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Literature summary extracted from

  • Hoover, G.J.; Jorgensen, R.; Rochon, A.; Bajwa, V.S.; Merrill, A.R.; Shelp, B.J.
    Identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants (2013), Biochim. Biophys. Acta, 1834, 2663-2671.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.B47 gene GLYR1, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 pLysS Arabidopsis thaliana
1.1.1.79 gene GLYR1, sequence comparisons of GLYR genes and HPR genes Arabidopsis thaliana
1.1.1.79 gene GLYR1, sequence comparisons of GLYR genes and HPR genes, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 pLysS Arabidopsis thaliana
1.1.1.79 gene GLYR2, sequence comparisons of GLYR genes and HPR genes, recombinant expression of a His6-tagged truncated AtGLYR2 cDNA sequence, lacking the N-terminal 58 amino acids, in Escherichia coli strain BL21 pLysS Arabidopsis thaliana
1.1.1.81 gene HPR3, sequence comparisons of GLYR genes and HPR genes Arabidopsis thaliana

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.B47 purified apo-enzyme, sitting drop vapor diffusion method, mixing of 0.002 ml of protein solution with 0.002 ml of reservoir solution containing 0.2 M calcium acetate hydrate, 20% PEG 3350, pH 6.5, 20°C, 6 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using a previously unrecognized member of the beta-HAD family, cytokine-like nuclear factor, structure Arabidopsis thaliana
1.1.1.79 purified apo-enzyme, sitting drop vapor diffusion method, mixing of 0.002 ml of protein solution with 0.002 ml of reservoir solution containing 0.2 M calcium acetate hydrate, 20% PEG 3350, pH 6.5, 20°C, 6 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using a previously unrecognized member of the beta-HAD family, cytokine-like nuclear factor, structure Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.B47 D239A site-directed mutagenesis Arabidopsis thaliana
1.1.1.B47 F231A site-directed mutagenesis Arabidopsis thaliana
1.1.1.B47 K170A site-directed mutagenesis, catalytically inactive mutant Arabidopsis thaliana
1.1.1.B47 K170E site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type Arabidopsis thaliana
1.1.1.B47 K170H site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type Arabidopsis thaliana
1.1.1.B47 K170R site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type Arabidopsis thaliana
1.1.1.B47 N174A site-directed mutagenesis Arabidopsis thaliana
1.1.1.B47 S121A site-directed mutagenesis Arabidopsis thaliana
1.1.1.B47 T95A site-directed mutagenesis Arabidopsis thaliana
1.1.1.79 D239A site-directed mutagenesis Arabidopsis thaliana
1.1.1.79 F231A site-directed mutagenesis Arabidopsis thaliana
1.1.1.79 K170A site-directed mutagenesis, catalytically inactive mutant Arabidopsis thaliana
1.1.1.79 K170E site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type Arabidopsis thaliana
1.1.1.79 K170H site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type Arabidopsis thaliana
1.1.1.79 K170R site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type Arabidopsis thaliana
1.1.1.79 N174A site-directed mutagenesis Arabidopsis thaliana
1.1.1.79 S121A site-directed mutagenesis Arabidopsis thaliana
1.1.1.79 T95A site-directed mutagenesis Arabidopsis thaliana

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.B47 additional information
-
 additional information Michaelis-Menten kinetics, the activities of the mutant enzymes with succinic semialdehyde are generally too low for kinetic studies Arabidopsis thaliana
1.1.1.B47 0.0022
-
 NADPH pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer Arabidopsis thaliana
1.1.1.B47 0.87
-
 Succinic semialdehyde pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer Arabidopsis thaliana
1.1.1.79 additional information
-
 additional information Michaelis-Menten kinetics Arabidopsis thaliana
1.1.1.79 0.0009
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A Arabidopsis thaliana
1.1.1.79 0.0018
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A Arabidopsis thaliana
1.1.1.79 0.002
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A Arabidopsis thaliana
1.1.1.79 0.0022
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a double beam spectrophotometer Arabidopsis thaliana
1.1.1.79 0.0027
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A Arabidopsis thaliana
1.1.1.79 0.0034
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme Arabidopsis thaliana
1.1.1.79 0.0045
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a double beam spectrophotometer Arabidopsis thaliana
1.1.1.79 0.016
-
 glyoxylate pH 7.8, temperature not specified in the publication, recombinant truncated enzyme Arabidopsis thaliana
1.1.1.79 0.018
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme Arabidopsis thaliana
1.1.1.79 0.033
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E Arabidopsis thaliana
1.1.1.79 0.061
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R Arabidopsis thaliana
1.1.1.79 0.0648
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A Arabidopsis thaliana
1.1.1.79 0.088
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A Arabidopsis thaliana
1.1.1.79 0.181
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A Arabidopsis thaliana
1.1.1.79 3
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A Arabidopsis thaliana
1.1.1.79 4.6
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A Arabidopsis thaliana
1.1.1.79 12.4
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A Arabidopsis thaliana
1.1.1.81 6.1
-
 Hydroxypyruvate GLYR1, at pH 7.8 and 22°C Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.26 peroxisome
-
 Arabidopsis thaliana 5777
-
1.1.1.29 peroxisome
-
 Arabidopsis thaliana 5777
-
1.1.1.B47 cytosol
-
 Arabidopsis thaliana 5829
-
1.1.1.79 chloroplast
-
 Arabidopsis thaliana 9507
-
1.1.1.79 cytosol
-
 Arabidopsis thaliana 5829
-
1.1.1.81 chloroplast
-
 Arabidopsis thaliana 9507
-
1.1.1.81 cytosol
-
 Arabidopsis thaliana 5829
-
1.1.1.81 peroxisome
-
 Arabidopsis thaliana 5777
-
1.1.1.81 plastid
-
 Arabidopsis thaliana 9536
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.26 glycolate + NAD+ Arabidopsis thaliana
-
 glyoxylate + NADH + H+
-
 r
1.1.1.26 additional information Arabidopsis thaliana the recombinant AtHPR1 prefers prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate ?
-
 ?
1.1.1.29 hydroxypyruvate + NADH + H+ Arabidopsis thaliana
-
 D-glycerate + NAD+
-
 ?
1.1.1.B47 additional information Arabidopsis thaliana the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, the enzyme has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate ?
-
 ?
1.1.1.B47 succinic semialdehyde + NADPH + H+ Arabidopsis thaliana
-
 4-hydroxybutyrate + NADP+
-
 ?
1.1.1.79 glycolate + NADP+ Arabidopsis thaliana
-
 glyoxylate + NADPH + H+
-
 r
1.1.1.79 additional information Arabidopsis thaliana HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate ?
-
 ?
1.1.1.79 additional information Arabidopsis thaliana the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate ?
-
 ?
1.1.1.79 additional information Arabidopsis thaliana the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate ?
-
 ?
1.1.1.79 additional information Arabidopsis thaliana the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly ?
-
 ?
1.1.1.81 D-glycerate + NAD+ Arabidopsis thaliana
-
 hydroxypyruvate + NADH + H+
-
 ?
1.1.1.81 D-glycerate + NADP+ Arabidopsis thaliana
-
 hydroxypyruvate + NADPH + H+
-
 r
1.1.1.81 additional information Arabidopsis thaliana HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate ?
-
 ?
1.1.1.81 additional information Arabidopsis thaliana the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate ?
-
 ?
1.1.1.81 additional information Arabidopsis thaliana the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly ?
-
 ?
1.1.1.298 3-hydroxypropanoate + NADP+ Thermus thermophilus
-
 malonate semialdehyde + NADPH + H+
-
 ?
1.1.1.298 3-hydroxypropanoate + NADP+ Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 malonate semialdehyde + NADPH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.26 Arabidopsis thaliana Q9C9W5 cf. EC 1.1.1.29
-
1.1.1.29 Arabidopsis thaliana Q9C9W5
-
-
1.1.1.B47 Arabidopsis thaliana Q9LSV0
-
-
1.1.1.60 Salmonella enterica subsp. enterica serovar Typhimurium Q8ZLV8
-
-
1.1.1.79 Arabidopsis thaliana A0A178WMD4
-
-
1.1.1.79 Arabidopsis thaliana F4I907
-
-
1.1.1.79 Arabidopsis thaliana Q9CA90
-
-
1.1.1.79 Arabidopsis thaliana Q9LSV0
-
-
1.1.1.81 Arabidopsis thaliana A0A178WMD4
-
-
1.1.1.81 Arabidopsis thaliana A0A1I9LPQ6
-
-
1.1.1.81 Arabidopsis thaliana Q9C9W5
-
-
1.1.1.81 Arabidopsis thaliana Q9CA90
-
-
1.1.1.81 Arabidopsis thaliana Q9LE33
-
-
1.1.1.298 Thermus thermophilus Q5SLQ6
-
-
1.1.1.298 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q5SLQ6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.B47 recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography Arabidopsis thaliana
1.1.1.79 recombinant His6-tagged truncated mutant enzyme from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography Arabidopsis thaliana
1.1.1.79 recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography Arabidopsis thaliana

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.B47 4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH + H+ the enzyme performs an acid/base catalytic mechanism involving Lys170 as the general acid and a conserved active-site water molecule Arabidopsis thaliana
a
1.1.1.79 glycolate + NADP+ = glyoxylate + NADPH + H+ the enzyme performs an acid/base catalytic mechanism involving Lys170 as the general acid and a conserved active-site water molecule Arabidopsis thaliana
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.26 glycolate + NAD+
-
 Arabidopsis thaliana glyoxylate + NADH + H+
-
 r
1.1.1.26 additional information the recombinant AtHPR1 prefers prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate Arabidopsis thaliana ?
-
 ?
1.1.1.29 hydroxypyruvate + NADH + H+
-
 Arabidopsis thaliana D-glycerate + NAD+
-
 ?
1.1.1.B47 additional information the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, the enzyme has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate Arabidopsis thaliana ?
-
 ?
1.1.1.B47 succinic semialdehyde + NADPH + H+
-
 Arabidopsis thaliana 4-hydroxybutyrate + NADP+
-
 ?
1.1.1.79 glycolate + NADP+
-
 Arabidopsis thaliana glyoxylate + NADPH + H+
-
 r
1.1.1.79 glyoxylate + NADPH + H+
-
 Arabidopsis thaliana glycolate + NADP+
-
 r
1.1.1.79 additional information HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate Arabidopsis thaliana ?
-
 ?
1.1.1.79 additional information the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate Arabidopsis thaliana ?
-
 ?
1.1.1.79 additional information the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate Arabidopsis thaliana ?
-
 ?
1.1.1.79 additional information the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly Arabidopsis thaliana ?
-
 ?
1.1.1.81 D-glycerate + NAD+
-
 Arabidopsis thaliana hydroxypyruvate + NADH + H+
-
 ?
1.1.1.81 D-glycerate + NADP+
-
 Arabidopsis thaliana hydroxypyruvate + NADPH + H+
-
 r
1.1.1.81 hydroxypyruvate + NADH + H+
-
 Arabidopsis thaliana D-glycerate + NAD+
-
 ?
1.1.1.81 hydroxypyruvate + NADH + H+ isoform HPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate Arabidopsis thaliana D-glycerate + NAD+
-
 ?
1.1.1.81 hydroxypyruvate + NADH + H+ isoform HPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly Arabidopsis thaliana D-glycerate + NAD+
-
 ?
1.1.1.81 hydroxypyruvate + NADH + H+ isoform HPR3 prefers NADPH over NADH and glyoxylate over hydroxypyvruvate Arabidopsis thaliana D-glycerate + NAD+
-
 ?
1.1.1.81 hydroxypyruvate + NADPH + H+ isoform HPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate Arabidopsis thaliana D-glycerate + NADP+
-
 ?
1.1.1.81 hydroxypyruvate + NADPH + H+ isoform HPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly Arabidopsis thaliana D-glycerate + NADP+
-
 ?
1.1.1.81 hydroxypyruvate + NADPH + H+ isoform HPR3 prefers NADPH over NADH and glyoxylate over hydroxypyvruvate Arabidopsis thaliana D-glycerate + NADP+
-
 ?
1.1.1.81 additional information the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH Arabidopsis thaliana ?
-
 ?
1.1.1.81 additional information HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate Arabidopsis thaliana ?
-
 ?
1.1.1.81 additional information the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate Arabidopsis thaliana ?
-
 ?
1.1.1.81 additional information the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly Arabidopsis thaliana ?
-
 ?
1.1.1.298 3-hydroxypropanoate + NADP+
-
 Thermus thermophilus malonate semialdehyde + NADPH + H+
-
 ?
1.1.1.298 3-hydroxypropanoate + NADP+
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 malonate semialdehyde + NADPH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.B47 More enzyme domain structure analysis, overview Arabidopsis thaliana
1.1.1.79 More domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
1.1.1.26 glycerate dehydrogenase
-
 Arabidopsis thaliana
1.1.1.26 HPR1
-
 Arabidopsis thaliana
1.1.1.29 HPR1
-
 Arabidopsis thaliana
1.1.1.29 hydroxypyruvate reductase
-
 Arabidopsis thaliana
1.1.1.B47 At3g25530
-
 Arabidopsis thaliana
1.1.1.B47 AtGLYR1
-
 Arabidopsis thaliana
1.1.1.B47 SSA
-
 Arabidopsis thaliana
1.1.1.B47 succinic semialdehyde reductase
-
 Arabidopsis thaliana
1.1.1.60 tartronate semialdehyde reductase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.60 TSAR
-
 Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.79 At3g25530
-
 Arabidopsis thaliana
1.1.1.79 AtGLYR1
-
 Arabidopsis thaliana
1.1.1.79 AtGLYR2
-
 Arabidopsis thaliana
1.1.1.79 glycerate dehydrogenase
-
 Arabidopsis thaliana
1.1.1.79 GLYR1
-
 Arabidopsis thaliana
1.1.1.79 GLYR2
-
 Arabidopsis thaliana
1.1.1.79 HPR2
-
 Arabidopsis thaliana
1.1.1.79 HPR3
-
 Arabidopsis thaliana
1.1.1.79 More cf. EC 1.1.1.26 Arabidopsis thaliana
1.1.1.81 glycerate dehydrogenase
-
 Arabidopsis thaliana
1.1.1.81 GLYR1
-
 Arabidopsis thaliana
1.1.1.81 HPR1
-
 Arabidopsis thaliana
1.1.1.81 HPR1 isoform Arabidopsis thaliana
1.1.1.81 HPR2
-
 Arabidopsis thaliana
1.1.1.81 HPR2 isoform Arabidopsis thaliana
1.1.1.81 HPR3
-
 Arabidopsis thaliana
1.1.1.81 HPR3 isoform Arabidopsis thaliana
1.1.1.81 More cf. EC 1.1.1.26 Arabidopsis thaliana
1.1.1.298 3-HIBADH
-
 Thermus thermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.79 0.0052
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E Arabidopsis thaliana
1.1.1.79 0.051
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R Arabidopsis thaliana
1.1.1.79 6.06
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A Arabidopsis thaliana
1.1.1.79 9.09
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A Arabidopsis thaliana
1.1.1.79 9.56
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A Arabidopsis thaliana
1.1.1.79 11
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A Arabidopsis thaliana
1.1.1.79 22
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A Arabidopsis thaliana
1.1.1.79 25.4
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A Arabidopsis thaliana
1.1.1.79 51.1
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A Arabidopsis thaliana
1.1.1.79 54.6
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme Arabidopsis thaliana
1.1.1.79 67.8
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A Arabidopsis thaliana
1.1.1.79 84.1
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme Arabidopsis thaliana
1.1.1.79 86.4
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A Arabidopsis thaliana
1.1.1.79 93.7
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A Arabidopsis thaliana
1.1.1.79 3407
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.B47 7.8
-
 assay at Arabidopsis thaliana
1.1.1.79 7.8
-
 assay at Arabidopsis thaliana
1.1.1.81 7.8
-
 assay at Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.26 NAD+
-
 Arabidopsis thaliana
1.1.1.26 NADH
-
 Arabidopsis thaliana
1.1.1.29 NADH
-
 Arabidopsis thaliana
1.1.1.B47 additional information recombinant AtGLYR1 prefers NADPH over NADH Arabidopsis thaliana
1.1.1.B47 NADP+
-
 Arabidopsis thaliana
1.1.1.B47 NADPH
-
 Arabidopsis thaliana
1.1.1.79 additional information recombinant AtGLYR1 prefers NADPH over NADH Arabidopsis thaliana
1.1.1.79 additional information recombinant AtGLYR2 prefers NADPH over NADH Arabidopsis thaliana
1.1.1.79 additional information recombinant HPR3 prefers NADPH over NADH Arabidopsis thaliana
1.1.1.79 additional information the recombinant AtHPR2 prefers NADPH over NADH Arabidopsis thaliana
1.1.1.79 NADP+
-
 Arabidopsis thaliana
1.1.1.79 NADPH
-
 Arabidopsis thaliana
1.1.1.81 additional information recombinant HPR3 prefers NADPH over NADH Arabidopsis thaliana
1.1.1.81 additional information the recombinant AtHPR2 prefers NADPH over NADH Arabidopsis thaliana
1.1.1.81 NAD+
-
 Arabidopsis thaliana
1.1.1.81 NADH
-
 Arabidopsis thaliana
1.1.1.81 NADH isoform HPR1 prefers NADH over NADPH Arabidopsis thaliana
1.1.1.81 NADH isoform HPR2 prefers NADPH over NADH Arabidopsis thaliana
1.1.1.81 NADH isoform HPR3 prefers NADPH over NADH Arabidopsis thaliana
1.1.1.81 NADP+
-
 Arabidopsis thaliana
1.1.1.81 NADPH
-
 Arabidopsis thaliana
1.1.1.81 NADPH isoform HPR1 prefers NADH over NADPH Arabidopsis thaliana
1.1.1.81 NADPH isoform HPR2 prefers NADPH over NADH Arabidopsis thaliana
1.1.1.81 NADPH isoform HPR3 prefers NADPH over NADH Arabidopsis thaliana
1.1.1.298 NADP+
-
 Thermus thermophilus

General Information

EC Number General Information Comment Organism
1.1.1.26 evolution the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs Arabidopsis thaliana
1.1.1.B47 evolution the primary sequence of cytosolic AtGLYR1 reveals several sequence elements that are consistent with the beta-HAD (beta-hydroxyacid dehydrogenase) protein family, sequence alignment of AtGLYR1 and beta-HAD family members, overview Arabidopsis thaliana
1.1.1.B47 additional information identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis Arabidopsis thaliana
1.1.1.79 evolution the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family Arabidopsis thaliana
1.1.1.79 evolution the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs Arabidopsis thaliana
1.1.1.79 evolution the primary sequence of cytosolic AtGLYR1 reveals several sequence elements that are consistent with the beta-HAD (beta-hydroxyacid dehydrogenase) protein family, sequence alignment of AtGLYR1 and beta-HAD family members, overview. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs Arabidopsis thaliana
1.1.1.79 evolution the primary sequence of plastidial AtGLYR2 reveals several sequence elements that are consistent with the beta-HAD (beta-hydroxyacid dehydrogenase) protein family, sequence alignment of AtGLYR2 and beta-HAD family members, overview. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs Arabidopsis thaliana
1.1.1.79 additional information identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis. Residues Thr95, Phe231 and Asp239 serve a more important role in substrate orientation and docking than in catalysis Arabidopsis thaliana
1.1.1.81 evolution the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs Arabidopsis thaliana
1.1.1.81 physiological function hydroxypyruvate reductase activity is important in the recycling of metabolites derived during photorespiration Arabidopsis thaliana

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.B47 11.6
-
 Succinic semialdehyde pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer Arabidopsis thaliana
1.1.1.79 0.19
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E Arabidopsis thaliana
1.1.1.79 0.86
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R Arabidopsis thaliana
1.1.1.79 0.87
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A Arabidopsis thaliana
1.1.1.79 7.45
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A Arabidopsis thaliana
1.1.1.79 14.6
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A Arabidopsis thaliana
1.1.1.79 72.8
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A Arabidopsis thaliana
1.1.1.79 480
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A Arabidopsis thaliana
1.1.1.79 779
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A Arabidopsis thaliana
1.1.1.79 2870
-
 glyoxylate pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer Arabidopsis thaliana
1.1.1.79 3407
-
 glyoxylate pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme Arabidopsis thaliana
1.1.1.79 4340
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A Arabidopsis thaliana
1.1.1.79 10400
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A Arabidopsis thaliana
1.1.1.79 10900
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A Arabidopsis thaliana
1.1.1.79 24450
-
 NADPH pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a microplate reader Arabidopsis thaliana
1.1.1.79 51700
-
 NADPH pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A Arabidopsis thaliana
1.1.1.81 0.232
-
 Hydroxypyruvate GLYR1, at pH 7.8 and 22°C Arabidopsis thaliana