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Literature summary extracted from

  • Tani, Y.; Morita, H.; Nishise, H.; Ogata, K.
    Separation and characterization of glycolaldehyde dehydrogenase isozymes in Escherichia coli B (1978), Agric. Biol. Chem., 42, 63-68.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.21 Al3+ 1 mM, isozyme A, 26% inhibition Escherichia coli
1.2.1.21 As3+ 1 mM, isozyme A, 42% inhibition, isozyme B, 11% inhibition, isozyme C, 55% inhibition, complete inhibition of isozyme A from pyridoxine auxotroph mutant strain WG3 Escherichia coli
1.2.1.21 Ca2+ 1 mM, isozyme A, 42% inhibition, isozyme B, 32% inhibition, complete inhibition of isozyme A from pyridoxine auxotroph mutant strain WG3 Escherichia coli
1.2.1.21 Co2+ 1 mM, isozyme A, 71% inhibition, isozyme B, 51% inhibition, complete inhibition of isozyme A from pyridoxine auxotroph mutant strain WG3 Escherichia coli
1.2.1.21 Fe2+ 1 mM, isozyme A, 18% inhibition Escherichia coli
1.2.1.21 HgCl2 1 mM, complete inhibition of isozymes A, B, and C Escherichia coli
1.2.1.21 KCN isozymes A and C Escherichia coli
1.2.1.21 Mg2+ 1 mM, isozyme A, 33% inhibition, isozyme B, 54% inhibition, complete inhibition of isozyme A from pyridoxine auxotroph mutant strain WG3 Escherichia coli
1.2.1.21 Mn2+ 1 mM, isozyme A, 20% inhibition, isozyme C, 44% inhibition Escherichia coli
1.2.1.21 monoiodoacetate 1 mM, isozymes A, 83% inhibition, isozyme C, 100% inhibition Escherichia coli
1.2.1.21 MoO22- 1 mM, complete inhibition of isozyme A from pyridoxine auxotroph mutant strain WG3 Escherichia coli
1.2.1.21 Zn2+ 1 mM, isozyme A, 30% inhibition Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.21 68000
-
isozyme B, gel filtration Escherichia coli
1.2.1.21 225000
-
isozyme A, gel filtration Escherichia coli
1.2.1.21 345000
-
isozyme C, gel filtration Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.21 Escherichia coli
-
-
-
1.2.1.21 Escherichia coli B WG1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.21 partial: isozymes A, B and C Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.21 2.7
-
isozyme B Escherichia coli
1.2.1.21 2.75
-
isozyme C Escherichia coli
1.2.1.21 3.66
-
isozyme A Escherichia coli
1.2.1.21 6.38
-
isozyme A from pyridoxine auxotroph strain WG3 Escherichia coli

Storage Stability

EC Number Storage Stability Organism
1.2.1.21 -20°C Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.21 acetaldehyde + NAD+ + H2O reverse reaction, isozyme A, 188% of activity with glycolate, isozyme B, 112%, isozyme C, 74% Escherichia coli acetate + NADH + H+
-
r
1.2.1.21 acetaldehyde + NAD+ + H2O reverse reaction, isozyme A, 188% of activity with glycolate, isozyme B, 112%, isozyme C, 74% Escherichia coli B WG1 acetate + NADH + H+
-
r
1.2.1.21 benzaldehyde + NAD+ + H2O isozyme A, 195% of activity with glycolate in reverse reaction Escherichia coli benzoate + NADH + H+
-
?
1.2.1.21 benzaldehyde + NAD+ + H2O isozyme A, 195% of activity with glycolate in reverse reaction Escherichia coli B WG1 benzoate + NADH + H+
-
?
1.2.1.21 betaine + NADH isozyme A 139% of activity with glycolate, isozyme B, 76% Escherichia coli betaine aldehyde + NAD+ + H2O glucono-delta-lactone is not used as substrate ?
1.2.1.21 formate + NADH isozyme A, 163% of activity with glycolate Escherichia coli methanal + NAD+
-
?
1.2.1.21 glycolaldehyde + NAD+ + H2O
-
Escherichia coli glycolate + NADH
-
r
1.2.1.21 glycolaldehyde + NAD+ + H2O
-
Escherichia coli B WG1 glycolate + NADH
-
r
1.2.1.21 glyoxylate + NADH isozyme A, 417% of activity with glycolate, isozyme B 714%, isozyme C 150% Escherichia coli glyoxal + NAD+
-
?
1.2.1.21 malonate + NADH isozyme A, 83% of activity with glycolate Escherichia coli malonic semialdehyde + NAD+ + H2O
-
?
1.2.1.21 oxalate + NADH isozyme A, 167% of activity with glycolate, isozyme B, 71% Escherichia coli glyoxylate + NAD+
-
?
1.2.1.21 oxalate + NADH isozyme A, 167% of activity with glycolate, isozyme B, 71% Escherichia coli B WG1 glyoxylate + NAD+
-
?
1.2.1.21 succinate + NADH isozyme A, 146% of activity with glycolate, isozyme B 6% Escherichia coli succinic semialdehyde + NAD+ + H2O
-
?
1.2.1.21 succinate + NADH isozyme A, 146% of activity with glycolate, isozyme B 6% Escherichia coli B WG1 succinic semialdehyde + NAD+ + H2O
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.21 20
-
isozyme A Escherichia coli
1.2.1.21 30
-
isozyme A from strain WG3 Escherichia coli
1.2.1.21 45
-
isozymes B and C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.21 5
-
glycolate reduction, isozyme A, B Escherichia coli
1.2.1.21 5.4
-
isozyme A, glycolaldehyde oxidation Escherichia coli
1.2.1.21 6
-
glycolate reduction, isozyme C Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.21 NADP+
-
Escherichia coli