BRENDA - Enzyme Database show
show all sequences of 1.1.1.26

A highly specific glyoxylate reductase derived from a formate dehydrogenase

Shinoda, T.; Arai, K.; Taguchi, H.; Biochem. Biophys. Res. Commun. 355, 782-787 (2007)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of a E141N/Q313E mutant formate dehydrogenase which gains glyoxylate reductase activity improved through enhancement of the hydrogen transfer step in the catalytic process, while the replacement induces no marked activity toward other 2-koxoacid substrates, and diminishes the enzyme's activity as to formate oxidation, substrate specificity and kinetic switch of the mutant, overview
Paracoccus sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
7.4
-
glyoxylate
pH 7.0, 30°C, recombinant E141N/Q313E mutant formate dehydrogenase
Paracoccus sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Paracoccus sp.
-
strain 12-A
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
glyoxylate + NADH
a E141N/Q313E mutant formate dehydrogenase shows glyoxylate reductase activity improved through enhancement of the hydrogen transfer step in the catalytic process, overview
684838
Paracoccus sp.
glycolate + NAD+
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at, E141N/Q313E mutant formate dehydrogenase
Paracoccus sp.
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.3
-
glyoxylate
pH 7.0, 30°C, recombinant E141N/Q313E mutant formate dehydrogenase
Paracoccus sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at, E141N/Q313E mutant formate dehydrogenase
Paracoccus sp.
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Paracoccus sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Paracoccus sp.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of a E141N/Q313E mutant formate dehydrogenase which gains glyoxylate reductase activity improved through enhancement of the hydrogen transfer step in the catalytic process, while the replacement induces no marked activity toward other 2-koxoacid substrates, and diminishes the enzyme's activity as to formate oxidation, substrate specificity and kinetic switch of the mutant, overview
Paracoccus sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
7.4
-
glyoxylate
pH 7.0, 30°C, recombinant E141N/Q313E mutant formate dehydrogenase
Paracoccus sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
glyoxylate + NADH
a E141N/Q313E mutant formate dehydrogenase shows glyoxylate reductase activity improved through enhancement of the hydrogen transfer step in the catalytic process, overview
684838
Paracoccus sp.
glycolate + NAD+
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at, E141N/Q313E mutant formate dehydrogenase
Paracoccus sp.
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.3
-
glyoxylate
pH 7.0, 30°C, recombinant E141N/Q313E mutant formate dehydrogenase
Paracoccus sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at, E141N/Q313E mutant formate dehydrogenase
Paracoccus sp.
Other publictions for EC 1.1.1.26
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
722899
Ching
Glyoxylate reductase isoform 1 ...
Arabidopsis thaliana
J. Integr. Plant Biol.
54
152-168
2012
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715548
Nunn
Metabolism of pentose sugars i ...
Sulfolobus solfataricus, Sulfolobus solfataricus P2
J. Biol. Chem.
285
33701-33709
2010
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696125
Allan
Role of plant glyoxylate reduc ...
Arabidopsis thaliana
Biochem. J.
423
15-22
2009
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1
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1
2
2
1
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684838
Shinoda
A highly specific glyoxylate r ...
Paracoccus sp.
Biochem. Biophys. Res. Commun.
355
782-787
2007
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1
1
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685349
Fauvart
Identification of a novel glyo ...
Rhizobium etli, Rhizobium etli CFN42
Biochim. Biophys. Acta
1774
1092-1098
2007
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1
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4
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3
6
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6
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1
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11
1
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11
1
1
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4
1
1
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685901
Hoover
Characteristics of an Arabidop ...
Arabidopsis thaliana
Can. J. Bot.
85
883-895
2007
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1
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3
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1
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1
1
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655702
Cregeen
Molecular analysis of the glyo ...
Homo sapiens
Hum. Mutat.
22
497
2003
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1
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3
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727414
Ohshima
A novel hyperthermophilic arch ...
Thermococcus litoralis, Thermococcus litoralis DSM 5473
Eur. J. Biochem.
268
4740-4747
2001
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1
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5
3
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3
2
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10
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1
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1
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6
1
2
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1
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1
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1
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1
1
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5
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3
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3
2
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1
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1
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6
1
2
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1
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1
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286417
Rumsby
Identification and expression ...
Homo sapiens
Biochim. Biophys. Acta
1446
383-388
1999
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1
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1
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286416
Giafi
Kinetic analysis and tissue di ...
Homo sapiens
Ann. Clin. Biochem.
35
104-109
1998
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1
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1
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1
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286418
Givan
The enzymic reduction of glyox ...
Hordeum vulgare, Nicotiana tabacum, Petroselinum crispum, Pisum sativum, Spinacia oleracea, Zea mays
Plant Physiol.
100
552-556
1992
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1
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6
5
9
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5
7
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10
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2
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9
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2
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12
2
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2
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286419
Betsche
Identification and characteria ...
Cyanophora paradoxa, Pisum sativum
Plant Physiol.
98
887-893
1992
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4
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1
10
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8
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2
1
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286409
Yokota
Occurrence and subcellular dis ...
Euglena gracilis
Agric. Biol. Chem.
45
15-22
1981
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1
1
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286408
Hullin
Glyoxylate reductase, two form ...
Pseudomonas fluorescens
Methods Enzymol.
41B
343-348
1975
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2
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1
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2
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1
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286414
Bergmeyer
-
Glyoxylate reductase ...
Spinacia oleracea
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
2
126-328
1974
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1
3
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286410
Suzuki
Studies on peroxisomes. IV. in ...
Rattus norvegicus
J. Biochem.
73
1033-1038
1973
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1
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286413
Cerff
Glyceraldehyde 3-phosphate deh ...
Sinapis alba
Plant Physiol.
51
76-81
1973
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1
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286411
Zelitch
-
Glycolic acid oxidase and glyo ...
Nicotiana tabacum, Spinacia oleracea
Methods Enzymol.
1
528-535
1955
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3
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286412
Zelitch
The isolation and action of cr ...
Nicotiana tabacum
J. Biol. Chem.
216
553-575
1955
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1
1
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286415
Zelitch
Oxidation and reduction of gly ...
Spinacia oleracea
J. Biol. Chem.
201
719-726
1953
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