Cloned (Comment) | Organism |
---|---|
phylogenetic analysis | Pseudomonas putida |
Protein Variants | Comment | Organism |
---|---|---|
E199A | site-directed mutagenesis, the mutant shows reduced activity and reduced affinity for Co2+ compared to the wild-type enzyme | Pseudomonas putida |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
oxalate | competitive inhibition | Pseudomonas putida | |
oxalate | competitive inhibition | Saccharomyces cerevisiae | |
oxalate | competitive inhibition | Thermus thermophilus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.1265 | - |
4-hydroxy-4-methyl-2-oxoglutarate | pH 8.0, 25°C, RraA-like protein Yer010Cp | Saccharomyces cerevisiae | |
0.1507 | - |
4-hydroxy-4-methyl-2-oxoglutarate | pH 8.0, 25°C, RraA-like protein TtRraA | Thermus thermophilus | |
0.1876 | - |
4-hydroxy-4-methyl-2-oxoglutarate | pH 8.0, 25°C, wild-type enzyme | Pseudomonas putida | |
0.7086 | - |
4-hydroxy-4-methyl-2-oxoglutarate | pH 8.0, 25°C, mutant E199A | Pseudomonas putida |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | required, best activating metal ion, Km is 0.00838 mM for the wild-type enzyme, and 0.446 mM for the mutant E199A | Pseudomonas putida | |
Co2+ | required, equally activating as Ni2+ | Thermus thermophilus | |
Mg2+ | a magnesium ion is coordinated directly or indirectly via water through interactions with Asp102, Asp124, and Glu199 | Pseudomonas putida | |
additional information | the enzyme is a class II divalent metal ion-dependent aldolase | Thermus thermophilus | |
additional information | the enzyme is a class II divalent metal ion-dependent aldolase | Saccharomyces cerevisiae | |
additional information | the enzyme is a class II divalent metal ion-dependent aldolase. Coordination of a metal ion to support the binding of a pyruvyl moiety in the class II aldolase is essential, metal binding Glu199 residue | Pseudomonas putida | |
Ni2+ | required, best activating metal ion | Saccharomyces cerevisiae | |
Ni2+ | required, equally activating as Co2+ | Thermus thermophilus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-hydroxy-4-methyl-2-oxoglutarate | Pseudomonas putida | - |
2 pyruvate | - |
? | |
additional information | Pseudomonas putida | the enzyme is a class II, divalent metal ion-dependent, pyruvate aldolase that catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate and 4-carboxy-4-hydroxy-2-oxoadipate into two molecules of pyruvate in the former and a molecule of each pyruvate and oxaloacetate in the latter, cf. 4-carboxy-4-hydroxy-2-oxoadipate aldolase, EC 4.1.3. The enzyme also contains a secondary oxaloacetate decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retroaldol and decarboxylase reactions | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
Thermus thermophilus | - |
- |
- |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-hydroxy-4-methyl-2-oxoglutarate | - |
Thermus thermophilus | 2 pyruvate | - |
? | |
4-hydroxy-4-methyl-2-oxoglutarate | - |
Saccharomyces cerevisiae | 2 pyruvate | - |
? | |
4-hydroxy-4-methyl-2-oxoglutarate | - |
Pseudomonas putida | 2 pyruvate | - |
? | |
4-hydroxy-4-methyl-2-oxoglutarate | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | 2 pyruvate | - |
? | |
additional information | the enzyme is a class II, divalent metal ion-dependent, pyruvate aldolase that catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate and 4-carboxy-4-hydroxy-2-oxoadipate into two molecules of pyruvate in the former and a molecule of each pyruvate and oxaloacetate in the latter, cf. 4-carboxy-4-hydroxy-2-oxoadipate aldolase, EC 4.1.3. The enzyme also contains a secondary oxaloacetate decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retroaldol and decarboxylase reactions | Pseudomonas putida | ? | - |
? | |
additional information | the RNAse E activity A-like protein TtRraA from Thermus thermophilus HB8 contains HMG aldolase and oxaloacetate decarboxylase activities | Thermus thermophilus | ? | - |
? | |
additional information | the RNAse E activity A-like protein Yer010Cp from Saccharomyces cerevisiae S288C contains HMG aldolase and oxaloacetate decarboxylase activities | Saccharomyces cerevisiae | ? | - |
? | |
additional information | the RNAse E activity A-like protein TtRraA from Thermus thermophilus HB8 contains HMG aldolase and oxaloacetate decarboxylase activities | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
trimer | - |
Pseudomonas putida |
Synonyms | Comment | Organism |
---|---|---|
4-hydroxy-4-methyl-2-oxoglutarate aldolase | - |
Pseudomonas putida |
4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase | - |
Pseudomonas putida |
HMG aldolase | - |
Thermus thermophilus |
HMG aldolase | - |
Saccharomyces cerevisiae |
HMG aldolase | - |
Pseudomonas putida |
HMG/CHA aldolase | - |
Pseudomonas putida |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Thermus thermophilus |
25 | - |
assay at | Saccharomyces cerevisiae |
25 | - |
assay at | Pseudomonas putida |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0276 | - |
4-hydroxy-4-methyl-2-oxoglutarate | pH 8.0, 25°C, RraA-like protein Yer010Cp | Saccharomyces cerevisiae | |
0.061 | - |
4-hydroxy-4-methyl-2-oxoglutarate | pH 8.0, 25°C, mutant E199A | Pseudomonas putida | |
0.356 | - |
4-hydroxy-4-methyl-2-oxoglutarate | pH 8.0, 25°C, RraA-like protein TtRraA | Thermus thermophilus | |
15.6 | - |
4-hydroxy-4-methyl-2-oxoglutarate | pH 8.0, 25°C, wild-type enzyme | Pseudomonas putida |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Thermus thermophilus |
8 | - |
assay at | Saccharomyces cerevisiae |
8 | - |
assay at | Pseudomonas putida |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0319 | - |
oxalate | pH 8.0, 25°C, RraA-like protein Yer010Cp | Saccharomyces cerevisiae | |
0.0377 | - |
oxalate | pH 8.0, 25°C, RraA-like protein TtRraA | Thermus thermophilus |
General Information | Comment | Organism |
---|---|---|
evolution | RNase E activity A, RraA, like protein (RraA-like protein) TtRraA from Thermus thermophilus HB8 (TtRraA) contains HMG aldolase and oxaloacetate decarboxylase activities. The enzyme TtRraA contains a G-X20-R-D-X2-E/D motif | Thermus thermophilus |
evolution | RNase E activity A, RraA, like proteins TtRraA and Yer010Cp from Thermus thermophilus HB8 (TtRraA) and Saccharomyces cerevisiae S288C (Yer010Cp) contain HMG aldolase and oxaloacetate decarboxylase activities and a G-X20-R-D-X2-E/D motif, that may support metal binding. The Pseudomonas putida F1 HMG/CHA aldolase has a D-X20-R-D motif. Structural and fucntional relationships of the HMG/CHA aldolase and RraA-like proteins, overview | Pseudomonas putida |
evolution | RNase E activity A-like protein (RraA-like protein) Yer010Cp from Saccharomyces cerevisiae S288C contains HMG aldolase and oxaloacetate decarboxylase activities. The enzyme Yer010Cp contains a G-X20-R-D-X2-E/D motif | Saccharomyces cerevisiae |
metabolism | 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolases are class II pyruvate aldolases from the meta cleavage pathways of protocatechuate and gallate | Pseudomonas putida |
additional information | the Pseudomonas putida F1 HMG/CHA aldolase has a D-X20-R-D motif, active site structure, structure-function relationship, overview. The Glu199 residue in HMG/CHA aldolase positions one water molecule and in concert with the Asp102 residue positions a second water molecule that coordinate with the bound magnesium ion | Pseudomonas putida |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
86 | - |
4-hydroxy-4-methyl-2-oxoglutarate | pH 8.0, 25°C, mutant E199A | Pseudomonas putida | |
210 | - |
4-hydroxy-4-methyl-2-oxoglutarate | pH 8.0, 25°C, RraA-like protein Yer010Cp | Saccharomyces cerevisiae | |
2400 | - |
4-hydroxy-4-methyl-2-oxoglutarate | pH 8.0, 25°C, RraA-like protein TtRraA | Thermus thermophilus | |
83000 | - |
4-hydroxy-4-methyl-2-oxoglutarate | pH 8.0, 25°C, wild-type enzyme | Pseudomonas putida |