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Literature summary for 1.1.99.14 extracted from

  • Lord, J.M.
    Glycolate oxidoreductase in Escherichia coli (1971), Biochim. Biophys. Acta, 267, 227-237.
    View publication on PubMed

Inhibitors

Inhibitors Comment 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 Comment Organism Structure
0.04
-
glycolate
-
Escherichia coli
0.7
-
D(-)-lactate
-
Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Escherichia coli 5737
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycolate + acceptor Escherichia coli the bacterial enzyme catalyzes phenazine methosulfate dependent reduction of 2,6-dichlorophenolindophenol or cytochrome c glyocylate + reduced acceptor
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) 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] Comment 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-lactate + acceptor best substrate 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 Escherichia coli pyruvate + reduced acceptor
-
?
(S)-lactate + acceptor about 16% activity of glycolate Escherichia coli pyruvate + reduced acceptor
-
?
DL-malate + acceptor about 3% activity of glycolate 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 Escherichia coli glyoxylate + reduced acceptor
-
?
glycolate + acceptor the bacterial enzyme catalyzes phenazine methosulfate dependent reduction of 2,6-dichlorophenolindophenol or cytochrome c Escherichia coli glyocylate + reduced acceptor
-
?
glyoxylate + acceptor about 6% activity of glycolate Escherichia coli oxalate + reduced acceptor
-
?
phosphoglycolate + acceptor about 9% activity of glycolate Escherichia coli ? + reduced acceptor
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 8.8
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7.3 9 about half-maximal activity at pH 7.3 and 9.0 Escherichia coli

Cofactor

Cofactor Comment 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