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Literature summary for 1.1.1.79 extracted from
- New insights into the mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductases (2016), Sci. Rep., 6, 20629.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL | Pyrococcus horikoshii |
| recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL | Pyrococcus yayanosii |
| recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL | Pyrococcus furiosus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| analysis of the three-dimensional crystal structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR | Pyrococcus horikoshii |
| purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, hanging drop vapour diffusion method, from a mother liquor containing 100 mM sodium acetate, pH 5.2, 15% PEG 400, and 100 mM NaCl, 20°C, X-ray diffraction structure determination and analysis at 1.4-2.0 A resolution | Pyrococcus furiosus |
| purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, sitting drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml protein solution with 0.0015 ml of mother liquor containing 1.7 malonate, pH 7.0, 20°C, X-ray diffraction structure determination and analysis at 1.4 A-2.0 A resolution, molecular replacement using the three-dimensional structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR | Pyrococcus yayanosii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) | Pyrococcus horikoshii |
| additional information | constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) | Pyrococcus yayanosii |
| additional information | constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) | Pyrococcus furiosus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glycolate + NADP+ | Pyrococcus horikoshii | - |
glyoxylate + NADPH + H+ | - |
? |  |
| glycolate + NADP+ | Pyrococcus yayanosii | - |
glyoxylate + NADPH + H+ | - |
? | |
| glycolate + NADP+ | Pyrococcus furiosus | - |
glyoxylate + NADPH + H+ | - |
? | |
| glycolate + NADP+ | Pyrococcus yayanosii CH1 | - |
glyoxylate + NADPH + H+ | - |
? | |
| additional information | Pyrococcus horikoshii | a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview | ? | - |
? | |
| additional information | Pyrococcus yayanosii | a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview | ? | - |
? | |
| additional information | Pyrococcus furiosus | a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview | ? | - |
? | |
| additional information | Pyrococcus yayanosii CH1 | a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | Q8U3Y2 | - |
- |
| Pyrococcus horikoshii | - |
- |
- |
| Pyrococcus yayanosii | F8AEA4 | - |
- |
| Pyrococcus yayanosii CH1 | F8AEA4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration | Pyrococcus horikoshii |
| recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration | Pyrococcus yayanosii |
| recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration | Pyrococcus furiosus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glycolate + NADP+ | - |
Pyrococcus horikoshii | glyoxylate + NADPH + H+ | - |
? | |
| glycolate + NADP+ | - |
Pyrococcus yayanosii | glyoxylate + NADPH + H+ | - |
? | |
| glycolate + NADP+ | - |
Pyrococcus furiosus | glyoxylate + NADPH + H+ | - |
? | |
| glycolate + NADP+ | - |
Pyrococcus yayanosii CH1 | glyoxylate + NADPH + H+ | - |
? | |
| additional information | a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview | Pyrococcus horikoshii | ? | - |
? | |
| additional information | a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview | Pyrococcus yayanosii | ? | - |
? | |
| additional information | a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview | Pyrococcus furiosus | ? | - |
? | |
| additional information | a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview | Pyrococcus yayanosii CH1 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GRHPR | - |
Pyrococcus horikoshii |
| GRHPR | - |
Pyrococcus yayanosii |
| GRHPR | - |
Pyrococcus furiosus |
| NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases | - |
Pyrococcus horikoshii |
| NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases | - |
Pyrococcus yayanosii |
| NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases | - |
Pyrococcus furiosus |
| PfuGRHPR | - |
Pyrococcus furiosus |
| PhoGRHPR | - |
Pyrococcus horikoshii |
| PyaGRHPR | - |
Pyrococcus yayanosii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
assay at | Pyrococcus horikoshii |
| 50 | - |
assay at | Pyrococcus yayanosii |
| 50 | - |
assay at | Pyrococcus furiosus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Pyrococcus furiosus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | comparison of cofactor specificities of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) using glyoxylate or hydroxypyruvate as substrates and NADH or NADPH as cofactors, crystal structures analysis, overview | Pyrococcus horikoshii | |
| additional information | comparison of cofactor specificities of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) using glyoxylate or hydroxypyruvate as substrates and NADH or NADPH as cofactors, crystal structures analysis, overview | Pyrococcus yayanosii | |
| additional information | comparison of cofactor specificities of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) using glyoxylate or hydroxypyruvate as substrates and NADH or NADPH as cofactors, crystal structures analysis, overview | Pyrococcus furiosus | |
| NADP+ | - |
Pyrococcus horikoshii | |
| NADP+ | - |
Pyrococcus yayanosii | |
| NADP+ | - |
Pyrococcus furiosus | |
| NADPH | - |
Pyrococcus horikoshii | |
| NADPH | - |
Pyrococcus yayanosii | |
| NADPH | - |
Pyrococcus furiosus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | role in the substrate binding mode and role of Leu53 and Trp138 in substrate trafficking is conserved between human and archeal enzymes, modelling, overview | Pyrococcus horikoshii |
| evolution | role in the substrate binding mode and role of Leu53 and Trp138 in substrate trafficking is conserved between human and archeal enzymes, modelling, overview | Pyrococcus yayanosii |
| evolution | role in the substrate binding mode and role of Leu53 and Trp138 in substrate trafficking is conserved between human and archeal enzymes, modelling, overview | Pyrococcus furiosus |
| additional information | residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview | Pyrococcus horikoshii |
| additional information | residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview | Pyrococcus yayanosii |
| additional information | residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview | Pyrococcus furiosus |
| physiological function | the NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases (GRHPR) regulate the glyoxylate content within cells, highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. The enzyme from the hyperthermophilic archaeon, displays a higher preference for glyoxylate than hydroxypyruvate in presence of NADH, whereas no activity is detected in presence of NADPH | Pyrococcus furiosus |
| physiological function | the NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases (GRHPR) regulates the glyoxylate content within cells, highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. The enzyme from the hyperthermophilic archaeon, displays a higher preference for glyoxylate than hydroxypyruvate in presence of NADH, whereas no activity is detected in presence of NADPH | Pyrococcus horikoshii |
| physiological function | the NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases (GRHPR) regulates the glyoxylate content within cells, highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. The enzyme from the hyperthermophilic archaeon, displays a higher preference for glyoxylate than hydroxypyruvate in presence of NADH, whereas no activity is detected in presence of NADPH | Pyrococcus yayanosii |
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