteriol.
192
1324-1331
2010
Rhodospirillum rubrum, Rhodospirillum rubrum Str-2
brenda
Carre-Mlouka, A.; Mejean, A.; Quillardet, P.; Ashida, H.; Saito, Y.; Yokota, A.; Callebaut, I.; Sekowska, A.; Dittmann, E.; Bouchier, C.; de Marsac, N.T.
A new rubisco-like protein coexists with a photosynthetic rubisco in the planktonic cyanobacteria Microcystis
J. Biol. Chem.
281
24462-24471
2006
Microcystis aeruginosa
brenda
Ashida, H.; Danchin, A.; Yokota, A.
Was photosynthetic RuBisCO recruited by acquisitive evolution from RuBisCO-like proteins involved in sulfur metabolism?
Res. Microbiol.
156
611-618
2005
Bacillus subtilis
brenda
Warlick, B.P.; Imker, H.J.; Sriram, J.; Tabita, F.R.; Gerlt, J.A.
Mechanistic diversity in the RuBisCO superfamily: RuBisCO from Rhodospirillum rubrum is not promiscuous for reactions catalyzed by RuBisCO-like proteins
Biochemistry
51
9470-9479
2012
Geobacillus kaustophilus, no activity in Rhodospirillum rubrum
brenda
Nakano, T.; Ohki, I.; Yokota, A.; Ashida, H.
MtnBD is a multifunctional fusion enzyme in the methionine salvage pathway of Tetrahymena thermophila
PLoS ONE
8
e67385
2013
Tetrahymena thermophila
brenda
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