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Literature summary for 1.1.1.81 extracted from

  • Yoshikawa, S.; Arai, R.; Kinoshita, Y.; Uchikubo-Kamo, T.; Wakamatsu, T.; Akasaka, R.; Masui, R.; Terada, T.; Kuramitsu, S.; Shirouzu, M.; Yokoyama, S.
    Structure of archaeal glyoxylate reductase from Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate (2007), Acta Crystallogr. Sect. D, 63, 357-365.
    View publication on PubMed
Search for more literature for 1.1.1.81

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL and Escherichia coli B834(DE3)pRARE Pyrococcus horikoshii OT3

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method in the presence of NAD, crystal structure analysis reveals tightly bound NADP(H) at the enzyme originating from Escherichia coli expression, which is not replaceable by NAD Pyrococcus horikoshii OT3

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
 NADH with hydroxypyruvate as substrate, pH 7.5 Pyrococcus horikoshii OT3
0.015
-
 NADH with glyoxylate as substrate, pH 7.5 Pyrococcus horikoshii OT3
0.021
-
 NADPH with glyoxylate as substrate, pH 7.5 Pyrococcus horikoshii OT3
0.025
-
 NADPH with hydroxypyruvate as substrate, pH 7.5 Pyrococcus horikoshii OT3

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
 x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation Pyrococcus horikoshii OT3
76500
-
 analytical ultracentrifugation Pyrococcus horikoshii OT3

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii OT3
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein from Escherichia coli Pyrococcus horikoshii OT3

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glyoxylate + NADH
-
 Pyrococcus horikoshii OT3 glycolate + NAD+
-
 ?
glyoxylate + NADPH
-
 Pyrococcus horikoshii OT3 glycolate + NADP+
-
 ?
hydroxypyruvate + NADH
-
 Pyrococcus horikoshii OT3 D-glycerate + NAD+
-
 ?
hydroxypyruvate + NADPH
-
 Pyrococcus horikoshii OT3 D-glycerate + NADP+
-
 ?

Subunits

Subunits Comment Organism
dimer x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation Pyrococcus horikoshii OT3

Synonyms

Synonyms Comment Organism
More hydroxypyruvate reductase (EC 1.1.1.81) activity is found for the same protein showing NADH- and NADPH-dependent glyoxylate reductase (EC 1.1.1.26 or 1.1.1.79) activity, closely related to D-glycerate dehydrogense (EC 1.1.1.29) Pyrococcus horikoshii OT3

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8
-
 NADPH with hydroxypyruvate as substrate, pH 7.5 Pyrococcus horikoshii OT3
2.4
-
 NADPH with glyoxylate as substrate, pH 7.5 Pyrococcus horikoshii OT3
4.1
-
 NADH with hydroxypyruvate as substrate, pH 7.5 Pyrococcus horikoshii OT3
11
-
 NADH with glyoxylate as substrate, pH 7.5 Pyrococcus horikoshii OT3

Cofactor

Cofactor Comment Organism Structure
NADH enzyme has a higher affinity for NADPH than for NADH when incubated without substrate Pyrococcus horikoshii OT3
NADPH enzyme has a higher affinity for NADPH than for NADH when incubated without substrate Pyrococcus horikoshii OT3