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Information on EC 3.5.1.29 - 2-(acetamidomethylene)succinate hydrolase
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3.5.1.29 2-(acetamidomethylene)succinate hydrolaseIUBMB Comments
Involved in the degradation of pyridoxin in Pseudomonas.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
e-2ams hydrolase, mlr6787, 2-(acetamidomethylene)succinate hydrolase, aams amidohydrolase, compound a hydrolase, alpha-(n-acetylaminomethylene)succinic acid hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAMS amidohydrolase
AAMSAH
alpha-(N-acetylaminomethylene)succinic acid amidohydrolase
alpha-(N-acetylaminomethylene)succinic acid hydrolase
-
-
-
-
E-2AMS hydrolase
alpha-(N-acetylaminomethylene)succinic acid amidohydrolase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-(acetamidomethylene)succinate + 2 H2O = acetate + succinate semialdehyde + NH3 + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Deamination
-
-
-
-
decarboxylation
-
-
-
-
hydrolysis of peptide bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
2-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating)
Involved in the degradation of pyridoxin in Pseudomonas.
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CAS REGISTRY NUMBER
COMMENTARY
37289-09-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2-acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
-
?
(E)-2-(acetamidomethylene)succinate + H2O
succinic semialdehyde + acetate + CO2 + NH3
-
-
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
molecular docking of two substrate isomers E- and Z-2-(acetamidomethylene)succinate to the hydrolase, molecular dynamics simulations and calculations of binding free energies, overview
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
same products as formed by acid hydrolysis
ir
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
same products as formed by acid hydrolysis
ir
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
step in the pathway of enzymatic degradation of vitamin B6
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
same products as formed by acid hydrolysis
ir
additional information
?
-
-
the enzyme is involved in the catabolism of pyridoxal 5'-phosphate (vitamin B6)
-
-
?
additional information
?
-
-
the enzyme is involved in the catabolism of pyridoxal 5'-phosphate (vitamin B6)
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2-acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
-
?
(E)-2-(acetamidomethylene)succinate + H2O
succinic semialdehyde + acetate + CO2 + NH3
-
-
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
step in the pathway of enzymatic degradation of vitamin B6
-
-
?
2-(acetamidomethylene)succinate + 2 H2O
acetate + succinate semialdehyde + NH3 + CO2
-
-
-
-
?
additional information
?
-
-
the enzyme is involved in the catabolism of pyridoxal 5'-phosphate (vitamin B6)
-
-
?
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
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
Itaconate
-
competitively inhibited by di-and tricarboxylic acids, itaconic acid being most effective, monocarboxylic acids do not inhibit
Itaconate
-
competitively inhibited by di-and tricarboxylic acids, itaconic acid being most effective, monocarboxylic acids do not inhibit
SO32-
-
inhibitory effect increases rapidly with time to a constant level, not competitve with substrate
SO32-
-
inhibitory effect increases rapidly with time to a constant level, not competitve with substrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
-
pH 6 potassium phosphate buffer, pH 7 in diphosphate buffer, pH 7-7.5 in Tris buffer
6.5 - 7.5
-
pH 6.5 in 50 mM sodium phosphate, MES and HEPES buffers, pH 7.5 in Tris buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
metabolism
AAMS amidohydrolase is involved in a degradation pathway of vitamin B6 (final step in degradation pathway I of vitamin B6)
metabolism
-
the enzyme catalyzes the final reaction in the degradation of vitamin B6
metabolism
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
Show AA Sequence and Transmembrane Helices (168 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
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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
-
sitting drop vapor diffusion method, using 100 mM Tris-HCl buffer (final pH 8.5), 20% (w/v) PEG 8000, 275 mM MgCl2
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S230A
-
inactive, the active site mutant cannot be assayed because this protein precipitates in the assay buffer
S230N
-
inactive, the active site mutant cannot be assayed because this protein precipitates in the assay buffer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
-
at pH 8 and 70°C stable for 1 min, loses activity completely in 1 min at 90°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, butyl-Toyopearl column chromatography, hydoxylapatite column chromatography, and Sephadex G25 gel filtration
-
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
brenda
Nyns, E.J.; Zach, D.; Snell, E.E.
The bacterial oxidation of vitamin B6
J. Biol. Chem.
244
2601-2605
1969
Pseudomonas sp.
brenda
Mukherjee, T.; Hilmey, D.G.; Begley, T.P.
PLP Catabolism: Identification of the 2-(acetamidomethylene)succinate hydrolase gene in Mesorhizobium loti MAFF303099
Biochemistry
47
6233-6241
2008
Mesorhizobium loti, Mesorhizobium loti MAFF303099
brenda
Yuan, B.; Yokochi, N.; Yoshikane, Y.; Ohnishi, K.; Ge, F.; Yagi, T.
Gene identification and characterization of the pyridoxine degradative enzyme alpha-(N-acetylaminomethylene)succinic acid amidohydrolase from Mesorhizobium loti MAFF303099
J. Nutr. Sci. Vitaminol.
54
185-190
2008
Mesorhizobium loti, Mesorhizobium loti MAFF303099
brenda
Kobayashi, J.; Yoshida, H.; Chu, H.N.; Yoshikane, Y.; Kamitori, S.; Yagi, T.
Crystallization and preliminary X-ray analysis of AAMS amidohydrolase, the final enzyme in degradation pathway I of pyridoxine
Acta Crystallogr. Sect. F
65
829-831
2009
Mesorhizobium japonicum MAFF 303099 (Q988D4), Mesorhizobium japonicum MAFF 303099
brenda
McCulloch, K.M.; Mukherjee, T.; Begley, T.P.; Ealick, S.E.
Structure determination and characterization of the vitamin B6 degradative enzyme (E)-2-(acetamidomethylene)succinate hydrolase
Biochemistry
49
1226-1235
2010
Mesorhizobium japonicum MAFF 303099
brenda
Nagase, T.; Mugo, A.N.; Chu, H.N.; Yoshikane, Y.; Ohnishi, K.; Yagi, T.
The mll6786 gene encodes a repressor protein controlling the degradation pathway for vitamin B6 in Mesorhizobium loti
FEMS Microbiol. Lett.
329
116-122
2012
Mesorhizobium loti (Q988D4), Mesorhizobium loti
brenda
Zhang, J.L.; Zheng, Q.C.; Li, Z.Q.; Zhang, H.X.
How does (E)-2-(acetamidomethylene)succinate bind to its hydrolase? From the binding process to the final result
PLoS ONE
8
e53811
2013
Mesorhizobium loti (Q988D4)
brenda
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