Information on EC 3.5.1.29 - 2-(acetamidomethylene)succinate hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.29
-
RECOMMENDED NAME
GeneOntology No.
2-(acetamidomethylene)succinate hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-(acetamidomethylene)succinate + 2 H2O = acetate + succinate semialdehyde + NH3 + CO2
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
-
-
-
-
decarboxylation
-
-
-
-
hydrolysis of peptide bond
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
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-
vitamin B6 degradation
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-
Vitamin B6 metabolism
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SYSTEMATIC NAME
IUBMB Comments
2-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating)
Involved in the degradation of pyridoxin in Pseudomonas.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-09-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Cr-7
-
-
Manually annotated by BRENDA team
Cr-7
-
-
Manually annotated by BRENDA team
MA-1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
-
binding of (E)-2-(acetamidomethylene)succinate to the enzyme is crucial for biological function of the enzyme and the last step reaction of vitamin B6 biological degradation
additional information
-
molecular docking of the two substrate isomers E- and Z-2-(acetamidomethylene)succinate to the hydrolase, molecular dynamics simulations and calculations of binding free energies, usage of X-ray crystal structure of E-2AMS hydrolase, PDB ID 3KXP, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2-acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
show the reaction diagram
-
-
-
?
(E)-2-(acetamidomethylene)succinate + H2O
succinic semialdehyde + acetate + CO2 + NH3
show the reaction diagram
-
-
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
show the reaction diagram
additional information
?
-
-
the enzyme is involved in the catabolism of pyridoxal 5'-phosphate (vitamin B6)
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-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2-acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
show the reaction diagram
Q988D4
-
-
-
?
(E)-2-(acetamidomethylene)succinate + H2O
succinic semialdehyde + acetate + CO2 + NH3
show the reaction diagram
-
-
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
show the reaction diagram
additional information
?
-
-
the enzyme is involved in the catabolism of pyridoxal 5'-phosphate (vitamin B6)
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-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
not activated by Zn2+, Fe2+, or Ni2+ (1 mM each)
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-hydroxyglutarate
-
competitive inhibition
alpha-ketoglutarate
citrate
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competitive inhibition
diphosphate
fumarate
glutamate
-
competitive inhibition
Glutarate
-
competitive inhibition
Itaconate
malate
-
competitive inhibition
Maleate
-
competitive inhibition
malonate
-
competitive inhibition
N-acetyl-DL-aspartate
oxaloacetate
phosphate
SO32-
succinate
additional information
-
not inhibited by Zn2+, Fe2+, or Ni2+ (1 mM each), the enzyme is not affected when incubated for 30 min at 30°C in buffer containing 100 mM EDTA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.058
(N-acetylaminomethylene)succinic acid
0.143
2-(Acetamidomethylene)succinate
-
-
0.0537
alpha-(N-acetylaminomethylene)succinic acid
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at 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.67
(N-acetylaminomethylene)succinic acid
Pseudomonas sp.
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-
0.6
2-(Acetamidomethylene)succinate
Mesorhizobium loti
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-
307.3
alpha-(N-acetylaminomethylene)succinic acid
Mesorhizobium loti
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at 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.468
-
crude extract, at 25°C
1.89
-
purified enzyme, at 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
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pH 6 potassium phosphate buffer, pH 7 in diphosphate buffer, pH 7-7.5 in Tris buffer
6.5 - 7.5
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pH 6.5 in 50 mM sodium phosphate, MES and HEPES buffers, pH 7.5 in Tris buffer
7
-
in 100 mM GTA buffer; in sodium diphosphate buffer
7.5
-
in potassium or sodium phosphate buffer
8
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in Tris-HCl
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
most efficient between pH 6.0 and 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
in 0.1 M potassium phosphate buffer (pH 7.0)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29896
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2 * 29896, calculated from amino acid sequence
32500
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gel filtration
64000
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native enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 29896, calculated from amino acid sequence; 2 * 34000, SDS-PAGE
homodimer
2 * 34000, SDS-PAGE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 9% (w/v) PEG 8000, 200 mM MgCl2, and 100 mM Tris at pH 7.8
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sitting drop vapor diffusion method, using 100 mM Tris-HCl buffer (final pH 8.5), 20% (w/v) PEG 8000, 275 mM MgCl2
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
loses activity rapidly between 4.0 and 5.0
172028
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
the enzyme is stable at 50°C for 10 min, the half-lives of the enzyme are 193.6, 77.3, 21.6, and 13.6 min at 50, 55, 58, and 60°C, respectively
70 - 90
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at pH 8 and 70°C stable for 1 min, loses activity completely in 1 min at 90°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable at room temperature between pH 6 and 10
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, butyl-Toyopearl column chromatography, hydoxylapatite column chromatography, and Sephadex G25 gel filtration
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ammonium sulfate precipitation, butyl-Toyopearl column chromatography, hydroxylapatite column chromatography, and 5-diol-300II gel filtration
Ni-NTA column chromatography and Superdex 75 gel filtration
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purified 22-fold
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834(DE3) cells
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expressed in Escherichia coli BL21 (DE3) and JM109 cells
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expressed in Escherichia coli BL21(DE3) cells
overexpressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S230A
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inactive, the active site mutant cannot be assayed because this protein precipitates in the assay buffer
S230N
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inactive, the active site mutant cannot be assayed because this protein precipitates in the assay buffer