BRENDA - Enzyme Database show
show all sequences of 1.1.99.14

Glycolate oxidoreductase in Escherichia coli

Lord, J.M.; Biochim. Biophys. Acta 267, 227-237 (1971)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
CuSO4
-
Escherichia coli
cytochrome c
inhibits rate of phenazine methosulfate stimulated dichlorophenolindophenol reduction
Escherichia coli
HgCl2
complete
Escherichia coli
K3[Fe(CN)6]
complete inhibition
Escherichia coli
KCN
-
Escherichia coli
additional information
high ionic strength; overview over inhibitors at different concentrations
Escherichia coli
PCMB
-
Escherichia coli
ZnCl2
-
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
glycolate
-
Escherichia coli
0.7
-
D(-)-lactate
-
Escherichia coli
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Escherichia coli
5737
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
glycolate + acceptor
Escherichia coli
the bacterial enzyme catalyzes phenazine methosulfate dependent reduction of 2,6-dichlorophenolindophenol or cytochrome c
glyocylate + reduced acceptor
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Commentary
Organism
partially, from cells grown on glycolate
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.14
-
glyoxylate formation in the presence of phenazine methosulfate
Escherichia coli
0.15
-
crude extract
Escherichia coli
3.1
-
partially purified protein
Escherichia coli
Storage Stability
Storage Stability
Organism
2°C, half-life of 10 days, FMN or FAD do not restore activity
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-lactate + acceptor
best substrate
348285
Escherichia coli
pyruvate + reduced acceptor
-
-
-
?
(R)-lactate + acceptor
artificial acceptor 2,6-dichlorophenolindophenol is reduced via phenazine methosulfate, cytochrome c can replace 2,6-dichlorophenolindophenol
348285
Escherichia coli
pyruvate + reduced acceptor
-
-
-
?
(S)-lactate + acceptor
about 16% activity of glycolate
348285
Escherichia coli
pyruvate + reduced acceptor
-
-
-
?
DL-malate + acceptor
about 3% activity of glycolate
348285
Escherichia coli
2-oxosuccinate + reduced acceptor
-
-
-
?
glycolate + acceptor
artificial acceptor 2,6-dichlorophenolindophenol is reduced via phenazine methosulfate, cytochrome c can replace 2,6-dichlorophenolindophenol
348285
Escherichia coli
glyoxylate + reduced acceptor
-
348285
Escherichia coli
?
glycolate + acceptor
the bacterial enzyme catalyzes phenazine methosulfate dependent reduction of 2,6-dichlorophenolindophenol or cytochrome c
348285
Escherichia coli
glyocylate + reduced acceptor
-
-
-
?
glyoxylate + acceptor
about 6% activity of glycolate
348285
Escherichia coli
oxalate + reduced acceptor
-
-
-
?
phosphoglycolate + acceptor
about 9% activity of glycolate
348285
Escherichia coli
? + reduced acceptor
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
8.8
-
Escherichia coli
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7.3
9
about half-maximal activity at pH 7.3 and 9.0
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
2,6-dichlorophenolindophenol
in vitro requirement, terminal acceptor
Escherichia coli
cytochrome c
can replace dichlorophenolindophenol as acceptor
Escherichia coli
additional information
FAD, FMN, NAD+, NADP+, oxidized glutathione, KNO3, ferricyanide, FeCl3, cytochrome c do not stimulate electron transfer from glycolate to dichlorophenolindophenol
Escherichia coli
phenazine methosulfate
transfers electrons from the substrate preferentially to 2,6-dichlorophenolindophenol
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
2,6-dichlorophenolindophenol
in vitro requirement, terminal acceptor
Escherichia coli
cytochrome c
can replace dichlorophenolindophenol as acceptor
Escherichia coli
additional information
FAD, FMN, NAD+, NADP+, oxidized glutathione, KNO3, ferricyanide, FeCl3, cytochrome c do not stimulate electron transfer from glycolate to dichlorophenolindophenol
Escherichia coli
phenazine methosulfate
transfers electrons from the substrate preferentially to 2,6-dichlorophenolindophenol
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
CuSO4
-
Escherichia coli
cytochrome c
inhibits rate of phenazine methosulfate stimulated dichlorophenolindophenol reduction
Escherichia coli
HgCl2
complete
Escherichia coli
K3[Fe(CN)6]
complete inhibition
Escherichia coli
KCN
-
Escherichia coli
additional information
high ionic strength; overview over inhibitors at different concentrations
Escherichia coli
PCMB
-
Escherichia coli
ZnCl2
-
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
glycolate
-
Escherichia coli
0.7
-
D(-)-lactate
-
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Escherichia coli
5737
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
glycolate + acceptor
Escherichia coli
the bacterial enzyme catalyzes phenazine methosulfate dependent reduction of 2,6-dichlorophenolindophenol or cytochrome c
glyocylate + reduced acceptor
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
partially, from cells grown on glycolate
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.14
-
glyoxylate formation in the presence of phenazine methosulfate
Escherichia coli
0.15
-
crude extract
Escherichia coli
3.1
-
partially purified protein
Escherichia coli
Storage Stability (protein specific)
Storage Stability
Organism
2°C, half-life of 10 days, FMN or FAD do not restore activity
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-lactate + acceptor
best substrate
348285
Escherichia coli
pyruvate + reduced acceptor
-
-
-
?
(R)-lactate + acceptor
artificial acceptor 2,6-dichlorophenolindophenol is reduced via phenazine methosulfate, cytochrome c can replace 2,6-dichlorophenolindophenol
348285
Escherichia coli
pyruvate + reduced acceptor
-
-
-
?
(S)-lactate + acceptor
about 16% activity of glycolate
348285
Escherichia coli
pyruvate + reduced acceptor
-
-
-
?
DL-malate + acceptor
about 3% activity of glycolate
348285
Escherichia coli
2-oxosuccinate + reduced acceptor
-
-
-
?
glycolate + acceptor
artificial acceptor 2,6-dichlorophenolindophenol is reduced via phenazine methosulfate, cytochrome c can replace 2,6-dichlorophenolindophenol
348285
Escherichia coli
glyoxylate + reduced acceptor
-
348285
Escherichia coli
?
glycolate + acceptor
the bacterial enzyme catalyzes phenazine methosulfate dependent reduction of 2,6-dichlorophenolindophenol or cytochrome c
348285
Escherichia coli
glyocylate + reduced acceptor
-
-
-
?
glyoxylate + acceptor
about 6% activity of glycolate
348285
Escherichia coli
oxalate + reduced acceptor
-
-
-
?
phosphoglycolate + acceptor
about 9% activity of glycolate
348285
Escherichia coli
? + reduced acceptor
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
8.8
-
Escherichia coli
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7.3
9
about half-maximal activity at pH 7.3 and 9.0
Escherichia coli
Other publictions for EC 1.1.99.14
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)
741130
Ahmad
-
Improvement of biomass accumul ...
Synechocystis sp.
Plant Biotechnol. Rep.
10
269-276
2016
-
-
1
-
-
-
-
-
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1
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1
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1
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1
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1
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-
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-
-
-
-
740208
Dalal
A photorespiratory bypass incr ...
Camelina sativa
Biotechnol. Biofuels
8
175
2015
-
-
1
-
-
-
-
-
1
-
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1
-
7
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1
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1
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741129
Noelke
The expression of a recombinan ...
Escherichia coli
Plant Biotechnol. J.
12
734-742
2014
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1
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1
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2
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1
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4
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2
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1
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1
1
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741190
Aboelmy
Enzymatic characterization of ...
Chlamydomonas reinhardtii
Plant Physiol. Biochem.
79
25-30
2014
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1
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3
2
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5
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7
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1
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1
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7
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1
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3
1
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2
2
725738
Isobe
-
Characterization and applicati ...
Trichoderma harzianum, Trichoderma harzianum AIU 353
J. Mol. Catal. B
83
94-99
2012
-
-
-
-
-
-
17
4
-
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5
2
-
2
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-
1
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-
2
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14
1
1
-
1
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1
-
1
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1
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-
-
-
-
-
-
17
-
4
-
-
5
2
-
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1
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2
-
14
1
1
-
1
-
1
-
1
1
-
-
-
-
-
-
700960
Eisenhut
The photorespiratory glycolate ...
Synechocystis sp. PCC 6803
Proc. Natl. Acad. Sci. USA
105
17199-17204
2008
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-
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6
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688079
Niessen
Mitochondrial glycolate oxidat ...
Arabidopsis thaliana
J. Exp. Bot.
58
2709-2715
2007
-
-
-
-
-
-
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1
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4
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3
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676615
Eisenhut
The plant-like C2 glycolate cy ...
Synechocystis sp.
Plant Physiol.
142
333-342
2006
-
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1
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1
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1
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5
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1
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1
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2
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1
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1
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1
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1
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1
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2
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1
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656411
Bari
A glycolate dehydrogenase in t ...
Arabidopsis thaliana
J. Exp. Bot.
55
623-630
2004
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1
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2
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1
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5
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2
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348290
Sallal
-
Effects of crude oil and hydro ...
Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 1405-1
Microbios
90
33-43
1997
1
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2
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2
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348289
Stabenau
-
Localization of glycolate dehy ...
Dunaliella primolecta, Dunaliella primolecta 183.80, Dunaliella salina
Planta
191
362-364
1993
-
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2
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3
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348287
Sallal
Localization of glycollate deh ...
Dunaliella salina
Planta
171
429-432
1987
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2
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1
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348288
Yokota
-
The mechanism of induction of ...
Euglena gracilis, Euglena gracilis Z
Agric. Biol. Chem.
51
665-670
1987
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2
1
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2
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21
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4
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1
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4
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348286
Paul
Photorespiration in diatoms. T ...
Thalassiosira pseudonana
Arch. Microbiol.
101
115-120
1974
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3
3
1
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348285
Lord
Glycolate oxidoreductase in Es ...
Escherichia coli
Biochim. Biophys. Acta
267
227-237
1971
-
-
-
-
-
-
8
2
1
-
-
1
-
2
-
-
1
-
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3
1
8
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1
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1
1
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4
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4
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8
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2
1
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1
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1
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3
1
8
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1
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1
1
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