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Information on EC 3.5.1.66 - 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase for references in articles please use BRENDA:EC3.5.1.66
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EC Tree
IUBMB Comments Involved in the degradation of pyridoxin by Pseudomonas and Arthrobacter.
The enzyme appears in viruses and cellular organisms
Synonyms
alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid hydrolase, compound B hydrolase,
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alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid hydrolase
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compound B hydrolase
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + 2 H2O = acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2
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hydrolysis of linear amides
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deaminating, decarboxylating
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating)
Involved in the degradation of pyridoxin by Pseudomonas and Arthrobacter.
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2
3-(acetamidomethylene)succinate + H2O
acetate + 4-oxobutanoate + NH3 + CO2
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compound A, alpha-(N-acetylaminomethylene)succinic acid: poor substrate
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additional information
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
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compound B, alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
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involved in pyridoxine degradation
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
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compound B, alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
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compound B, alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2
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compound B, alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2
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compound B, alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2
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compound B, alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid
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additional information
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high substrate specificity
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additional information
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enzyme highly specific, inducible amidohydrolase
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additional information
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enzyme of vitamin B6 degradation, utilizing pyridoxine as sole source of carbon and nitrogen
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additional information
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enzyme of vitamin B6 degradation, utilizing pyridoxine as sole source of carbon and nitrogen
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additional information
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enzyme of vitamin B6 degradation, utilizing pyridoxine as sole source of carbon and nitrogen
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
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additional information
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
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compound B, alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
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involved in pyridoxine degradation
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
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compound B, alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid
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2-(hydroxymethyl)-3-(acetamidomethylene)succinate + H2O
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compound B, alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid
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additional information
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enzyme of vitamin B6 degradation, utilizing pyridoxine as sole source of carbon and nitrogen
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additional information
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enzyme of vitamin B6 degradation, utilizing pyridoxine as sole source of carbon and nitrogen
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additional information
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enzyme of vitamin B6 degradation, utilizing pyridoxine as sole source of carbon and nitrogen
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additional information
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some inorganic cations activate
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Dicarboxylic acids
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competitive
diphosphate
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competitive
Hg2+
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0.01 mM, 15 min, 82% activity remains
Itaconic acid
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competitive, most effective inhibitor, Ki: 0.74 mM
malonate
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competitive, Ki: 20 mM
sulfite
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noncompetitive, inhibition by a time-dependent mechanism, addition of succinic semialdehyde protects against sulfite inhibition
Tricarboxylic acids
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competitive
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Zn2+
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1 mM: 40% inhibition
additional information
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no inhibition by: organic protein reagents, 0.1 mM, 15 min, p-chloromercuribenzoate, 1.0 mM Ni2+, 1.0 mM Co2+, 1.0 mM Mn2+, 1.0 mM Mg2+, 1.0 mM Ca2+, 1.0 mM Cu2+, 1.0 mM Cs+, 1.0 mM Li+, SO42-, NO3-, Cl-, 10 mM dithiothreitol, 100 mM monocarboxylic acids
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0.025 - 0.56
2-(Hydroxymethyl)-3-(acetamidomethylene)succinate
0.68
3-(acetamidomethylene)succinate
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compound A, 25°C, pH 7.0
additional information
additional information
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kinetic data
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0.025
2-(Hydroxymethyl)-3-(acetamidomethylene)succinate
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compound B, 25°C, Tris-HCl, pH 7.0
0.123
2-(Hydroxymethyl)-3-(acetamidomethylene)succinate
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compound B, 2-(N-morpholino)ethane-sulfonic acid, pH 6.0
0.25
2-(Hydroxymethyl)-3-(acetamidomethylene)succinate
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compound B, Tris-HCl, pH 8.0
0.56
2-(Hydroxymethyl)-3-(acetamidomethylene)succinate
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compound B, 2-(N-morpholino)ethane-sulfonic acid, pH 6.5
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2.3
2-(Hydroxymethyl)-3-(acetamidomethylene)succinate
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turnover no./subunit, 25°C
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0.74
Itaconic acid
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competitive, most effective inhibitor
20
malonate
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competitive
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additional information
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additional information
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pI: 4.2, effect of buffer on pH optimum
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Cr-7
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brenda
IA
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brenda
IA
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brenda
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205000
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Cr-7, gel filtration
36600
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Cr-7, probably six identical subunits, 6 * 36600, SDS-PAGE
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multimer
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Cr-7, probably six identical subunits, 6 * 36600, SDS-PAGE
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4 - 5
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rapid loss of activity
172028
6 - 10
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stable at room temperature
172028
8
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70°C, 1 min, stable at
172028
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100
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1 min, 65% activity retained
70
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pH 8.0, 1 min, stable at
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Cr-7, -20°C, 0.1 M Tris-HCl, pH 7.0, stable for several months
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Huynh, M.S.; Snell, E.E.
Enzymes of vitamin B6 degradation. Purification and properties of two N-acetylamidohydrolases
J. Biol. Chem.
260
2379-2383
1985
Arthrobacter sp., Pseudomonas sp., Pseudomonas sp. IA
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3.5.1.66 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase
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