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Literature summary extracted from

  • Lassalle, L.; Engilberge, S.; Madern, D.; Vauclare, P.; Franzetti, B.; Girard, E.
    New insights into the mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductases (2016), Sci. Rep., 6, 20629.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.79 recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL Pyrococcus horikoshii
1.1.1.79 recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL Pyrococcus yayanosii
1.1.1.79 recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL Pyrococcus furiosus
1.1.1.81 expressed in Escherichia coli BL21(DE3) cells Pyrococcus horikoshii
1.1.1.81 expressed in Escherichia coli BL21(DE3) cells Pyrococcus yayanosii
1.1.1.81 expressed in Escherichia coli BL21(DE3) cells Pyrococcus furiosus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.79 analysis of the three-dimensional crystal structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR Pyrococcus horikoshii
1.1.1.79 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
1.1.1.79 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
1.1.1.81 in complex with D-glycerate and NADPH, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 5.2, 15% (w/v) polyethylene glycol 400 and 100 mM NaCl Pyrococcus horikoshii
1.1.1.81 in complex with D-glycerate and NADPH, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 5.2, 15% (w/v) polyethylene glycol 400 and 100 mM NaCl Pyrococcus yayanosii
1.1.1.81 in complex with D-glycerate and NADPH, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 5.2, 15% (w/v) polyethylene glycol 400 and 100 mM NaCl Pyrococcus furiosus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.79 additional information constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) Pyrococcus horikoshii
1.1.1.79 additional information constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) Pyrococcus yayanosii
1.1.1.79 additional information constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) Pyrococcus furiosus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.81 Hydroxypyruvate
-
 Pyrococcus furiosus
1.1.1.81 Hydroxypyruvate
-
 Pyrococcus horikoshii
1.1.1.81 Hydroxypyruvate
-
 Pyrococcus yayanosii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.81 0.02
-
 Hydroxypyruvate with NADPH as cosubstrate, at pH 8.0 and 50°C Pyrococcus horikoshii
1.1.1.81 0.07
-
 Hydroxypyruvate with NADH as cosubstrate, at pH 8.0 and 50°C Pyrococcus horikoshii
1.1.1.81 0.09
-
 Hydroxypyruvate with NADPH as cosubstrate, at pH 8.0 and 50°C Pyrococcus furiosus
1.1.1.81 0.14
-
 Hydroxypyruvate with NADH as cosubstrate, at pH 8.0 and 50°C Pyrococcus furiosus
1.1.1.81 0.165
-
 Hydroxypyruvate with NADPH as cosubstrate, at pH 8.0 and 50°C Pyrococcus yayanosii
1.1.1.81 0.41
-
 Hydroxypyruvate with NADH as cosubstrate, at pH 8.0 and 50°C Pyrococcus yayanosii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.79 glycolate + NADP+ Pyrococcus horikoshii
-
 glyoxylate + NADPH + H+
-
 ?
1.1.1.79 glycolate + NADP+ Pyrococcus yayanosii
-
 glyoxylate + NADPH + H+
-
 ?
1.1.1.79 glycolate + NADP+ Pyrococcus furiosus
-
 glyoxylate + NADPH + H+
-
 ?
1.1.1.79 glycolate + NADP+ Pyrococcus yayanosii CH1
-
 glyoxylate + NADPH + H+
-
 ?
1.1.1.79 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 ?
-
 ?
1.1.1.79 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 ?
-
 ?
1.1.1.79 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 ?
-
 ?
1.1.1.79 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 ?
-
 ?
1.1.1.81 hydroxypyruvate + NADH + H+ Pyrococcus horikoshii
-
 D-glycerate + NAD+
-
 ?
1.1.1.81 hydroxypyruvate + NADH + H+ Pyrococcus yayanosii
-
 D-glycerate + NAD+
-
 ?
1.1.1.81 hydroxypyruvate + NADH + H+ Pyrococcus furiosus
-
 D-glycerate + NAD+
-
 ?
1.1.1.81 hydroxypyruvate + NADH + H+ Pyrococcus yayanosii CH1
-
 D-glycerate + NAD+
-
 ?
1.1.1.81 hydroxypyruvate + NADPH + H+ Pyrococcus horikoshii
-
 D-glycerate + NADP+
-
 ?
1.1.1.81 hydroxypyruvate + NADPH + H+ Pyrococcus yayanosii
-
 D-glycerate + NADP+
-
 ?
1.1.1.81 hydroxypyruvate + NADPH + H+ Pyrococcus furiosus
-
 D-glycerate + NADP+
-
 ?
1.1.1.81 hydroxypyruvate + NADPH + H+ Pyrococcus yayanosii CH1
-
 D-glycerate + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.79 Pyrococcus furiosus Q8U3Y2
-
-
1.1.1.79 Pyrococcus horikoshii
-
-
-
1.1.1.79 Pyrococcus yayanosii F8AEA4
-
-
1.1.1.79 Pyrococcus yayanosii CH1 F8AEA4
-
-
1.1.1.81 Pyrococcus furiosus Q8U3Y2
-
-
1.1.1.81 Pyrococcus horikoshii
-
-
-
1.1.1.81 Pyrococcus yayanosii F8AEA4
-
-
1.1.1.81 Pyrococcus yayanosii CH1 F8AEA4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.79 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
1.1.1.79 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
1.1.1.79 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
1.1.1.81 Resource Q column chromatography and Superose 12 column chromatography Pyrococcus horikoshii
1.1.1.81 Resource Q column chromatography and Superose 12 column chromatography Pyrococcus yayanosii
1.1.1.81 Resource Q column chromatography and Superose 12 column chromatography Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.79 glycolate + NADP+
-
 Pyrococcus horikoshii glyoxylate + NADPH + H+
-
 ?
1.1.1.79 glycolate + NADP+
-
 Pyrococcus yayanosii glyoxylate + NADPH + H+
-
 ?
1.1.1.79 glycolate + NADP+
-
 Pyrococcus furiosus glyoxylate + NADPH + H+
-
 ?
1.1.1.79 glycolate + NADP+
-
 Pyrococcus yayanosii CH1 glyoxylate + NADPH + H+
-
 ?
1.1.1.79 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 ?
-
 ?
1.1.1.79 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 ?
-
 ?
1.1.1.79 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 ?
-
 ?
1.1.1.79 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 ?
-
 ?
1.1.1.81 hydroxypyruvate + NADH + H+
-
 Pyrococcus horikoshii D-glycerate + NAD+
-
 ?
1.1.1.81 hydroxypyruvate + NADH + H+
-
 Pyrococcus yayanosii D-glycerate + NAD+
-
 ?
1.1.1.81 hydroxypyruvate + NADH + H+
-
 Pyrococcus furiosus D-glycerate + NAD+
-
 ?
1.1.1.81 hydroxypyruvate + NADH + H+
-
 Pyrococcus yayanosii CH1 D-glycerate + NAD+
-
 ?
1.1.1.81 hydroxypyruvate + NADPH + H+
-
 Pyrococcus horikoshii D-glycerate + NADP+
-
 ?
1.1.1.81 hydroxypyruvate + NADPH + H+
-
 Pyrococcus yayanosii D-glycerate + NADP+
-
 ?
1.1.1.81 hydroxypyruvate + NADPH + H+
-
 Pyrococcus furiosus D-glycerate + NADP+
-
 ?
1.1.1.81 hydroxypyruvate + NADPH + H+
-
 Pyrococcus yayanosii CH1 D-glycerate + NADP+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.79 GRHPR
-
 Pyrococcus horikoshii
1.1.1.79 GRHPR
-
 Pyrococcus yayanosii
1.1.1.79 GRHPR
-
 Pyrococcus furiosus
1.1.1.79 NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases
-
 Pyrococcus horikoshii
1.1.1.79 NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases
-
 Pyrococcus yayanosii
1.1.1.79 NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases
-
 Pyrococcus furiosus
1.1.1.79 PfuGRHPR
-
 Pyrococcus furiosus
1.1.1.79 PhoGRHPR
-
 Pyrococcus horikoshii
1.1.1.79 PyaGRHPR
-
 Pyrococcus yayanosii
1.1.1.81 glyoxylate/hydroxypyruvate reductase
-
 Pyrococcus horikoshii
1.1.1.81 glyoxylate/hydroxypyruvate reductase
-
 Pyrococcus yayanosii
1.1.1.81 glyoxylate/hydroxypyruvate reductase
-
 Pyrococcus furiosus
1.1.1.81 GRHPR
-
 Pyrococcus horikoshii
1.1.1.81 GRHPR
-
 Pyrococcus yayanosii
1.1.1.81 GRHPR
-
 Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.79 50
-
 assay at Pyrococcus horikoshii
1.1.1.79 50
-
 assay at Pyrococcus yayanosii
1.1.1.79 50
-
 assay at Pyrococcus furiosus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.81 0.6
-
 Hydroxypyruvate with NADPH as cosubstrate, at pH 8.0 and 50°C Pyrococcus horikoshii
1.1.1.81 1.2
-
 Hydroxypyruvate with NADPH as cosubstrate, at pH 8.0 and 50°C Pyrococcus furiosus
1.1.1.81 4.5
-
 Hydroxypyruvate with NADH as cosubstrate, at pH 8.0 and 50°C Pyrococcus horikoshii
1.1.1.81 6.5
-
 Hydroxypyruvate with NADPH as cosubstrate, at pH 8.0 and 50°C Pyrococcus yayanosii
1.1.1.81 10
-
 Hydroxypyruvate with NADH as cosubstrate, at pH 8.0 and 50°C Pyrococcus furiosus
1.1.1.81 25
-
 Hydroxypyruvate with NADH as cosubstrate, at pH 8.0 and 50°C Pyrococcus yayanosii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.79 8
-
 assay at Pyrococcus furiosus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.79 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
1.1.1.79 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
1.1.1.79 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
1.1.1.79 NADP+
-
 Pyrococcus horikoshii
1.1.1.79 NADP+
-
 Pyrococcus yayanosii
1.1.1.79 NADP+
-
 Pyrococcus furiosus
1.1.1.79 NADPH
-
 Pyrococcus horikoshii
1.1.1.79 NADPH
-
 Pyrococcus yayanosii
1.1.1.79 NADPH
-
 Pyrococcus furiosus
1.1.1.81 NADH the enzyme prefers NADH over NADPH Pyrococcus horikoshii
1.1.1.81 NADH the enzyme prefers NADH over NADPH Pyrococcus yayanosii
1.1.1.81 NADH the enzyme prefers NADH over NADPH Pyrococcus furiosus
1.1.1.81 NADPH the enzyme prefers NADH over NADPH Pyrococcus horikoshii
1.1.1.81 NADPH the enzyme prefers NADH over NADPH Pyrococcus yayanosii
1.1.1.81 NADPH the enzyme prefers NADH over NADPH Pyrococcus furiosus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.81 0.35
-
 Hydroxypyruvate in the presence of NADH, at pH 8.0 and 50°C Pyrococcus furiosus
1.1.1.81 0.76
-
 Hydroxypyruvate in the presence of NADH, at pH 8.0 and 50°C Pyrococcus yayanosii
1.1.1.81 2
-
 Hydroxypyruvate in the presence of NADPH, at pH 8.0 and 50°C Pyrococcus yayanosii
1.1.1.81 3.82
-
 Hydroxypyruvate in the presence of NADH, at pH 8.0 and 50°C Pyrococcus horikoshii

General Information

EC Number General Information Comment Organism
1.1.1.79 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
1.1.1.79 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
1.1.1.79 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
1.1.1.79 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
1.1.1.79 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
1.1.1.79 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
1.1.1.79 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
1.1.1.79 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
1.1.1.79 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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.81 15
-
 Hydroxypyruvate with NADPH as cosubstrate, at pH 8.0 and 50°C Pyrococcus furiosus
1.1.1.81 30
-
 Hydroxypyruvate with NADPH as cosubstrate, at pH 8.0 and 50°C Pyrococcus horikoshii
1.1.1.81 40
-
 Hydroxypyruvate with NADPH as cosubstrate, at pH 8.0 and 50°C Pyrococcus yayanosii
1.1.1.81 60
-
 Hydroxypyruvate with NADH as cosubstrate, at pH 8.0 and 50°C Pyrococcus yayanosii
1.1.1.81 65
-
 Hydroxypyruvate with NADH as cosubstrate, at pH 8.0 and 50°C Pyrococcus horikoshii
1.1.1.81 75
-
 Hydroxypyruvate with NADH as cosubstrate, at pH 8.0 and 50°C Pyrococcus furiosus